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Protein

Lysine-specific demethylase 5A

Gene

KDM5A

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

Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif (PubMed:18270511). May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation (PubMed:19430464). May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity). Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells (PubMed:27427228).By similarity8 Publications

<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

Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The inhibitors KDOAM-25, CPI-455 and others inhibits its demethylase activity, resulting to cell growth arrest in cancer cells.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 are 2.1 min(-1) and 1.9 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.1 Publication
  1. KM=9 µM for 2-oxoglutarate1 Publication
  2. KM=2.9 µM for histone H3K4me31 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei4092-oxoglutarate2 Publications1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi483Iron; catalyticPROSITE-ProRule annotation4 Publications1
    Metal bindingi485Iron; catalytic4 Publications1
    Binding sitei4912-oxoglutarate2 Publications1
    Binding sitei4932-oxoglutarate2 Publications1
    Binding sitei5012-oxoglutarate2 Publications1
    Metal bindingi571Iron; catalyticPROSITE-ProRule annotation4 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri293 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST51
    Zinc fingeri676 – 728C5HC2Combined sources2 PublicationsAdd BLAST53
    Zinc fingeri1161 – 1218PHD-type 2PROSITE-ProRule annotationAdd BLAST58
    Zinc fingeri1607 – 1661PHD-type 31 PublicationAdd BLAST55

    <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 functionActivator, Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase
    Biological processBiological rhythms, Transcription, Transcription regulation
    LigandIron, Metal-binding, Zinc

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-3214842 HDMs demethylate histones

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P29375

    <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:
    Lysine-specific demethylase 5A (EC:1.14.11.-)
    Alternative name(s):
    Histone demethylase JARID1A
    Jumonji/ARID domain-containing protein 1A
    Retinoblastoma-binding protein 2
    Short name:
    RBBP-2
    <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:KDM5AImported
    Synonyms:JARID1A, RBBP2, RBP21 Publication
    <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 12

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000073614.11

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:9886 KDM5A

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    180202 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P29375

    <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

    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

    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>Mutagenesisi112R → E: Decreases DNA-binding. 1 Publication1
    Mutagenesisi152K → E: Abolishes DNA-binding. 1 Publication1
    Mutagenesisi156S → D: Decreases DNA-binding. 1 Publication1
    Mutagenesisi157L → E: Decreases DNA-binding. 1 Publication1
    Mutagenesisi626C → S: No effect on lysine-specific histone demethylase activity; when associated with S-636. 1 Publication1
    Mutagenesisi636C → S: No effect on lysine-specific histone demethylase activity; when associated with S-626. 1 Publication1
    Mutagenesisi1609V → G: No effect on interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication1
    Mutagenesisi1625W → A: Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication1
    Mutagenesisi1634 – 1635EW → AA: Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication2

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    5927

    Open Targets

    More...
    OpenTargetsi
    ENSG00000073614

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA34250

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2424504

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2680

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    KDM5A

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    215274124

    <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 ‘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_00002005841 – 1690Lysine-specific demethylase 5AAdd BLAST1690

    Amino acid modifications

    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 <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-linki191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    <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 residuei204PhosphoserineCombined sources1
    Cross-linki1007Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei1111PhosphoserineCombined sources1
    Modified residuei1330PhosphoserineCombined sources1
    Modified residuei1331PhosphoserineCombined sources1
    Modified residuei1343PhosphothreonineBy similarity1
    Modified residuei1345PhosphoserineBy similarity1
    Modified residuei1438PhosphoserineCombined sources1
    Modified residuei1488PhosphoserineCombined sources1
    Modified residuei1595PhosphotyrosineBy similarity1
    Modified residuei1598PhosphoserineCombined sources1
    Modified residuei1603PhosphoserineCombined sources1
    Modified residuei1666PhosphoserineCombined sources1

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P29375

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P29375

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

    More...
    PaxDbi
    P29375

    PeptideAtlas

    More...
    PeptideAtlasi
    P29375

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P29375

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    54559
    54560 [P29375-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P29375

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

    More...
    PhosphoSitePlusi
    P29375

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P29375

    <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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000073614 Expressed in 244 organ(s), highest expression level in peritoneum

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_JARID1A
    HS_RBP2

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P29375 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P29375 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA006201

    <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

    Interacts with SUZ12; the interaction is direct (By similarity). Interacts with the viral protein-binding domain of RB1. Interacts with ESR1, MYC, MYCN and LMO2. Interacts with HDAC1 (By similarity). Interacts with ARNTL/BMAL1 and CLOCK. Interacts (via PHD-type 1 zinc finger) with histone H3 unmodified at 'Lys-4' and (via PHD-type 3 zinc finger) with histone H3 di- and trimethylated at 'Lys-4' (PubMed:19430464).By similarity8 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

