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Entry version 211 (29 Sep 2021)
Sequence version 2 (05 Jul 2004)
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Protein

Parkinson disease protein 7

Gene

PARK7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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:17015834, PubMed:20304780, PubMed:18711745, PubMed:12796482, PubMed:19229105, 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:15502874, PubMed:14749723, PubMed:17015834, PubMed:21097510, PubMed:18711745).

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:28013050, PubMed:26995087).

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:31653696, PubMed:28993701).

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:19229105, PubMed:16632486).

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).

By similarity27 Publications

Caution

Glyoxalase activity has been reported (PubMed:22523093, PubMed:31653696). It may however reflect its deglycase activity (PubMed:25416785).3 Publications
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).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Note: Deglycase activity does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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).2 Publications
  1. KM=173.4 µM for casein1 Publication
  2. KM=0.44 mM for glycated N-acetylarginine (at pH 7.0 and 22 degrees Celsius)1 Publication
  3. KM=0.35 mM for glycated N-acetyllysine (at pH 7.0 and 22 degrees Celsius)1 Publication
  4. KM=0.32 mM for glycated N-acetylcysteine (at pH 7.0 and 22 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei106Nucleophile2 Publications1
Active sitei1261 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone, Hydrolase, Protease, RNA-binding
Biological processAutophagy, DNA damage, DNA repair, Fertilization, Inflammatory response, Stress response
LigandCopper

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:ENSG00000116288-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.5.1.124, 2681
4.2.1.130, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
Q99497

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-3899300, SUMOylation of transcription cofactors
R-HSA-9613829, Chaperone Mediated Autophagy
R-HSA-9615710, Late endosomal microautophagy
R-HSA-9646399, Aggrephagy

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q99497

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q99497

SIGNOR Signaling Network Open Resource

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SIGNORi
Q99497

Protein family/group databases

MEROPS protease database

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MEROPSi
C56.002

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Parkinson disease protein 7Curated
Alternative name(s):
Maillard deglycase1 Publication
Oncogene DJ1Curated
Parkinsonism-associated deglycaseImported
Protein DJ-1Curated
Short name:
DJ-1
Protein/nucleic acid deglycase DJ-12 Publications (EC:3.1.2.-1 Publication, EC:3.5.1.-1 Publication, EC:3.5.1.1241 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PARK7Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:16369, PARK7

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602533, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q99497

