Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Z2V6

- HDAC5_MOUSE

UniProt

Q9Z2V6 - HDAC5_MOUSE

Protein

Histone deacetylase 5

Gene

Hdac5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi687 – 6871ZincBy similarity
    Metal bindingi689 – 6891ZincBy similarity
    Metal bindingi695 – 6951ZincBy similarity
    Metal bindingi772 – 7721ZincBy similarity
    Active sitei824 – 8241By similarity

    GO - Molecular functioni

    1. core promoter sequence-specific DNA binding Source: UniProtKB
    2. histone deacetylase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    5. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    7. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    8. protein binding Source: UniProtKB
    9. protein kinase binding Source: UniProtKB
    10. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
    11. RNA polymerase II transcription factor binding Source: BHF-UCL
    12. transcription corepressor activity Source: MGI
    13. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. B cell activation Source: UniProtKB
    2. B cell differentiation Source: UniProtKB
    3. cellular response to fluid shear stress Source: UniProtKB
    4. chromatin modification Source: UniProtKB
    5. heart development Source: MGI
    6. histone deacetylation Source: GOC
    7. inflammatory response Source: UniProtKB
    8. multicellular organismal response to stress Source: MGI
    9. negative regulation of osteoblast differentiation Source: MGI
    10. negative regulation of striated muscle tissue development Source: UniProtKB
    11. negative regulation of transcription, DNA-templated Source: UniProtKB
    12. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    13. nervous system development Source: UniProtKB
    14. osteoblast development Source: MGI
    15. positive regulation of neural precursor cell proliferation Source: BHF-UCL
    16. positive regulation of stem cell proliferation Source: BHF-UCL
    17. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    18. regulation of myotube differentiation Source: UniProtKB
    19. regulation of skeletal muscle fiber development Source: MGI
    20. regulation of striated muscle cell differentiation Source: MGI
    21. renal tubule morphogenesis Source: UniProtKB
    22. response to cocaine Source: MGI

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 5 (EC:3.5.1.98)
    Short name:
    HD5
    Alternative name(s):
    Histone deacetylase mHDA1
    Gene namesi
    Name:Hdac5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1333784. Hdac5.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-250 and Ser-488 by AMPK, CaMK1 and SIK1.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: MGI
    3. histone deacetylase complex Source: UniProtKB
    4. nuclear body Source: MGI
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi250 – 2501S → A: Abolishes phosphorylation by SIK1 and fails to promote beta-catenin expression; when associated with A-488. 2 Publications
    Mutagenesisi488 – 4881S → A: Abolishes phosphorylation by SIK1 and fails to promote beta-catenin expression; when associated with A-250. 2 Publications
    Mutagenesisi824 – 8241H → A: Abolishes deacetylase activity. 1 Publication
    Mutagenesisi884 – 8841H → F: Disrupts the dot-like nuclear pattern. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11131113Histone deacetylase 5PRO_0000114702Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei250 – 2501Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD13 Publications
    Modified residuei283 – 2831Phosphothreonine; by PKCBy similarity
    Modified residuei488 – 4881Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD13 Publications
    Modified residuei523 – 5231N6-acetyllysineBy similarity
    Modified residuei650 – 6501PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-250 and Ser-488. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import By similarity. Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription.By similarity3 Publications
    Ubiquitinated. Polyubiquitination however does not lead to its degradation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9Z2V6.
    PRIDEiQ9Z2V6.

    PTM databases

    PhosphoSiteiQ9Z2V6.

    Expressioni

    Gene expression databases

    CleanExiMM_HDAC5.
    GenevestigatoriQ9Z2V6.

    Interactioni

    Subunit structurei

    Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts with EP300 in the presence of TFAP2C.8 Publications

    Protein-protein interaction databases

    DIPiDIP-40855N.
    IntActiQ9Z2V6. 4 interactions.
    MINTiMINT-125422.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2V6.
    SMRiQ9Z2V6. Positions 68-132, 672-1052.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni675 – 1019345Histone deacetylaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1072 – 111342Nuclear export signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi47 – 526Poly-Gly
    Compositional biasi85 – 928Poly-Gln
    Compositional biasi577 – 58812Poly-GluAdd
    BLAST

    Domaini

    The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    HOVERGENiHBG057100.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF12203. HDAC4_Gln. 1 hit.
    PF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSiPR01270. HDASUPER.

    Sequencei

    Sequence statusi: Complete.