    WithEntry#Exp.IntActNotes
    RB1P064002EBI-1560836,EBI-491274

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    111862, 33 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-472N

    Protein interaction database and analysis system

    More...
    IntActi
    P29375, 11 interactors

    Molecular INTeraction database

    More...
    MINTi
    P29375

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000382688

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P29375

    <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

    11690
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P29375

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

    More...
    SMRi
    P29375

    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
    P29375

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini19 – 60JmjNPROSITE-ProRule annotationAdd BLAST42
    Domaini84 – 174ARIDPROSITE-ProRule annotationAdd BLAST91
    Domaini437 – 603JmjCPROSITE-ProRule annotationAdd BLAST167

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1623 – 1690Interaction with LMO21 PublicationAdd BLAST68

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi419 – 423GSGFP motifBy similarity5

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1492 – 1587Lys-richAdd BLAST96

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The GSGFP motif is required for the interaction with SUZ12 (By similarity). The ARID domain specifically binds to the CCGCCC motif and is required for the lysine-specific histone demethylase activity (PubMed:18270511). The PHD-type 3 zinc finger is required for the interaction with histone H3 di- and trimethylated at 'Lys-4' (PubMed:19430464).By similarity2 Publications

    <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 JARID1 histone demethylase family.Curated

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri293 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST51
    Zinc fingeri676 – 728C5HC2Combined sources2 PublicationsAdd BLAST53
    Zinc fingeri1161 – 1218PHD-type 2PROSITE-ProRule annotationAdd BLAST58
    Zinc fingeri1607 – 1661PHD-type 31 PublicationAdd BLAST55

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1246 Eukaryota
    ENOG410XR9J LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157170

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000290719

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P29375

    KEGG Orthology (KO)

    More...
    KOi
    K11446

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    PICDWRV

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P29375

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF106476

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.150.60, 1 hit
    3.30.40.10, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001606 ARID_dom
    IPR036431 ARID_dom_sf
    IPR003347 JmjC_dom
    IPR003349 JmjN
    IPR013637 Lys_sp_deMease-like_dom
    IPR019786 Zinc_finger_PHD-type_CS
    IPR004198 Znf_C5HC2
    IPR011011 Znf_FYVE_PHD
    IPR001965 Znf_PHD
    IPR019787 Znf_PHD-finger
    IPR013083 Znf_RING/FYVE/PHD

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01388 ARID, 1 hit
    PF02373 JmjC, 1 hit
    PF02375 JmjN, 1 hit
    PF00628 PHD, 2 hits
    PF08429 PLU-1, 1 hit
    PF02928 zf-C5HC2, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00501 BRIGHT, 1 hit
    SM00558 JmjC, 1 hit
    SM00545 JmjN, 1 hit
    SM00249 PHD, 3 hits

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF46774 SSF46774, 1 hit
    SSF57903 SSF57903, 3 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51011 ARID, 1 hit
    PS51184 JMJC, 1 hit
    PS51183 JMJN, 1 hit
    PS01359 ZF_PHD_1, 2 hits
    PS50016 ZF_PHD_2, 3 hits

    <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>Sequences (2+)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.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P29375-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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    MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK
    60 70 80 90 100
    IRPPKDWQPP FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL
    110 120 130 140 150
    QGSTLKIPVV ERKILDLYAL SKIVASKGGF EMVTKEKKWS KVGSRLGYLP
    160 170 180 190 200
    GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPNLDLKE KVEPEVLSTD
    210 220 230 240 250
    TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ IFGAGPKVVG
    260 270 280 290 300
    LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
    310 320 330 340 350
    RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE
    360 370 380 390 400
    AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS
    410 420 430 440 450
    IEEDVIVEYG ADISSKDFGS GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV
    460 470 480 490 500
    LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP
    510 520 530 540 550
    KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV
    560 570 580 590 600
    PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
    610 620 630 640 650
    HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR
    660 670 680 690 700
    ESVVQMGVLM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL
    710 720 730 740 750
    YHPTDLCPCP MQKKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL
    760 770 780 790 800
    SANFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCASVAQL
    810 820 830 840 850
    LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI SQARQVKNLL
    860 870 880 890 900
    DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
    910 920 930 940 950
    ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT
    960 970 980 990 1000
    VSERWEEKAK VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK
    1010 1020 1030 1040 1050
    AREWTAKVEA IQSGSNYAYL EQLESLSAKG RPIPVRLEAL PQVESQVAAA
    1060 1070 1080 1090 1100
    RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKELIEKE
    1110 1120 1130 1140 1150
    KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA MHSLRAANLA
    1160 1170 1180 1190 1200
    KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
    1210 1220 1230 1240 1250
    SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT
    1260 1270 1280 1290 1300
    ERAMSWQDRA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL
    1310 1320 1330 1340 1350
    QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPRQTMDYDD EETDSDEDIR
    1360 1370 1380 1390 1400
    ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH
    1410 1420 1430 1440 1450
    AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM
    1460 1470 1480 1490 1500
    VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD
    1510 1520 1530 1540 1550
    SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK
    1560 1570 1580 1590 1600
    LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA
    1610 1620 1630 1640 1650
    EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN
    1660 1670 1680 1690
    EDYICINCAK KQGPVSPGPA PPPSFIMSYK LPMEDLKETS
    Length:1,690
    Mass (Da):192,095
    Last modified:November 25, 2008 - v3
    <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:iFCF6DC22DEF001DF
    GO
    Isoform 2 (identifier: P29375-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1623-1690: VDWVQCDGGC...LPMEDLKETS → GVVFVTEEERDKKY

