##gff-version 3 Q99497 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25944712;Dbxref=PMID:25944712 Q99497 UniProtKB Active site 106 106 . . . Note=Nucleophile;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:20304780,ECO:0000305|PubMed:25416785;Dbxref=PMID:20304780,PMID:25416785 Q99497 UniProtKB Active site 126 126 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20304780;Dbxref=PMID:20304780 Q99497 UniProtKB Site 149 150 . . . Note=Cleavage%3B by CASP6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LX0 Q99497 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25944712;Dbxref=PMID:25944712 Q99497 UniProtKB Modified residue 67 67 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:15592455;Dbxref=PMID:15592455 Q99497 UniProtKB Modified residue 106 106 . . . Note=Cysteine sulfinic acid (-SO2H)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12939276;Dbxref=PMID:12939276 Q99497 UniProtKB Modified residue 148 148 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LX0 Q99497 UniProtKB Modified residue 182 182 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LX0 Q99497 UniProtKB Lipidation 46 46 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23847046;Dbxref=PMID:23847046 Q99497 UniProtKB Lipidation 53 53 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23847046;Dbxref=PMID:23847046 Q99497 UniProtKB Lipidation 106 106 . . . Note=S-palmitoyl cysteine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23847046;Dbxref=PMID:23847046 Q99497 UniProtKB Cross-link 130 130 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15976810;Dbxref=PMID:15976810 Q99497 UniProtKB Natural variant 10 10 . . . ID=VAR_084339;Note=In PARK7%3B uncertain significance. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18785233;Dbxref=PMID:18785233 Q99497 UniProtKB Natural variant 26 26 . . . ID=VAR_020492;Note=In PARK7%3B does not affect protein stability and degradation%3B does not interfere with homodimerization%3B decreased detoxification activity on methylglyocal-adducted CoA. M->I;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12953260,ECO:0000269|PubMed:14713311,ECO:0000269|PubMed:28993701;Dbxref=dbSNP:rs74315351,PMID:12953260,PMID:14713311,PMID:28993701 Q99497 UniProtKB Natural variant 39 39 . . . ID=VAR_072589;Note=Found in early-onset Parkinson disease with digenic inheritance%3B likely pathogenic%3B the patient also carries PINK1 mutation L-399%3B no effect on detoxification activity on methylglyocal-adducted CoA. A->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16632486,ECO:0000269|PubMed:28993701;Dbxref=dbSNP:rs137853051,PMID:16632486,PMID:28993701 Q99497 UniProtKB Natural variant 45 45 . . . ID=VAR_083277;Note=In PARK7. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26972524;Dbxref=PMID:26972524 Q99497 UniProtKB Natural variant 64 64 . . . ID=VAR_020493;Note=In PARK7%3B no apparent effect on protein stability%3B impaired mitochondrial morphology%3B no effect on detoxification activity on methylglyocal-adducted CoA. E->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14607841,ECO:0000269|PubMed:15365989,ECO:0000269|PubMed:20186336,ECO:0000269|PubMed:28993701;Dbxref=dbSNP:rs74315353,PMID:14607841,PMID:15365989,PMID:20186336,PMID:28993701 Q99497 UniProtKB Natural variant 98 98 . . . ID=VAR_020494;Note=R->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12953260,ECO:0000269|PubMed:14705128,ECO:0000269|PubMed:14872018,ECO:0000269|PubMed:15254937;Dbxref=dbSNP:rs71653619,PMID:12953260,PMID:14705128,PMID:14872018,PMID:15254937 Q99497 UniProtKB Natural variant 104 104 . . . ID=VAR_020495;Note=In PARK7%3B loss of protection against metal cytotoxicity%3B decreased detoxification activity on methylglyocal-adducted CoA. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15254937,ECO:0000269|PubMed:23792957,ECO:0000269|PubMed:28993701;Dbxref=dbSNP:rs774005786,PMID:15254937,PMID:23792957,PMID:28993701 Q99497 UniProtKB Natural variant 149 149 . . . ID=VAR_020496;Note=In PARK7%3B loss of protection against metal cytotoxicity%3B decreased detoxification activity on methylglyocal-adducted CoA. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12953260,ECO:0000269|PubMed:23792957,ECO:0000269|PubMed:28993701;Dbxref=dbSNP:rs74315352,PMID:12953260,PMID:23792957,PMID:28993701 Q99497 UniProtKB Natural variant 150 150 . . . ID=VAR_020497;Note=G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.10;Dbxref=dbSNP:rs368420490 Q99497 UniProtKB Natural variant 163 163 . . . ID=VAR_034801;Note=In PARK7%3B uncertain significance%3B no effect on detoxification activity on methylglyocal-adducted CoA. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16240358,ECO:0000269|PubMed:28993701;Dbxref=dbSNP:rs74315354,PMID:16240358,PMID:28993701 Q99497 UniProtKB Natural variant 166 166 . . . ID=VAR_020498;Note=In PARK7%3B strongly decreases enzymatic activity%3B reduces protein stability and leads to increased degradation%3B ubiquitinated by PRKN leading to its recognition by HDAC6 and targeting to aggresome where is degraded%3B interferes with homodimerization%3B abolishes interaction with PIAS2%3B reduced localization in lipid rafts%3B almost abolished detoxification activity on methylglyocal-adducted CoA. L->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12446870,ECO:0000269|PubMed:12851414,ECO:0000269|PubMed:14607841,ECO:0000269|PubMed:14713311,ECO:0000269|PubMed:17846173,ECO:0000269|PubMed:19229105,ECO:0000269|PubMed:22523093,ECO:0000269|PubMed:23847046,ECO:0000269|PubMed:28993701;Dbxref=dbSNP:rs28938172,PMID:12446870,PMID:12851414,PMID:14607841,PMID:14713311,PMID:17846173,PMID:19229105,PMID:22523093,PMID:23847046,PMID:28993701 Q99497 UniProtKB Natural variant 171 171 . . . ID=VAR_020499;Note=A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15254937;Dbxref=dbSNP:rs777026628,PMID:15254937 Q99497 UniProtKB Mutagenesis 10 10 . . . Note=Abolishes detoxification activity on methylglyocal-adducted CoA. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28993701;Dbxref=PMID:28993701 Q99497 UniProtKB Mutagenesis 18 18 . . . Note=Strongly decreases enzymatic activity. Almost abolishes detoxification activity on methylglyocal-adducted CoA. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22523093,ECO:0000269|PubMed:28993701;Dbxref=PMID:22523093,PMID:28993701 Q99497 UniProtKB Mutagenesis 18 18 . . . Note=Strongly decreases enzymatic activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22523093;Dbxref=PMID:22523093 Q99497 UniProtKB Mutagenesis 18 18 . . . Note=Strongly decreases enzymatic activity. E->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22523093;Dbxref=PMID:22523093 Q99497 UniProtKB Mutagenesis 18 18 . . . Note=Strongly decreases enzymatic activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22523093;Dbxref=PMID:22523093 Q99497 UniProtKB Mutagenesis 46 46 . . . Note=Reduces protein stability. No effect on oxidation. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:18711745,ECO:0000269|PubMed:23847046;Dbxref=PMID:15181200,PMID:15502874,PMID:18711745,PMID:23847046 Q99497 UniProtKB Mutagenesis 46 46 . . . Note=Reduces protein stability. No effect on oxidation. Reduced localization in lipid rafts%3B when associated with A-106. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:18711745,ECO:0000269|PubMed:23847046;Dbxref=PMID:15181200,PMID:15502874,PMID:18711745,PMID:23847046 Q99497 UniProtKB Mutagenesis 46 46 . . . Note=No effect on mitochondrial translocation neither on deglycase activity. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:18711745,ECO:0000269|PubMed:23847046,ECO:0000269|PubMed:25416785;Dbxref=PMID:15181200,PMID:15502874,PMID:18711745,PMID:23847046,PMID:25416785 Q99497 UniProtKB Mutagenesis 51 51 . . . Note=Disrupts dimer formation and strongly reduces ability to eliminate hydrogen peroxide. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14749723;Dbxref=PMID:14749723 Q99497 UniProtKB Mutagenesis 53 53 . . . Note=Strongly reduces chaperone activity and ability to eliminate hydrogen peroxide. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14749723,ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:18711745;Dbxref=PMID:14749723,PMID:15181200,PMID:15502874,PMID:18711745 Q99497 UniProtKB Mutagenesis 53 53 . . . Note=No effect on mitochondrial translocation neither on deglycase activity. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14749723,ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:18711745,ECO:0000269|PubMed:25416785;Dbxref=PMID:14749723,PMID:15181200,PMID:15502874,PMID:18711745,PMID:25416785 Q99497 UniProtKB Mutagenesis 106 106 . . . Note=Abolishes enzymatic activity. Abolishes oxidation%2C association with mitochondria and protease activity. No effect on chaperone activity. Reduces binding to OTUD7B. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:16390825,ECO:0000269|PubMed:18711745,ECO:0000269|PubMed:20304780,ECO:0000269|PubMed:21097510,ECO:0000269|PubMed:22523093,ECO:0000269|PubMed:23847046;Dbxref=PMID:15181200,PMID:15502874,PMID:16390825,PMID:18711745,PMID:20304780,PMID:21097510,PMID:22523093,PMID:23847046 Q99497 UniProtKB Mutagenesis 106 106 . . . Note=Abolishes enzymatic activity. Abolishes oxidation%2C association with mitochondria and protease activity. No effect on chaperone activity. Reduces binding to OTUD7B. Removes the glycations and restores histone 3. Reduced localization in lipid rafts%3B when associated with A-46. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:16390825,ECO:0000269|PubMed:18711745,ECO:0000269|PubMed:20304780,ECO:0000269|PubMed:21097510,ECO:0000269|PubMed:22523093,ECO:0000269|PubMed:23847046,ECO:0000269|PubMed:30894531;Dbxref=PMID:15181200,PMID:15502874,PMID:16390825,PMID:18711745,PMID:20304780,PMID:21097510,PMID:22523093,PMID:23847046,PMID:30894531 Q99497 UniProtKB Mutagenesis 106 106 . . . Note=Abolishes oxidation and association with mitochondria. No effect on chaperone activity. C->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:16390825,ECO:0000269|PubMed:18711745,ECO:0000269|PubMed:20304780,ECO:0000269|PubMed:21097510,ECO:0000269|PubMed:23847046;Dbxref=PMID:15181200,PMID:15502874,PMID:16390825,PMID:18711745,PMID:20304780,PMID:21097510,PMID:23847046 Q99497 UniProtKB Mutagenesis 106 106 . . . Note=Loss of protein and nucleic acid deglycase activity. No effect on mitochondrial translocation. Reduced protease activity. No effect on protection against metal cytotoxicity. No effect on methylglyoxal-adducted glutathione or CoA. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15181200,ECO:0000269|PubMed:15502874,ECO:0000269|PubMed:16390825,ECO:0000269|PubMed:18711745,ECO:0000269|PubMed:20304780,ECO:0000269|PubMed:21097510,ECO:0000269|PubMed:23847046,ECO:0000269|PubMed:25416785,ECO:0000269|PubMed:28596309,ECO:0000269|PubMed:28993701;Dbxref=PMID:15181200,PMID:15502874,PMID:16390825,PMID:18711745,PMID:20304780,PMID:21097510,PMID:23847046,PMID:25416785,PMID:28596309,PMID:28993701 Q99497 UniProtKB Mutagenesis 126 126 . . . Note=Strongly decreases enzymatic activity. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20304780,ECO:0000269|PubMed:22523093;Dbxref=PMID:20304780,PMID:22523093 Q99497 UniProtKB Mutagenesis 130 130 . . . Note=Partially compensates for loss of stability%3B when associated with P-166. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12851414;Dbxref=PMID:12851414 Q99497 UniProtKB Mutagenesis 179 179 . . . Note=No effect on detoxification activity on methylglyocal-adducted CoA. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28993701;Dbxref=PMID:28993701 Q99497 UniProtKB Sequence conflict 119 119 . . . Note=F->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99497 UniProtKB Beta strand 5 10 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 16 28 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Beta strand 32 37 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Turn 38 41 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1PDW Q99497 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4N0M Q99497 UniProtKB Beta strand 51 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OR3 Q99497 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 58 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Beta strand 68 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 76 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 86 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Beta strand 101 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Turn 106 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 109 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 127 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 130 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Turn 134 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Beta strand 139 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Beta strand 145 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Beta strand 152 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 158 160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 161 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 175 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3 Q99497 UniProtKB Helix 183 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RK3