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000116288

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Parkinson disease 7 (PARK7)16 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA 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).
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08433910L → P in PARK7; unknown pathological significance. 1 Publication1
Natural variantiVAR_02049226M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization; decreased detoxification acivity on methylglyocal-adducted CoA. 3 PublicationsCorresponds to variant dbSNP:rs74315351EnsemblClinVar.1
Natural variantiVAR_08327745Missing in PARK7. 1 Publication1
Natural variantiVAR_02049364E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology; no effect on detoxification acivity on methylglyocal-adducted CoA. 4 PublicationsCorresponds to variant dbSNP:rs74315353EnsemblClinVar.1
Natural variantiVAR_020495104A → T in PARK7; loss of protection against metal cytotoxicity; decreased detoxification acivity on methylglyocal-adducted CoA. 3 PublicationsCorresponds to variant dbSNP:rs774005786EnsemblClinVar.1
Natural variantiVAR_020496149D → A in PARK7; loss of protection against metal cytotoxicity; decreased detoxification acivity on methylglyocal-adducted CoA. 3 PublicationsCorresponds to variant dbSNP:rs74315352EnsemblClinVar.1
Natural variantiVAR_020498166L → P 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 acivity on methylglyocal-adducted CoA. 9 PublicationsCorresponds to variant dbSNP:rs28938172EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi10L → P: Abolishes detoxification acivity on methylglyocal-adducted CoA. 1 Publication1
Mutagenesisi18E → A: Strongly decreases enzymatic activity. Almost abolishes detoxification acivity on methylglyocal-adducted CoA. 2 Publications1
Mutagenesisi18E → D: Strongly decreases enzymatic activity. 1 Publication1
Mutagenesisi18E → N: Strongly decreases enzymatic activity. 1 Publication1
Mutagenesisi18E → Q: Strongly decreases enzymatic activity. 1 Publication1
Mutagenesisi46C → A: Reduces protein stability. No effect on oxidation. 4 Publications1
Mutagenesisi46C → A: Reduces protein stability. No effect on oxidation. Reduced localization in lipid rafts; when associated with A-106. 4 Publications1
Mutagenesisi46C → S: No effect on mitochondrial translocation neither on deglycase activity. 5 Publications1
Mutagenesisi51V → A: Disrupts dimer formation and strongly reduces ability to eliminate hydrogen peroxide. 1 Publication1
Mutagenesisi53C → A: Strongly reduces chaperone activity and ability to eliminate hydrogen peroxide. 4 Publications1
Mutagenesisi53C → S: No effect on mitochondrial translocation neither on deglycase activity. 5 Publications1
Mutagenesisi106C → A: Abolishes enzymatic activity. Abolishes oxidation, association with mitochondria and protease activity. No effect on chaperone activity. Reduces binding to OTUD7B. 8 Publications1
Mutagenesisi106C → A: Abolishes enzymatic activity. Abolishes oxidation, 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; when associated with A-46. 9 Publications1
Mutagenesisi106C → D: Abolishes oxidation and association with mitochondria. No effect on chaperone activity. 7 Publications1
Mutagenesisi106C → S: 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. 10 Publications1
Mutagenesisi126H → A: Strongly decreases enzymatic activity. 2 Publications1
Mutagenesisi130K → R: Partially compensates for loss of stability; when associated with P-166. 1 Publication1
Mutagenesisi179A → T: No effect on detoxification acivity on methylglyocal-adducted CoA. 1 Publication1

Keywords - Diseasei

Disease variant, Neurodegeneration, Parkinson disease, Parkinsonism, Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
11315

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
PARK7

MalaCards human disease database

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MalaCardsi
PARK7
MIMi168600, phenotype
606324, phenotype

Open Targets

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OpenTargetsi
ENSG00000116288

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
90020, Parkinson-dementia complex of Guam
2828, Young-onset Parkinson disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA32946

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q99497, Tbio

Chemistry databases

Drug and drug target database

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DrugBanki
DB09130, Copper

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PARK7

Domain mapping of disease mutations (DMDM)

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DMDMi
56404943

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001578492 – ?Parkinson disease protein 7
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000405558? – 189Removed in mature form

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi46S-palmitoyl cysteine1 Publication1
Lipidationi53S-palmitoyl cysteine1 Publication1
Modified residuei67PhosphotyrosineCombined sources1
Modified residuei106Cysteine sulfinic acid (-SO2H); alternate1 Publication1
Lipidationi106S-palmitoyl cysteine; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei148N6-acetyllysineBy similarity1
Modified residuei182N6-succinyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and essential for cell-growth promoting activity and transforming activity.1 Publication
Cys-106 is easily oxidized to sulfinic acid.2 Publications
Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Oxidation, Palmitate, Phosphoprotein, Ubl conjugation, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q99497

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q99497

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q99497

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q99497

PeptideAtlas

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PeptideAtlasi
Q99497

PRoteomics IDEntifications database

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PRIDEi
Q99497

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
78298

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q99497

2D gel databases

USC-OGP 2-DE database

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OGPi
Q99497

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00298547

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
Q99497

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
Q99497, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q99497

MetOSite database of methionine sulfoxide sites

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MetOSitei
Q99497

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q99497

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q99497

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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).5 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In pancreatic islets, expression increases during aging.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000116288, Expressed in metanephros and 245 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q99497, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q99497, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000116288, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:12851414, PubMed:12796482, PubMed:12855764, PubMed:31653696). Binds EFCAB6/DJBP and PIAS2 (PubMed:11477070, PubMed:12851414, PubMed:12612053).

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).

By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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GO - Molecular functioni