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Protein

Protein/nucleic acid deglycase DJ-1

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

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). Thus, functions as a protein deglycase that 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). Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity (PubMed:22523093). Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function (PubMed:17015834, PubMed:20304780, PubMed:18711745, PubMed:12796482, PubMed:19229105, PubMed:25416785, PubMed:26995087). 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). 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 similarity24 Publications

Caution

Glyoxalase activity was previously reported (PubMed:22523093). It may however reflect its deglycase activity (PubMed:25416785).2 Publications
The protein deglycation activity has been ascribed to a TRIS buffer artifact by a publication (PubMed:27903648). However, clear biochemical experiments showing that PARK7 is a bona fide deglycase have been performed (PubMed:25416785, PubMed:28013050). Deglycase activity is even strengthened by a an article that reports nucleotide deglycation activity (PubMed:28596309).4 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.1 Publication

<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.1 Publication
  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 ‘Function’ 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

    More...
    BioCyci
    MetaCyc:ENSG00000116288-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-3899300 SUMOylation of transcription cofactors

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q99497

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

    More...
    SignaLinki
    Q99497

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q99497

    Protein family/group databases

    MEROPS protease database

    More...
    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:
    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)
    Alternative name(s):
    Maillard deglycase1 Publication
    Oncogene DJ1Curated
    Parkinson disease protein 7Curated
    Parkinsonism-associated deglycaseImported
    Protein DJ-1Curated
    Short name:
    DJ-1
    <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

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000116288.12

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:16369 PARK7

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    602533 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q99497

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, 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)12 Publications
    The disease is caused by mutations 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).
    See also OMIM:606324
    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_02049226M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 2 PublicationsCorresponds to variant dbSNP:rs74315351EnsemblClinVar.1
    Natural variantiVAR_02049364E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 3 PublicationsCorresponds to variant dbSNP:rs74315353EnsemblClinVar.1
    Natural variantiVAR_020495104A → T in PARK7; loss of protection against metal cytotoxicity. 2 PublicationsCorresponds to variant dbSNP:rs774005786Ensembl.1
    Natural variantiVAR_020496149D → A in PARK7; loss of protection against metal cytotoxicity. 2 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. 8 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>Mutagenesisi18E → A: Strongly decreases enzymatic activity. 1 Publication1
    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: Reduced localization in lipid rafts; when associated with A-106. 4 Publications1
    Mutagenesisi46C → A: Reduces protein stability. No effect on oxidation. 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: Reduced localization in lipid rafts; when associated with A-46. 7 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. 9 Publications1
    Mutagenesisi126H → A: Strongly decreases enzymatic activity. 2 Publications1
    Mutagenesisi130K → R: Partially compensates for loss of stability; when associated with P-166. 1 Publication1

    Keywords - Diseasei

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

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    11315

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

    More...
    GeneReviewsi
    PARK7

    MalaCards human disease database

    More...
    MalaCardsi
    PARK7
    MIMi168600 phenotype
    606324 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000116288

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

    More...
    Orphaneti
    90020 Amyotrophic lateral sclerosis-parkinsonism-dementia complex
    2828 Young-onset Parkinson disease

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA32946

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PARK7

    Domain mapping of disease mutations (DMDM)

    More...
    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 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
    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001578492 – ?Protein/nucleic acid deglycase DJ-1

    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

    More...
    EPDi
    Q99497

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q99497

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

    More...
    PaxDbi
    Q99497

    PeptideAtlas

    More...
    PeptideAtlasi
    Q99497

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q99497

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    78298

    Consortium for Top Down Proteomics

    More...
    TopDownProteomicsi
    Q99497

    2D gel databases

    USC-OGP 2-DE database

    More...
    OGPi
    Q99497

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00298547

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    Q99497

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q99497

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

    More...
    PhosphoSitePlusi
    Q99497

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q99497

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...
    PMAP-CutDBi
    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

    More...
    Bgeei
    ENSG00000116288 Expressed in 233 organ(s), highest expression level in metanephros

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_PARK7

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q99497 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q99497 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB005870
    HPA004190

    <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). 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).By similarity7 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    116446, 163 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q99497

    Database of interacting proteins

    More...
    DIPi
    DIP-35515N

    Protein interaction database and analysis system

    More...
    IntActi
    Q99497, 113 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q99497

