Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 129 (07 Oct 2020)
Sequence version 1 (01 Oct 2002)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Bifunctional peptidase and arginyl-hydroxylase JMJD5

Gene

KDM8

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

Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monoxygenase (PubMed:28847961, PubMed:29459673, PubMed:28982940, PubMed:29563586). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (PubMed:28847961, PubMed:29459673, PubMed:28982940). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961, PubMed:29459673). Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage (PubMed:28982940). Additionnally, acts as Fe2+ and 2-oxoglutarate-dependent monoxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established (PubMed:29563586). Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation (PubMed:24981860). Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition (PubMed:24740926). Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation (PubMed:20457893). Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition (PubMed:28455245). Regulates the circadian gene expression in the liver (By similarity). Represses the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer in a catalytically-independent manner (PubMed:30500822). Negatively regulates the protein stability and function of CRY1; required for AMPK-FBXL3-induced CRY1 degradation (PubMed:30500822).By similarity9 Publications

Caution

The demethylase activity of JMJD5 is controversial. Demethylase activity toward H3K36me2 was observed in vivo and in vitro (PubMed:20457893). In addition, demethylase activity toward H3K36me3 when in a complex with RCCD1 has been observed (PubMed:24981860). In contrast, in other studies, JMJD5 was shown not to display any demethylase activity toward methylated H3K36 nor toward other methyllysines in the N-terminal tails of H3 and H4 in vitro (PubMed:28982940, PubMed:22851697, PubMed:24100311).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Fe2+3 PublicationsNote: Binds 1 Fe2+ ion per subunit.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

KM>300 µM for ARG-141 of RCCD1.1 Publication
  1. KM=60.4 µM for ARG-137 of RPS61 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei238N(omega)-methyl-L-arginine1 Publication1
    Binding sitei2722-oxoglutarateCombined sources1 Publication3 Publications1
    Binding sitei275N(omega)-methyl-L-arginine and symmetrical N(omega),N'(omega)-dimethyl-L-arginine binding1 Publication1
    Binding sitei3182-oxoglutarateCombined sources1 Publication3 Publications1
    Binding sitei318N(omega)-methyl-L-arginine and symmetrical N(omega),N'(omega)-dimethyl-L-arginine binding; via carbonyl oxygen1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi321Iron; catalyticPROSITE-ProRule annotationCombined sources2 Publications1
    Binding sitei3212-oxoglutarate1 Publication1
    Metal bindingi323Iron; catalyticPROSITE-ProRule annotationCombined sources2 Publications1
    Binding sitei3272-oxoglutarateCombined sources1 Publication3 Publications1
    Binding sitei3362-oxoglutarateCombined sources1 Publication3 Publications1
    Metal bindingi400Iron; catalyticPROSITE-ProRule annotationCombined sources2 Publications1
    Binding sitei4002-oxoglutarate1 Publication1
    Binding sitei4142-oxoglutarateCombined sources3 Publications1

    <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 functionAminopeptidase, Chromatin regulator, Dioxygenase, Hydrolase, Oxidoreductase, Protease
    Biological processBiological rhythms, Cell cycle, Transcription, Transcription regulation
    LigandIron, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:ENSG00000155666-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.11.27, 2681

    Pathway Commons web resource for biological pathway data

    More...
    PathwayCommonsi
    Q8N371

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Bifunctional peptidase and arginyl-hydroxylase JMJD53 Publications (EC:1.14.11.-1 Publication, EC:3.4.-.-2 Publications)
    Alternative name(s):
    JmjC domain-containing protein 51 Publication
    Jumonji C domain-containing protein 51 Publication
    L-arginine (3R)-hydroxylase KDM81 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:KDM82 PublicationsImported
    Synonyms:JMJD53 Publications
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 16

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000155666.11

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:25840, KDM8

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    611917, gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q8N371