    Show »
    Length:1,636
    Mass (Da):186,289
    Checksum:iF308F907C2F899E0
    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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    E7EV89E7EV89_HUMAN
    Lysine-specific demethylase 5A
    KDM5A
    715Annotation 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>
    F5H322F5H322_HUMAN
    Lysine-specific demethylase 5A
    KDM5A
    122Annotation 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>
    F5GZR8F5GZR8_HUMAN
    Lysine-specific demethylase 5A
    KDM5A
    131Annotation 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>
    F5GZ99F5GZ99_HUMAN
    Lysine-specific demethylase 5A
    KDM5A
    126Annotation 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>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAB28544 differs from that shown. Reason: Frameshift at several positions.Curated
    The sequence BAE06081 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    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 conflicti1411Q → QVFFGK in AAB28544 (PubMed:8414517).Curated1
    Sequence conflicti1547E → K in AAB28544 (PubMed:8414517).Curated1
    Sequence conflicti1612 – 1614AQN → EPD in AAB28544 (PubMed:8414517).Curated3

    Natural variant

    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_032984865M → T. Corresponds to variant dbSNP:rs11062385Ensembl.1
    Natural variantiVAR_0329851190P → A. Corresponds to variant dbSNP:rs2229353Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0357461623 – 1690VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2. 1 PublicationAdd BLAST68

    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
    S66431 mRNA Translation: AAB28544.1 Frameshift.
    AB209999 mRNA Translation: BAE06081.1 Different initiation.
    AC005844 Genomic DNA No translation available.
    AC007406 Genomic DNA No translation available.
    BC048307 mRNA Translation: AAH48307.1 Different termination.
    BC053893 mRNA Translation: AAH53893.1 Different termination.
    BC110916 mRNA Translation: AAI10917.1 Different termination.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS41736.1 [P29375-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    I78879

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001036068.1, NM_001042603.2 [P29375-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.76272

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000399788; ENSP00000382688; ENSG00000073614 [P29375-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    5927

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:5927

    UCSC genome browser

    More...
    UCSCi
    uc001qif.3 human [P29375-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, 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

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S66431 mRNA Translation: AAB28544.1 Frameshift.
    AB209999 mRNA Translation: BAE06081.1 Different initiation.
    AC005844 Genomic DNA No translation available.
    AC007406 Genomic DNA No translation available.
    BC048307 mRNA Translation: AAH48307.1 Different termination.
    BC053893 mRNA Translation: AAH53893.1 Different termination.
    BC110916 mRNA Translation: AAI10917.1 Different termination.
    CCDSiCCDS41736.1 [P29375-1]
    PIRiI78879
    RefSeqiNP_001036068.1, NM_001042603.2 [P29375-1]
    UniGeneiHs.76272

    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
    2JXJNMR-A85-175[»]
    2KGGNMR-A1609-1659[»]
    2KGINMR-A1609-1659[»]
    3GL6X-ray1.90A1609-1659[»]
    5C11X-ray2.80A1609-1659[»]
    5CEHX-ray3.14A12-797[»]
    5E6HX-ray2.24A1-87[»]
    A348-588[»]
    5ISLX-ray1.69A1-87[»]
    A348-588[»]
    5IVBX-ray1.39A1-87[»]
    A348-588[»]
    5IVCX-ray1.57A1-87[»]
    A348-588[»]
    5IVEX-ray1.78A1-87[»]
    A348-588[»]
    5IVFX-ray1.68A1-87[»]
    A348-588[»]
    5IVJX-ray1.57A1-87[»]
    A348-588[»]
    5IVVX-ray1.85A1-87[»]
    A348-588[»]
    5IVYX-ray1.45A1-87[»]
    A348-588[»]
    5IW0X-ray1.63A1-87[»]
    A348-588[»]
    5IWFX-ray2.29A1-87[»]
    A348-588[»]
    5K4LX-ray3.18A/B12-797[»]
    5V9PX-ray3.00A12-797[»]
    5V9TX-ray3.05A/B12-797[»]
    6BGUX-ray1.68A1-588[»]
    6BGVX-ray1.59A1-588[»]
    6BGWX-ray1.64A1-588[»]
    6BGXX-ray1.88A1-588[»]
    6BGYX-ray1.22A1-588[»]
    6BGZX-ray1.69A1-588[»]
    6BH0X-ray1.99A1-588[»]
    6BH1X-ray1.93A1-588[»]
    6BH2X-ray1.45A1-588[»]
    6BH3X-ray1.70A1-588[»]
    6BH4X-ray2.05A1-588[»]
    6BH5X-ray1.65A1-588[»]
    ProteinModelPortaliP29375
    SMRiP29375
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111862, 33 interactors
    DIPiDIP-472N
    IntActiP29375, 11 interactors
    MINTiP29375
    STRINGi9606.ENSP00000382688

