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Q9YGY4

- HDAC9_XENLA

UniProt

Q9YGY4 - HDAC9_XENLA

Protein

Histone deacetylase 9

Gene

hdac9

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting other histone deacetylases. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription.1 Publication

    Catalytic activityi

    Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

    GO - Molecular functioni

    1. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    2. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    3. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 9 (EC:3.5.1.98)
    Alternative name(s):
    Histone deacetylase-related protein
    MEF2-interacting transcription repressor MITR
    Gene namesi
    Name:hdac9
    Synonyms:hdrp, mitr
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-865808. hdac9.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 596596Histone deacetylase 9PRO_0000280538Add
    BLAST

    Expressioni

    Tissue specificityi

    Broadly expressed.1 Publication

    Developmental stagei

    Broadly expressed at low levels at all stages.1 Publication

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with mef2.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi97196. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9YGY4.
    SMRiQ9YGY4. Positions 64-131.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni172 – 22251Interaction with mef2Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG057100.
    KOiK11409.

    Family and domain databases

    InterProiIPR000286. His_deacetylse.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF12203. HDAC4_Gln. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9YGY4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLQTIYESES YFSSDGVAGR EQLLAEQRMH AMIGKDIKSE FPIGLESISP    50
    LDLRTDLRTA VPVGDPGLRE KQLQQELLII KQQQQIQKQL LIAEFQKQHE 100
    NLTRQHQVQL QEHLKLQQEL LAMKQQQELL EREKEQKMEQ QRKEQEAERH 150
    RQEQQLCHPR SKDRVKERAV ASTEVKQKLQ EFILSKSATK EPLTNGTSHS 200
    MGRHPKLWYT AAHHTSLDQS SPPPSGTSPT YKCPPPGNQD DFPLRKTASE 250
    PNLKVRSRLK QKVVERRSSP LLRRKDSIVS SSYKKRIFEV AESSVSSSSP 300
    VSGPSSPNNG PVAMEAEHET PVLSVNSRIE NLVSHHHLVH HERSLSLLNL 350
    YTSPSLPNIT LGLHATATQL NTSSSLKEQQ KYDPQAPRQG VSMAGQYAGG 400
    IPTSSNHVSL EGKANSHQAI LQHLLLKEQM RQQKILASGG TPVLHQSPLA 450
    AKDRVSPAGR VAHKLPRHRP LHRTQSAPLP QSTLAQLVIQ QQHQQFLEKQ 500
    KQYQQQIHMN KILSKSIEQL RQPEGHLEEA EEDLHGDNLM QEKSSSIDNT 550
    RSYSSTDLRT GPFGSVKVKE EPPDSENEIK THLQSEQKSV FAQQVT 596
    Length:596
    Mass (Da):67,307
    Last modified:March 20, 2007 - v2
    Checksum:i4E4BD92BAC605E84
    GO

    Sequence cautioni

    The sequence CAB10167.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97214 mRNA. Translation: CAB10167.1. Different initiation.
    RefSeqiNP_001079307.1. NM_001085838.1.
    UniGeneiXl.227.

    Genome annotation databases

    GeneIDi378615.
    KEGGixla:378615.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97214 mRNA. Translation: CAB10167.1 . Different initiation.
    RefSeqi NP_001079307.1. NM_001085838.1.
    UniGenei Xl.227.

    3D structure databases

    ProteinModelPortali Q9YGY4.
    SMRi Q9YGY4. Positions 64-131.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 97196. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 378615.
    KEGGi xla:378615.

    Organism-specific databases

    CTDi 9734.
    Xenbasei XB-GENE-865808. hdac9.

    Phylogenomic databases

    HOVERGENi HBG057100.
    KOi K11409.

    Family and domain databases

    InterProi IPR000286. His_deacetylse.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF12203. HDAC4_Gln. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MEF2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
    2. "Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5."
      Zhou X., Richon V.M., Rifkind R.A., Marks P.A.
      Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiHDAC9_XENLA
    AccessioniPrimary (citable) accession number: Q9YGY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 55 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3