    <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

    Chromosome, 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1 – 182Missing : No effect on L-arginyl 3-hydroxylase activity toward RPS6. 1 PublicationAdd BLAST182
    Mutagenesisi238E → A: Loss of L-arginyl 3-hydroxylase activity toward RPS6. 1 Publication1
    Mutagenesisi243Y → A: Loss of L-arginyl 3-hydroxylase activity toward RPS6. 1 Publication1
    Mutagenesisi275Q → A: Loss of L-arginyl 3-hydroxylase activity toward RPS6. Loss of peptidase activity toward methylated histones. 2 Publications1
    Mutagenesisi310W → A: Loss of L-arginyl 3-hydroxylase activity toward RPS6. 1 Publication1
    Mutagenesisi321 – 323HQD → AQA: Fails to cleave H3C1. 1 Publication3
    Mutagenesisi321H → A: Loss of H3K36me2 demethylase activity. 1 Publication1
    Mutagenesisi321H → A: Loss of L-arginyl 3-hydroxylase activity toward RPS6. Loss of peptidase activity toward methylated histones; when associated with A-323 and A-400. No effect on its regulatory function on the circadian clock or CRY1 stability. 3 Publications1
    Mutagenesisi323D → A: Loss of peptidase activity toward methylated histones; when associated with A-321 and A-400. 1 Publication1
    Mutagenesisi335 – 336RK → AA: Loss of interaction with H3C1. Fails to cleave H3C1. 1 Publication2
    Mutagenesisi336K → E: Loss of peptidase activity toward methylated histones. 1 Publication1
    Mutagenesisi356L → A: Reduces L-arginyl 3-hydroxylase activity toward RPS6 substrate. 1 Publication1
    Mutagenesisi398 – 400YWH → AAA: Fails to cleave H3C1. 1 Publication3
    Mutagenesisi400H → A: Loss of peptidase activity toward methylated histones; when associated with A-321 and A-323. 1 Publication1
    Mutagenesisi414W → A: Reduces L-arginyl 3-hydroxylase activity toward RPS6. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    79831

    Open Targets

    More...
    OpenTargetsi
    ENSG00000155666

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA143485510

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q8N371, Tbio

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    KDM8

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    74728780

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002920101 – 416Bifunctional peptidase and arginyl-hydroxylase JMJD5Add BLAST416

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q8N371

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q8N371

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q8N371

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q8N371

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

    More...
    PaxDbi
    Q8N371

    PeptideAtlas

    More...
    PeptideAtlasi
    Q8N371

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q8N371

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    71772 [Q8N371-1]
    71773 [Q8N371-2]
    71774 [Q8N371-3]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q8N371

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

    More...
    PhosphoSitePlusi
    Q8N371

    <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

    Weakly expressed in most cells. Highly expressed in breast cancer cells (PubMed:20457893). Expressed in embryonic stem cells (PubMed:24740926).2 Publications

    <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

    Up-regulated upon starvation, DNA replication stress, UV treatment and by camptothecin and etoposide treatment.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000155666, Expressed in right lobe of liver and 168 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q8N371, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q8N371, HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000155666, Tissue enhanced (liver)

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Can form homodimers (via JmjC domain) (PubMed:24100311, PubMed:28982940).

    Found in a complex with RCCD1 (PubMed:24981860).

    Interacts (via N-terminus) with RCCD1 (via N-terminus); this interaction stimulates H3K36me3 and H3K36me2 demethylation (PubMed:28455245, PubMed:24981860).

    Interacts (via JmjC domain) with H3C1 (PubMed:28982940).

    Interacts with FBXL3 and PSMD2 (By similarity).

    Interacts with CRY1 in a FBXL3-dependent manner (By similarity).

    By similarity4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    122923, 16 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q8N371

    Protein interaction database and analysis system

    More...
    IntActi
    Q8N371, 10 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000398410

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    Q8N371, protein

    <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

    1416
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    Q8N371

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <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%5Fand%5Fdomains%5Fsection">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>Domaini271 – 416JmjCPROSITE-ProRule annotationAdd BLAST146

    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>Regioni1 – 110Interaction with RCCD11 PublicationAdd BLAST110

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2132, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000158074

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_016785_0_3_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q8N371

    KEGG Orthology (KO)

    More...
    KOi
    K10277

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    ANHWPCM

    Database of Orthologous Groups

    More...
    OrthoDBi
    1385616at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q8N371

