{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q99497","secondaryAccessions":["B2R4Z1","O14805","Q6DR95","Q7LFU2"],"uniProtkbId":"PARK7_HUMAN","entryAudit":{"firstPublicDate":"2004-12-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-07-05","entryVersion":233,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Parkinson disease protein 7"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28596309"}],"value":"Maillard deglycase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Oncogene DJ1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:16369"}],"value":"Parkinsonism-associated deglycase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein DJ-1"},"shortNames":[{"value":"DJ-1"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25416785"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28596309"}],"value":"Protein/nucleic acid deglycase DJ-1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}],"value":"3.1.2.-"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}],"value":"3.5.1.-"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}],"value":"3.5.1.124"}]}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:16369"}],"value":"PARK7"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q99LX0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11477070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12612053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12855764"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12939276"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14749723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15181200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15502874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15976810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16390825"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17015834"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18626009"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18711745"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19229105"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20186336"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20304780"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21097510"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22523093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23792957"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23847046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26995087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28013050"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28993701"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30150385"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30894531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9070310"}],"value":"Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease (PubMed:12796482, PubMed:17015834, PubMed:18711745, PubMed:19229105, PubMed:20304780, PubMed:25416785, PubMed:26995087, PubMed:28993701). It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:12612053, PubMed:14749723, PubMed:15502874, PubMed:17015834, PubMed:18711745, PubMed:21097510). Has been described as a protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals (PubMed:25416785, PubMed:28596309). But this function is rebuted by other works (PubMed:27903648, PubMed:31653696). As a protein deglycase, repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (PubMed:25416785, PubMed:26995087, PubMed:28013050). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair (PubMed:28596309). Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin (PubMed:30150385). Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels (PubMed:30150385, PubMed:30894531). Displays a very low glyoxalase activity that may reflect its deglycase activity (PubMed:22523093, PubMed:28993701, PubMed:31653696). Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:16632486, PubMed:19229105). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (PubMed:18626009). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] + H2O = lactate + L-arginyl-[protein] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:49548"},{"database":"Rhea","id":"RHEA-COMP:10532"},{"database":"Rhea","id":"RHEA-COMP:12428"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:29965"},{"database":"ChEBI","id":"CHEBI:131708"}],"ecNumber":"3.5.1.124","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] + H2O = lactate + L-lysyl-[protein] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:49552"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:12429"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:131709"}],"ecNumber":"3.5.1.124","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] + H2O = lactate + L-cysteinyl-[protein] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:49556"},{"database":"Rhea","id":"RHEA-COMP:10131"},{"database":"Rhea","id":"RHEA-COMP:12430"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:131710"}],"ecNumber":"3.5.1.124","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] + H2O = L-arginyl-[protein] + glycolate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57188"},{"database":"Rhea","id":"RHEA-COMP:10532"},{"database":"Rhea","id":"RHEA-COMP:14844"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:29965"},{"database":"ChEBI","id":"CHEBI:141553"}],"ecNumber":"3.5.1.124","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] + H2O = glycolate + L-lysyl-[protein] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57192"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:14845"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:141554"}],"ecNumber":"3.5.1.124","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] + H2O = glycolate + L-cysteinyl-[protein] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57196"},{"database":"Rhea","id":"RHEA-COMP:10131"},{"database":"Rhea","id":"RHEA-COMP:14846"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:141555"}],"ecNumber":"3.5.1.124","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-(1-hydroxy-2-oxopropyl)-dGTP + H2O = lactate + dGTP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57244"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:61429"},{"database":"ChEBI","id":"CHEBI:141569"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-(1-hydroxy-2-oxopropyl)-GTP + H2O = lactate + GTP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57256"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:141570"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-(1-hydroxy-2-oxopropyl)-GDP + H2O = lactate + GDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57260"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:58189"},{"database":"ChEBI","id":"CHEBI:141573"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-(1-hydroxy-2-oxopropyl)-GMP + H2O = lactate + GMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57268"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:58115"},{"database":"ChEBI","id":"CHEBI:141575"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-(1-hydroxy-2-oxoethyl)-dGTP + H2O = dGTP + glycolate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57248"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:61429"},{"database":"ChEBI","id":"CHEBI:141572"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-(1-hydroxy-2-oxoethyl)-GTP + H2O = glycolate + GTP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57252"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:141571"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-(1-hydroxy-2-oxoethyl)-GDP + H2O = glycolate + GDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57264"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:58189"},{"database":"ChEBI","id":"CHEBI:141574"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-(1-hydroxy-2-oxoethyl)-GMP + H2O = glycolate + GMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57304"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:58115"},{"database":"ChEBI","id":"CHEBI:141576"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + lactate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57288"},{"database":"Rhea","id":"RHEA-COMP:14855"},{"database":"Rhea","id":"RHEA-COMP:14858"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:74269"},{"database":"ChEBI","id":"CHEBI:141580"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + lactate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57300"},{"database":"Rhea","id":"RHEA-COMP:11367"},{"database":"Rhea","id":"RHEA-COMP:14856"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24996"},{"database":"ChEBI","id":"CHEBI:85445"},{"database":"ChEBI","id":"CHEBI:141578"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57292"},{"database":"Rhea","id":"RHEA-COMP:14855"},{"database":"Rhea","id":"RHEA-COMP:14859"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:74269"},{"database":"ChEBI","id":"CHEBI:141581"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28596309"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57296"},{"database":"Rhea","id":"RHEA-COMP:11367"},{"database":"Rhea","id":"RHEA-COMP:14857"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29805"},{"database":"ChEBI","id":"CHEBI:85445"},{"database":"ChEBI","id":"CHEBI:141579"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28596309"}]}},{"commentType":"COFACTOR","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28993701"}],"value":"Deglycase activity does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":173.4,"unit":"uM","substrate":"casein","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20304780"}]},{"constant":0.44,"unit":"mM","substrate":"glycated N-acetylarginine (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]},{"constant":0.35,"unit":"mM","substrate":"glycated N-acetyllysine (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]},{"constant":0.32,"unit":"mM","substrate":"glycated N-acetylcysteine (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31653696"}],"value":"kcat is 0.27 sec(-1) for the deglycation of glycated N-acetylarginine. kcat is 0.28 sec(-1) for the deglycation of glycated N-acetyllysine. kcat is 0.42 sec(-1) for the deglycation of glycated N-acetylcysteine. kcat is 0.02 sec(-1) for glyoxalase activity (PubMed:31653696)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q99LX0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11477070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12612053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12796482"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12851414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12855764"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16390825"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21097510"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31536960"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31653696"}],"value":"Homodimer (PubMed:12796482, PubMed:12851414, PubMed:12855764, PubMed:31653696). Binds EFCAB6/DJBP and PIAS2 (PubMed:11477070, PubMed:12612053, PubMed:12851414). Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR (PubMed:12612053). Interacts (via N-terminus) with OTUD7B (PubMed:21097510). Interacts with BBS1, HIPK1, CLCF1 and MTERF (PubMed:16390825, PubMed:21097510). Forms a complex with PINK1 and PRKN (PubMed:19229105). Interacts (via C-terminus) with NCF1; the interaction is enhanced by LPS and modulates NCF1 phosphorylation and membrane translocation (By similarity). Interacts with NENF (PubMed:31536960)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P01023","geneName":"A2M","intActId":"EBI-640741"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P63010-2","geneName":"AP2B1","intActId":"EBI-11529439"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P05067","geneName":"APP","intActId":"EBI-77613"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P10275","geneName":"AR","intActId":"EBI-608057"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q8NFJ9","geneName":"BBS1","intActId":"EBI-1805484"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q8N5S9-2","geneName":"CAMKK1","intActId":"EBI-25850646"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q9UER7","geneName":"DAXX","intActId":"EBI-77321"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P50570-2","geneName":"DNM2","intActId":"EBI-10968534"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q13158","geneName":"FADD","intActId":"EBI-494804"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P06241-3","geneName":"FYN","intActId":"EBI-10691738"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q9HD26","geneName":"GOPC","intActId":"EBI-349832"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q6DN90-2","geneName":"IQSEC1","intActId":"EBI-21911304"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q9BYQ4","geneName":"KRTAP9-2","intActId":"EBI-1044640"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q9BYZ2","geneName":"LDHAL6B","intActId":"EBI-1108377"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"O94776","geneName":"MTA2","intActId":"EBI-1783035"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q8NFH3","geneName":"NUP43","intActId":"EBI-1059321"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q96FW1","geneName":"OTUB1","intActId":"EBI-1058491"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q6GQQ9","geneName":"OTUD7B","intActId":"EBI-527784"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q99497","geneName":"PARK7","intActId":"EBI-1164361"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P32322","geneName":"PYCR1","intActId":"EBI-848624"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"P63244","geneName":"RACK1","intActId":"EBI-296739"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99497","intActId":"EBI-1164361"},"interactantTwo":{"uniProtKBAccession":"Q6ZNA4-2","geneName":"RNF111","intActId":"EBI-21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LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14705119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18711745"}],"value":"Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage (PubMed:18711745). Detected in tau inclusions in brains from neurodegenerative disease patients (PubMed:14705119). Membrane raft localization in astrocytes and neuronal cells requires palmitoylation"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q99LX0"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q99LX0"}],"value":"Lipid-anchor","id":"SL-9901"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12851414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14579415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15976810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19229105"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12851414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14579415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15976810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16390825"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O88767"}],"value":"Membrane raft","id":"SL-0370"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15181200"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18711745"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19229105"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31536960"}],"value":"Mitochondrion","id":"SL-0173"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31536960"}],"value":"Endoplasmic reticulum","id":"SL-0095"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14579415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14662519"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14705119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22611253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9070310"}],"value":"Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain (at protein level). Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa. Expressed by pancreatic islets at higher levels than surrounding exocrine tissues (PubMed:22611253)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22611253"}],"value":"In pancreatic islets, expression increases during aging"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14749723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15976810"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22611253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26995087"}],"value":"By hydrogen peroxide and UV irradiation (PubMed:14749723, PubMed:15976810). In pancreatic islets, expression increases under hyperglycemic conditions (PubMed:22611253). Expression is also induced by sulforaphane, an isothiocyanate obtained from cruciferous vegetables (PubMed:26995087)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15976810"}],"value":"Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and essential for cell-growth promoting activity and transforming activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12939276"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15976810"}],"value":"Cys-106 is easily oxidized to sulfinic acid"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20304780"}],"value":"Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Parkinson disease 7","diseaseAccession":"DI-01240","acronym":"PARK7","description":"A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).","diseaseCrossReference":{"database":"MIM","id":"606324"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12446870"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12851414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12953260"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14607841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14713311"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15254937"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15365989"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16240358"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17846173"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18785233"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19229105"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22523093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23792957"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23847046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26972524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28993701"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30928208"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase C56 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22523093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31653696"}],"value":"Glyoxalase activity has been reported (PubMed:22523093, PubMed:31653696). It may however reflect its deglycase activity (PubMed:25416785)"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25416785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27903648"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28013050"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28596309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31653696"}],"value":"The protein deglycation activity is controversial. It has been ascribed to a TRIS buffer artifact by a publication (PubMed:27903648) and as a result of the removal of methylglyoxal by glyoxalase activity that leads to a subsequent decomposition of hemithioacetals and hemianimals due to the shift in equilibrium position by another one (PubMed:31653696). However, biochemical experiments showing that PARK7 is a bona fide deglycase have been performed (PubMed:25416785, PubMed:28013050, PubMed:28596309)"}],"commentType":"CAUTION"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"25944712"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":null,"modifier":"UNKNOWN"}},"description":"Parkinson disease protein 7","featureId":"PRO_0000157849"},{"type":"Propeptide","location":{"start":{"value":null,"modifier":"UNKNOWN"},"end":{"value":189,"modifier":"EXACT"}},"description":"Removed in mature form","featureId":"PRO_0000405558"},{"type":"Active site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20304780"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25416785"}]},{"type":"Active site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20304780"}]},{"type":"Site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"Cleavage; by CASP6","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q99LX0"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylalanine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"25944712"}]},{"type":"Modified residue","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"15592455"}]},{"type":"Modified residue","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Cysteine sulfinic acid (-SO2H); alternate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12939276"}]},{"type":"Modified residue","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q99LX0"}]},{"type":"Modified residue","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"N6-succinyllysine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q99LX0"}]},{"type":"Lipidation","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23847046"}]},{"type":"Lipidation","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23847046"}]},{"type":"Lipidation","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"S-palmitoyl cysteine; alternate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23847046"}]},{"type":"Cross-link","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15976810"}]},{"type":"Natural variant","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"in PARK7; uncertain significance","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18785233"}],"featureId":"VAR_084339","alternativeSequence":{"originalSequence":"L","alternativeSequences":["P"]}},{"type":"Natural variant","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization; decreased detoxification activity on methylglyocal-adducted CoA; 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no apparent effect on protein stability; impaired mitochondrial morphology; no effect on detoxification activity on methylglyocal-adducted CoA; dbSNP:rs74315353","featureCrossReferences":[{"database":"dbSNP","id":"rs74315353"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14607841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15365989"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20186336"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28993701"}],"featureId":"VAR_020493","alternativeSequence":{"originalSequence":"E","alternativeSequences":["D"]}},{"type":"Natural variant","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"in dbSNP:rs71653619","featureCrossReferences":[{"database":"dbSNP","id":"rs71653619"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12953260"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14705128"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14872018"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15254937"}],"featureId":"VAR_020494","alternativeSequence":{"originalSequence":"R","alternativeSequences":["Q"]}},{"type":"Natural variant","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"in PARK7; 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