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Entry version 197 (03 Jul 2019)
Sequence version 2 (05 Jul 2004)
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Protein/nucleic acid deglycase DJ-1



Homo sapiens (Human)
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


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="">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


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">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="">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="">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

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases


    Reactome - a knowledgebase of biological pathways and processes

    R-HSA-3899300 SUMOylation of transcription cofactors

    SABIO-RK: Biochemical Reaction Kinetics Database


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


    SIGNOR Signaling Network Open Resource


    Protein family/group databases

    MEROPS protease database


    <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="">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: Publication)
    Alternative name(s):
    Maillard deglycase1 Publication
    Oncogene DJ1Curated
    Parkinson disease protein 7Curated
    Parkinsonism-associated deglycaseImported
    Protein DJ-1Curated
    Short name:
    <p>This subsection of the <a href="">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
    <p>This subsection of the <a href="">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="">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="">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="">Names and taxonomy</a> section is present for entries that are part of a <a href="">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="">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

    HGNC:16369 PARK7

    Online Mendelian Inheritance in Man (OMIM)

    602533 gene

    neXtProt; the human protein knowledge platform


    <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 & Seán O’Donoghue; 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="">OMIM</a> database are represented with a <a href="">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).
    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_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


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">'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



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


    MalaCards human disease database

    MIMi168600 phenotype
    606324 phenotype

    Open Targets


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

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

    The Pharmacogenetics and Pharmacogenomics Knowledge Base


    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database


    Domain mapping of disease mutations (DMDM)


    <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="">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
    <p>This subsection of the <a href="">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="">lipids</a>, <a href="">glycans</a> and <a href="">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="">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="">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="">'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="">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


    jPOST - Japan Proteome Standard Repository/Database


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




    PRoteomics IDEntifications database


    ProteomicsDB human proteome resource


    Consortium for Top Down Proteomics


    2D gel databases

    USC-OGP 2-DE database




    University College Dublin 2-DE Proteome Database


    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context


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


    SwissPalm database of S-palmitoylation events


    Miscellaneous databases

    CutDB - Proteolytic event database


    <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="">P92958</a>, <a href="">Q8TDN4</a>, <a href="">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

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

    ExpressionAtlas, Differential and Baseline Expression

    Q99497 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    Q99497 HS

    Organism-specific databases

    Human Protein Atlas


    <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="">'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="">'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="">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="">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)

    116446, 172 interactors

    CORUM comprehensive resource of mammalian protein complexes


    Database of interacting proteins


    Protein interaction database and analysis system

    Q99497, 114 interactors

    Molecular INTeraction database


    STRING: functional protein association networks


    <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

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