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF315056

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR041667, Cupin_8
    IPR003347, JmjC_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF13621, Cupin_8, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00558, JmjC, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51184, JMJC, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 3 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q8N371-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MAGDTHCPAE PLAREGTLWE ALRALLPHSK EDLKLDLGEK VERSVVTLLQ
    60 70 80 90 100
    RATELFYEGR RDECLQSSEV ILDYSWEKLN TGTWQDVDKD WRRVYAIGCL
    110 120 130 140 150
    LKALCLCQAP EDANTVAAAL RVCDMGLLMG AAILGDILLK VAAILQTHLP
    160 170 180 190 200
    GKRPARGSLP EQPCTKKARA DHGLIPDVKL EKTVPRLHRP SLQHFREQFL
    210 220 230 240 250
    VPGRPVILKG VADHWPCMQK WSLEYIQEIA GCRTVPVEVG SRYTDEEWSQ
    260 270 280 290 300
    TLMTVNEFIS KYIVNEPRDV GYLAQHQLFD QIPELKQDIS IPDYCSLGDG
    310 320 330 340 350
    EEEEITINAW FGPQGTISPL HQDPQQNFLV QVMGRKYIRL YSPQESGALY
    360 370 380 390 400
    PHDTHLLHNT SQVDVENPDL EKFPKFAKAP FLSCILSPGE ILFIPVKYWH
    410
    YVRALDLSFS VSFWWS
    Length:416
    Mass (Da):47,270
    Last modified:October 1, 2002 - v1
    <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:i18CE6D01E00ED5A4
    GO
    Isoform 2 (identifier: Q8N371-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         167-362: Missing.

    Show »
    Length:220
    Mass (Da):24,686
    Checksum:i3B9B54CCB843C8CD
    GO
    Isoform 3 (identifier: Q8N371-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSREKCSPGEGAEEGRGSEASGLKASAGHGTEPAGGGPM

    Show »
    Length:454
    Mass (Da):50,852
    Checksum:iB7F33C98121DC9F1
    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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    H3BPT5H3BPT5_HUMAN
    Bifunctional peptidase and arginyl-...
    KDM8
    90Annotation 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>
    H3BR76H3BR76_HUMAN
    Bifunctional peptidase and arginyl-...
    KDM8
    163Annotation 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>
    H3BM39H3BM39_HUMAN
    Bifunctional peptidase and arginyl-...
    KDM8
    120Annotation 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 conflicti73D → G in BAB14706 (PubMed:14702039).Curated1

    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_032928302E → D. Corresponds to variant dbSNP:rs34445573Ensembl.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0398931M → MSREKCSPGEGAEEGRGSEA SGLKASAGHGTEPAGGGPM in isoform 3. 1 Publication1
    Alternative sequenceiVSP_026370167 – 362Missing in isoform 2. 1 PublicationAdd BLAST196

    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
    AK023860 mRNA Translation: BAB14706.1
    AK297166 mRNA Translation: BAG59661.1
    AY345239 mRNA Translation: AAQ23080.1
    AC092725 Genomic DNA No translation available.
    AC106739 Genomic DNA No translation available.
    AC109449 Genomic DNA No translation available.
    BC027911 mRNA Translation: AAH27911.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS10627.1 [Q8N371-1]
    CCDS45448.1 [Q8N371-3]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001138820.1, NM_001145348.1 [Q8N371-3]
    NP_079049.2, NM_024773.2 [Q8N371-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000286096; ENSP00000286096; ENSG00000155666 [Q8N371-1]
    ENST00000441782; ENSP00000398410; ENSG00000155666 [Q8N371-3]
    ENST00000568965; ENSP00000456901; ENSG00000155666 [Q8N371-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    79831

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:79831

    UCSC genome browser

    More...
    UCSCi
    uc002doh.3, human [Q8N371-1]

    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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK023860 mRNA Translation: BAB14706.1
    AK297166 mRNA Translation: BAG59661.1
    AY345239 mRNA Translation: AAQ23080.1
    AC092725 Genomic DNA No translation available.
    AC106739 Genomic DNA No translation available.
    AC109449 Genomic DNA No translation available.
    BC027911 mRNA Translation: AAH27911.1
    CCDSiCCDS10627.1 [Q8N371-1]
    CCDS45448.1 [Q8N371-3]
    RefSeqiNP_001138820.1, NM_001145348.1 [Q8N371-3]
    NP_079049.2, NM_024773.2 [Q8N371-1]