    Q9Z2V6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSPNESDGM SGREPSLGIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG     50
    GGSPSPVELR GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK 100
    QHDHLTRQHE VQLQKHLKQQ QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR 150
    LEQQLLILRN KEKSKESAIA STEVKLRLQE FLLSKSKEPT PGGLNHSLPQ 200
    HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR DDFPLRKTAS 250
    EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS 300
    VCNSAPGSGP SSPNSSHSTI AENGFTGSVP NIPTEMIPQH RALPLDSSPN 350
    QFSLYTSPSL PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ 400
    GGTLTGKFMS TSSIPGCLLG VALEGDTSPH GHASLLQHVC SWTGRQQSTL 450
    IAVPLHGQSP LVTGERVATS MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ 500
    LVMQQQHQQF LEKQKQQQMQ LGKILTKTGE LSRQPTTHPE ETEEELTEQQ 550
    EALLGEGALT IPREGSTESE STQEDLEEEE EEEEEEEEDC IQVKDEDGES 600
    GPDEGPDLEE SSAGYKKLFA DAQQLQPLQV YQAPLSLATV PHQALGRTQS 650
    SPAAPGSMKS PTDQPTVVKH LFTTGVVYDT FMLKHQCMCG NTHVHPEHAG 700
    RIQSIWSRLQ ETGLLGKCER IRGRKATLDE IQTVHSEYHT LLYGTSPLNR 750
    QKLDSKKLLG PISQKMYAML PCGGIGVDSD TVWNEMHSSS AVRMAVGCLV 800
    ELAFKVAAGE LKNGFAIIRP PGHHAEESTA MGFCFFNSVA ITAKLLQQKL 850
    SVGKVLIVDW DIHHGNGTQQ AFYNDPSVLY ISLHRYDNGN FFPGSGAPEE 900
    VGGGPGVGYN VNVAWTGGVD PPIGDVEYLT AFRTVVMPIA QEFSPDVVLV 950
    SAGFDAVEGH LSPLGGYSVT ARCFGHLTRQ LMTLAGGRVV LALEGGHDLT 1000
    AICDASEACV SALLSVELQP LDEAVLQQKP SVNAVATLEK VIEIQSKHWS 1050
    CVQRFAAGLG CSLREAQTGE KEEAETVSAM ALLSVGAEQA QAVATQEHSP 1100
    RPAEEPMEQE PAL 1113
    Length:1,113
    Mass (Da):120,942
    Last modified:May 1, 2000 - v2
    Checksum:i63071AF45B87815A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71S → SA in AAF31418. (PubMed:10640276)Curated
    Sequence conflicti18 – 181G → E in AAF31418. (PubMed:10640276)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006602 mRNA. Translation: AAD09834.2.
    AF207748 mRNA. Translation: AAF31418.1.
    UniGeneiMm.22665.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006602 mRNA. Translation: AAD09834.2 .
    AF207748 mRNA. Translation: AAF31418.1 .
    UniGenei Mm.22665.

    3D structure databases

    ProteinModelPortali Q9Z2V6.
    SMRi Q9Z2V6. Positions 68-132, 672-1052.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-40855N.
    IntActi Q9Z2V6. 4 interactions.
    MINTi MINT-125422.

    Chemistry

    BindingDBi Q9Z2V6.
    ChEMBLi CHEMBL2768.

    PTM databases

    PhosphoSitei Q9Z2V6.

    Proteomic databases

    PaxDbi Q9Z2V6.
    PRIDEi Q9Z2V6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:1333784. Hdac5.

    Phylogenomic databases

    eggNOGi COG0123.
    HOVERGENi HBG057100.

    Miscellaneous databases

    ChiTaRSi HDAC5. mouse.
    PROi Q9Z2V6.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_HDAC5.
    Genevestigatori Q9Z2V6.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF12203. HDAC4_Gln. 1 hit.
    PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSi PR01270. HDASUPER.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers."
      Verdel A., Khochbin S.
      J. Biol. Chem. 274:2440-2445(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Fetus.
    2. "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression."
      Kao H.-Y., Downes M., Ordentlich P., Evans R.M.
      Genes Dev. 14:55-66(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NCOR2.
      Strain: C57BL/6.
    3. Cited for: INTERACTION WITH HDAC7, NUCLEAR EXPORT, MUTAGENESIS OF HIS-824 AND HIS-884.
    4. "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor."
      Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.
      J. Biol. Chem. 276:35-39(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTBP1 AND HDAC9.
    5. "Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases."
      Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V., Seiser C.
      J. Biol. Chem. 279:24834-24843(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHB2.
    6. "Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition."
      Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V.
      Nucleic Acids Res. 32:1957-1966(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NRIP1.
    7. "Modulation of smooth muscle gene expression by association of histone acetyltransferases and deacetylases with myocardin."
      Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A., Wang D.Z., Olson E.N.
      Mol. Cell. Biol. 25:364-376(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYOCD.
    8. "SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes."
      Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T., Shelton G.D., Montminy M.
      Nat. Med. 13:597-603(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-250 AND SER-488, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-250 AND SER-488.
    9. "Molecular mechanism of transcriptional repression of AhR repressor involving ANKRA2, HDAC4, and HDAC5."
      Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.
      Biochem. Biophys. Res. Commun. 364:276-282(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AHRR.
    10. "Uncovering G protein-coupled receptor kinase-5 as a histone deacetylase kinase in the nucleus of cardiomyocytes."
      Martini J.S., Raake P., Vinge L.E., DeGeorge B.R. Jr., Chuprun J.K., Harris D.M., Gao E., Eckhart A.D., Pitcher J.A., Koch W.J.
      Proc. Natl. Acad. Sci. U.S.A. 105:12457-12462(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRK5, PHOSPHORYLATION.
    11. "AMP-activated protein kinase regulates beta-catenin transcription via histone deacetylase 5."
      Zhao J.X., Yue W.F., Zhu M.J., Du M.
      J. Biol. Chem. 286:16426-16434(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-250 AND SER-488, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-250 AND SER-488.

    Entry informationi

    Entry nameiHDAC5_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2V6
    Secondary accession number(s): Q9JL73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3