    Chemistry databases

    BindingDBiP29375
    ChEMBLiCHEMBL2424504
    GuidetoPHARMACOLOGYi2680

    PTM databases

    iPTMnetiP29375
    PhosphoSitePlusiP29375
    SwissPalmiP29375

    Polymorphism and mutation databases

    BioMutaiKDM5A
    DMDMi215274124

    Proteomic databases

    EPDiP29375
    MaxQBiP29375
    PaxDbiP29375
    PeptideAtlasiP29375
    PRIDEiP29375
    ProteomicsDBi54559
    54560 [P29375-2]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000399788; ENSP00000382688; ENSG00000073614 [P29375-1]
    GeneIDi5927
    KEGGihsa:5927
    UCSCiuc001qif.3 human [P29375-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    5927
    DisGeNETi5927
    EuPathDBiHostDB:ENSG00000073614.11

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    KDM5A

    H-Invitational Database, human transcriptome db

    More...
    H-InvDBi
    HIX0010308
    HGNCiHGNC:9886 KDM5A
    HPAiHPA006201
    MIMi180202 gene
    neXtProtiNX_P29375
    OpenTargetsiENSG00000073614
    PharmGKBiPA34250

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1246 Eukaryota
    ENOG410XR9J LUCA
    GeneTreeiENSGT00940000157170
    HOGENOMiHOG000290719
    InParanoidiP29375
    KOiK11446
    OMAiPICDWRV
    PhylomeDBiP29375
    TreeFamiTF106476

    Enzyme and pathway databases

    ReactomeiR-HSA-3214842 HDMs demethylate histones
    SIGNORiP29375

    Miscellaneous databases

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

    More...
    ChiTaRSi
    KDM5A human
    EvolutionaryTraceiP29375

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    JARID1A

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

    More...
    GenomeRNAii
    5927

    Protein Ontology

    More...
    PROi
    PR:P29375

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000073614 Expressed in 244 organ(s), highest expression level in peritoneum
    CleanExiHS_JARID1A
    HS_RBP2
    ExpressionAtlasiP29375 baseline and differential
    GenevisibleiP29375 HS

    Family and domain databases

    Gene3Di1.10.150.60, 1 hit
    3.30.40.10, 2 hits
    InterProiView protein in InterPro
    IPR001606 ARID_dom
    IPR036431 ARID_dom_sf
    IPR003347 JmjC_dom
    IPR003349 JmjN
    IPR013637 Lys_sp_deMease-like_dom
    IPR019786 Zinc_finger_PHD-type_CS
    IPR004198 Znf_C5HC2
    IPR011011 Znf_FYVE_PHD
    IPR001965 Znf_PHD
    IPR019787 Znf_PHD-finger
    IPR013083 Znf_RING/FYVE/PHD
    PfamiView protein in Pfam
    PF01388 ARID, 1 hit
    PF02373 JmjC, 1 hit
    PF02375 JmjN, 1 hit
    PF00628 PHD, 2 hits
    PF08429 PLU-1, 1 hit
    PF02928 zf-C5HC2, 1 hit
    SMARTiView protein in SMART
    SM00501 BRIGHT, 1 hit
    SM00558 JmjC, 1 hit
    SM00545 JmjN, 1 hit
    SM00249 PHD, 3 hits
    SUPFAMiSSF46774 SSF46774, 1 hit
    SSF57903 SSF57903, 3 hits
    PROSITEiView protein in PROSITE
    PS51011 ARID, 1 hit
    PS51184 JMJC, 1 hit
    PS51183 JMJN, 1 hit
    PS01359 ZF_PHD_1, 2 hits
    PS50016 ZF_PHD_2, 3 hits

    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 nameiKDM5A_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: P29375
    Secondary accession number(s): A8MV76, Q4LE72, Q86XZ1
    <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 annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: November 25, 2008
    Last modified: December 5, 2018
    This is version 188 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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