    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
    3UYJX-ray2.35A/B173-416[»]
    4AAPX-ray2.60A/B180-416[»]
    4GAZX-ray2.81A/B176-416[»]
    4GJYX-ray1.25A183-416[»]
    4GJZX-ray1.05A183-416[»]
    4QU1X-ray1.57A183-416[»]
    5FBJX-ray2.42A183-416[»]
    6AVSX-ray2.02A183-416[»]
    6AX3X-ray2.25A184-416[»]
    6F4MX-ray1.71A183-416[»]
    6F4NX-ray2.54A/B153-416[»]
    6F4OX-ray1.28A183-416[»]
    6F4PX-ray1.45A183-416[»]
    6F4QX-ray1.12A183-416[»]
    6F4RX-ray1.30A183-416[»]
    6F4SX-ray1.46A183-416[»]
    6F4TX-ray1.22A183-416[»]
    6I9LX-ray1.53A183-416[»]
    6I9MX-ray1.65A183-416[»]
    6I9NX-ray1.36A183-416[»]
    SMRiQ8N371
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi122923, 16 interactors
    CORUMiQ8N371
    IntActiQ8N371, 10 interactors
    STRINGi9606.ENSP00000398410

    PTM databases

    iPTMnetiQ8N371
    PhosphoSitePlusiQ8N371

    Polymorphism and mutation databases

    BioMutaiKDM8
    DMDMi74728780

    Proteomic databases

    EPDiQ8N371
    jPOSTiQ8N371
    MassIVEiQ8N371
    MaxQBiQ8N371
    PaxDbiQ8N371
    PeptideAtlasiQ8N371
    PRIDEiQ8N371
    ProteomicsDBi71772 [Q8N371-1]
    71773 [Q8N371-2]
    71774 [Q8N371-3]

    Protocols and materials databases

    ABCD curated depository of sequenced antibodies

    More...
    ABCDi
    Q8N371, 1 sequenced antibody

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    12808, 291 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    79831

    Genome annotation databases

    EnsembliENST00000286096; ENSP00000286096; ENSG00000155666 [Q8N371-1]
    ENST00000441782; ENSP00000398410; ENSG00000155666 [Q8N371-3]
    ENST00000568965; ENSP00000456901; ENSG00000155666 [Q8N371-2]
    GeneIDi79831
    KEGGihsa:79831
    UCSCiuc002doh.3, human [Q8N371-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    79831
    DisGeNETi79831
    EuPathDBiHostDB:ENSG00000155666.11

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    KDM8
    HGNCiHGNC:25840, KDM8
    HPAiENSG00000155666, Tissue enhanced (liver)
    MIMi611917, gene
    neXtProtiNX_Q8N371
    OpenTargetsiENSG00000155666
    PharmGKBiPA143485510

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2132, Eukaryota
    GeneTreeiENSGT00940000158074
    HOGENOMiCLU_016785_0_3_1
    InParanoidiQ8N371
    KOiK10277
    OMAiANHWPCM
    OrthoDBi1385616at2759
    PhylomeDBiQ8N371
    TreeFamiTF315056

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000155666-MONOMER
    BRENDAi1.14.11.27, 2681
    PathwayCommonsiQ8N371

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    79831, 330 hits in 886 CRISPR screens

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

    More...
    ChiTaRSi
    KDM8, human

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

    More...
    GenomeRNAii
    79831
    PharosiQ8N371, Tbio

    Protein Ontology

    More...
    PROi
    PR:Q8N371
    RNActiQ8N371, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000155666, Expressed in right lobe of liver and 168 other tissues
    ExpressionAtlasiQ8N371, baseline and differential
    GenevisibleiQ8N371, HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR041667, Cupin_8
    IPR003347, JmjC_dom
    PfamiView protein in Pfam
    PF13621, Cupin_8, 1 hit
    SMARTiView protein in SMART
    SM00558, JmjC, 1 hit
    PROSITEiView protein in PROSITE
    PS51184, JMJC, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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 nameiKDM8_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: Q8N371
    Secondary accession number(s): B4DLU9, Q6VAK5, Q9H8B1
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: October 1, 2002
    Last modified: October 7, 2020
    This is version 129 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again