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000340278

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1189
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1J42X-ray2.50A1-189[»]
    1P5FX-ray1.10A1-189[»]
    1PDVX-ray1.80A1-189[»]
    1PDWX-ray2.20A/B/C/D/E/F/G/H1-189[»]
    1PE0X-ray1.70A/B1-189[»]
    1Q2UX-ray1.60A1-189[»]
    1SOAX-ray1.20A1-189[»]
    1UCFX-ray1.95A/B1-189[»]
    2OR3X-ray1.20A/B1-189[»]
    2R1TX-ray1.70A/B2-188[»]
    2R1UX-ray1.50A/B2-188[»]
    2R1VX-ray1.70A/B2-188[»]
    2RK3X-ray1.05A1-189[»]
    2RK4X-ray1.15A1-189[»]
    2RK6X-ray1.15A1-189[»]
    3B36X-ray1.50A1-189[»]
    3B38X-ray1.85A1-189[»]
    3B3AX-ray1.50A1-189[»]
    3BWEX-ray2.40A/B/C/D/E/F/G1-189[»]
    3CY6X-ray1.35A1-189[»]
    3CYFX-ray1.60A1-189[»]
    3CZ9X-ray1.15A1-189[»]
    3CZAX-ray1.20A1-189[»]
    3EZGX-ray1.15A1-189[»]
    3F71X-ray1.20A1-189[»]
    3SF8X-ray1.56A/B1-189[»]
    4BTEX-ray1.38A1-189[»]
    4MNTX-ray1.58A1-189[»]
    4MTCX-ray1.47A1-189[»]
    4N0MX-ray1.95A1-189[»]
    4N12X-ray1.48A1-189[»]
    4OGFX-ray1.60A2-188[»]
    4OQ4X-ray1.49A1-189[»]
    4P2GX-ray1.35A1-189[»]
    4P34X-ray1.55A1-189[»]
    4P35X-ray1.75A1-189[»]
    4P36X-ray1.18A1-189[»]
    4RKWX-ray1.50A1-189[»]
    4RKYX-ray1.50A1-189[»]
    4S0ZX-ray1.45A1-189[»]
    4ZGGX-ray1.23A1-189[»]
    5IP5X-ray1.66A1-189[»]
    5SY6X-ray1.15A1-189[»]
    5SY9X-ray1.10A1-189[»]
    5SYAX-ray1.10A1-189[»]
    6AF5X-ray1.65A1-189[»]
    6AF7X-ray1.30A1-189[»]
    6AF9X-ray1.39A1-189[»]
    6AFAX-ray1.65A1-189[»]
    6AFBX-ray1.60A1-189[»]
    6AFCX-ray1.45A1-189[»]
    6AFDX-ray1.48A1-189[»]
    6AFEX-ray1.50A1-189[»]
    6AFFX-ray1.60A1-189[»]
    6AFGX-ray1.50A1-189[»]
    6AFHX-ray1.65A1-189[»]
    6AFIX-ray1.65A1-189[»]
    6AFJX-ray1.48A1-189[»]
    6AFLX-ray1.60A1-189[»]
    6E5ZX-ray1.35A1-189[»]
    6M8ZX-ray1.83A1-189[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q99497

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q99497

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q99497

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the peptidase C56 family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2764 Eukaryota
    COG0693 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000001231

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000063194

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG053511

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q99497

    KEGG Orthology (KO)

    More...
    KOi
    K05687

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CYPGFEK

    Database of Orthologous Groups

    More...
    OrthoDBi
    1165707at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q99497

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300119

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.880, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029062 Class_I_gatase-like
    IPR006287 DJ-1
    IPR002818 DJ-1/PfpI

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01965 DJ-1_PfpI, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52317 SSF52317, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01383 not_thiJ, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    Q99497-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV
    60 70 80 90 100
    VICPDASLED AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG
    110 120 130 140 150
    LIAAICAGPT ALLAHEIGFG SKVTTHPLAK DKMMNGGHYT YSENRVEKDG
    160 170 180
    LILTSRGPGT SFEFALAIVE ALNGKEVAAQ VKAPLVLKD
    Length:189
    Mass (Da):19,891
    Last modified:July 5, 2004 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4B21661B3A76BC67
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    K7ELW0K7ELW0_HUMAN
    Protein/nucleic acid deglycase DJ-1
    PARK7
    169Annotation score:

    Annotation score:1 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>
    K7EN27K7EN27_HUMAN
    Protein/nucleic acid deglycase DJ-1
    PARK7
    160Annotation score:

    Annotation score:1 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 Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti119F → C in BAB71782 (Ref. 3) Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_02049226M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 2 PublicationsCorresponds to variant dbSNP:rs74315351EnsemblClinVar.1
    Natural variantiVAR_07258939A → S Probable disease-associated mutation found in early-onset Parkinson disease with digenic inheritance; the patient also carries PINK1 mutation L-399. 1 PublicationCorresponds to variant dbSNP:rs137853051EnsemblClinVar.1
    Natural variantiVAR_02049364E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 3 PublicationsCorresponds to variant dbSNP:rs74315353EnsemblClinVar.1
    Natural variantiVAR_02049498R → Q4 PublicationsCorresponds to variant dbSNP:rs71653619EnsemblClinVar.1
    Natural variantiVAR_020495104A → T in PARK7; loss of protection against metal cytotoxicity. 2 PublicationsCorresponds to variant dbSNP:rs774005786Ensembl.1
    Natural variantiVAR_020496149D → A in PARK7; loss of protection against metal cytotoxicity. 2 PublicationsCorresponds to variant dbSNP:rs74315352EnsemblClinVar.1
    Natural variantiVAR_020497150G → S1 PublicationCorresponds to variant dbSNP:rs368420490EnsemblClinVar.1
    Natural variantiVAR_034801163E → K1 PublicationCorresponds to variant dbSNP:rs74315354EnsemblClinVar.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. 8 PublicationsCorresponds to variant dbSNP:rs28938172EnsemblClinVar.1
    Natural variantiVAR_020499171A → S1 PublicationCorresponds to variant dbSNP:rs777026628EnsemblClinVar.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    D61380 mRNA Translation: BAA09603.2
    AF021819 mRNA Translation: AAC12806.1
    AB073864 mRNA Translation: BAB71782.1
    AK312000 mRNA Translation: BAG34938.1
    AL034417 Genomic DNA No translation available.
    CH471130 Genomic DNA Translation: EAW71591.1
    BC008188 mRNA Translation: AAH08188.1
    AB045294 Genomic DNA No translation available.
    AY648999 Genomic DNA Translation: AAT68961.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS93.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    JC5394

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001116849.1, NM_001123377.1
    NP_009193.2, NM_007262.4
    XP_005263481.1, XM_005263424.3

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.419640

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000338639; ENSP00000340278; ENSG00000116288
    ENST00000377488; ENSP00000366708; ENSG00000116288
    ENST00000377491; ENSP00000366711; ENSG00000116288
    ENST00000493373; ENSP00000465404; ENSG00000116288
    ENST00000493678; ENSP00000418770; ENSG00000116288

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    11315

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:11315

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D61380 mRNA Translation: BAA09603.2
    AF021819 mRNA Translation: AAC12806.1
    AB073864 mRNA Translation: BAB71782.1
    AK312000 mRNA Translation: BAG34938.1
    AL034417 Genomic DNA No translation available.
    CH471130 Genomic DNA Translation: EAW71591.1
    BC008188 mRNA Translation: AAH08188.1
    AB045294 Genomic DNA No translation available.
    AY648999 Genomic DNA Translation: AAT68961.1
    CCDSiCCDS93.1
    PIRiJC5394
    RefSeqiNP_001116849.1, NM_001123377.1
    NP_009193.2, NM_007262.4
    XP_005263481.1, XM_005263424.3
    UniGeneiHs.419640

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1J42X-ray2.50A1-189[»]
    1P5FX-ray1.10A1-189[»]
    1PDVX-ray1.80A1-189[»]
    1PDWX-ray2.20A/B/C/D/E/F/G/H1-189[»]
    1PE0X-ray1.70A/B1-189[»]
    1Q2UX-ray1.60A1-189[»]
    1SOAX-ray1.20A1-189[»]
    1UCFX-ray1.95A/B1-189[»]
    2OR3X-ray1.20A/B1-189[»]
    2R1TX-ray1.70A/B2-188[»]
    2R1UX-ray1.50A/B2-188[»]
    2R1VX-ray1.70A/B2-188[»]
    2RK3X-ray1.05A1-189[»]
    2RK4X-ray1.15A1-189[»]
    2RK6X-ray1.15A1-189[»]
    3B36X-ray1.50A1-189[»]
    3B38X-ray1.85A1-189[»]
    3B3AX-ray1.50A1-189[»]
    3BWEX-ray2.40A/B/C/D/E/F/G1-189[»]
    3CY6X-ray1.35A1-189[»]
    3CYFX-ray1.60A1-189[»]
    3CZ9X-ray1.15A1-189[»]
    3CZAX-ray1.20A1-189[»]
    3EZGX-ray1.15A1-189[»]
    3F71X-ray1.20A1-189[»]
    3SF8X-ray1.56A/B1-189[»]
    4BTEX-ray1.38A1-189[»]
    4MNTX-ray1.58A1-189[»]
    4MTCX-ray1.47A1-189[»]
    4N0MX-ray1.95A1-189[»]
    4N12X-ray1.48A1-189[»]
    4OGFX-ray1.60A2-188[»]
    4OQ4X-ray1.49A1-189[»]
    4P2GX-ray1.35A1-189[»]
    4P34X-ray1.55A1-189[»]
    4P35X-ray1.75A1-189[»]
    4P36X-ray1.18A1-189[»]
    4RKWX-ray1.50A1-189[»]
    4RKYX-ray1.50A1-189[»]
    4S0ZX-ray1.45A1-189[»]
    4ZGGX-ray1.23A1-189[»]
    5IP5X-ray1.66A1-189[»]
    5SY6X-ray1.15A1-189[»]
    5SY9X-ray1.10A1-189[»]
    5SYAX-ray1.10A1-189[»]
    6AF5X-ray1.65A1-189[»]
    6AF7X-ray1.30A1-189[»]
    6AF9X-ray1.39A1-189[»]
    6AFAX-ray1.65A1-189[»]
    6AFBX-ray1.60A1-189[»]
    6AFCX-ray1.45A1-189[»]
    6AFDX-ray1.48A1-189[»]
    6AFEX-ray1.50A1-189[»]
    6AFFX-ray1.60A1-189[»]
    6AFGX-ray1.50A1-189[»]
    6AFHX-ray1.65A1-189[»]
    6AFIX-ray1.65A1-189[»]
    6AFJX-ray1.48A1-189[»]
    6AFLX-ray1.60A1-189[»]
    6E5ZX-ray1.35A1-189[»]
    6M8ZX-ray1.83A1-189[»]
    ProteinModelPortaliQ99497
    SMRiQ99497
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116446, 163 interactors
    CORUMiQ99497
    DIPiDIP-35515N
    IntActiQ99497, 113 interactors
    MINTiQ99497
    STRINGi9606.ENSP00000340278

    Protein family/group databases

    MEROPSiC56.002

    PTM databases

    iPTMnetiQ99497
    PhosphoSitePlusiQ99497
    SwissPalmiQ99497

    Polymorphism and mutation databases

    BioMutaiPARK7
    DMDMi56404943

    2D gel databases

    OGPiQ99497
    REPRODUCTION-2DPAGEiIPI00298547
    UCD-2DPAGEiQ99497

    Proteomic databases

    EPDiQ99497
    jPOSTiQ99497
    PaxDbiQ99497
    PeptideAtlasiQ99497
    PRIDEiQ99497
    ProteomicsDBi78298
    TopDownProteomicsiQ99497

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    11315
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000338639; ENSP00000340278; ENSG00000116288
    ENST00000377488; ENSP00000366708; ENSG00000116288
    ENST00000377491; ENSP00000366711; ENSG00000116288
    ENST00000493373; ENSP00000465404; ENSG00000116288
    ENST00000493678; ENSP00000418770; ENSG00000116288
    GeneIDi11315
    KEGGihsa:11315

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    11315
    DisGeNETi11315
    EuPathDBiHostDB:ENSG00000116288.12

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PARK7
    GeneReviewsiPARK7
    HGNCiHGNC:16369 PARK7
    HPAiCAB005870
    HPA004190
    MalaCardsiPARK7
    MIMi168600 phenotype
    602533 gene
    606324 phenotype
    neXtProtiNX_Q99497
    OpenTargetsiENSG00000116288
    Orphaneti90020 Amyotrophic lateral sclerosis-parkinsonism-dementia complex
    2828 Young-onset Parkinson disease
    PharmGKBiPA32946

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2764 Eukaryota
    COG0693 LUCA
    GeneTreeiENSGT00390000001231
    HOGENOMiHOG000063194
    HOVERGENiHBG053511
    InParanoidiQ99497
    KOiK05687
    OMAiCYPGFEK
    OrthoDBi1165707at2759
    PhylomeDBiQ99497
    TreeFamiTF300119

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000116288-MONOMER
    ReactomeiR-HSA-3899300 SUMOylation of transcription cofactors
    SABIO-RKiQ99497
    SignaLinkiQ99497
    SIGNORiQ99497

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    PARK7 human
    EvolutionaryTraceiQ99497

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    PARK7

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    11315
    PMAP-CutDBiQ99497

    Protein Ontology

    More...
    PROi
    PR:Q99497

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000116288 Expressed in 233 organ(s), highest expression level in metanephros
    CleanExiHS_PARK7
    ExpressionAtlasiQ99497 baseline and differential
    GenevisibleiQ99497 HS

    Family and domain databases

    Gene3Di3.40.50.880, 1 hit
    InterProiView protein in InterPro
    IPR029062 Class_I_gatase-like
    IPR006287 DJ-1
    IPR002818 DJ-1/PfpI
    PfamiView protein in Pfam
    PF01965 DJ-1_PfpI, 1 hit
    SUPFAMiSSF52317 SSF52317, 1 hit
    TIGRFAMsiTIGR01383 not_thiJ, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPARK7_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q99497
    Secondary accession number(s): B2R4Z1
    , O14805, Q6DR95, Q7LFU2
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotat