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Q80ZH1

- HDAC5_CRIGR

UniProt

Q80ZH1 - HDAC5_CRIGR

Protein

Histone deacetylase 5

Gene

HDAC5

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    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 bindingi685 – 6851ZincBy similarity
    Metal bindingi687 – 6871ZincBy similarity
    Metal bindingi693 – 6931ZincBy similarity
    Metal bindingi770 – 7701ZincBy similarity
    Active sitei822 – 8221By similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    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
    Gene namesi
    Name:HDAC5
    OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
    Taxonomic identifieri10029 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity
    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-489 by AMPK, CaMK1 and SIK1 By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. histone deacetylase complex Source: InterPro
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11111111Histone deacetylase 5PRO_0000357050Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei250 – 2501Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1By similarity
    Modified residuei283 – 2831Phosphothreonine; by PKCBy similarity
    Modified residuei489 – 4891Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1By similarity
    Modified residuei524 – 5241N6-acetyllysineBy similarity
    Modified residuei650 – 6501PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-250 and Ser-489. 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 similarity.By similarity
    Ubiquitinated. Polyubiquitination however does not lead to its degradation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ80ZH1.
    SMRiQ80ZH1. Positions 68-132, 670-1052.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni671 – 1017347Histone deacetylaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1070 – 110940Nuclear export signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi47 – 526Poly-Gly
    Compositional biasi85 – 928Poly-Gln
    Compositional biasi578 – 58811Poly-GluAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG057100.
    KOiK11406.

    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.

    Q80ZH1-1 [UniParc]FASTAAdd to Basket

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    MNSPNESDGM PGREPSLEIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG     50
    GGSPSPVELR GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK 100
    QHDHLTRQHE VQLQKHLKQQ QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR 150
    LEQQLLILRN KEKSKESAIA STEVKLRLQE FLLSKSKEPT PGSLNHSLPQ 200
    HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR DDFPLRKTAS 250
    EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS 300
    VCNSAPGSGP SSPNSSHSAI AENGFTGSVP NIPTEMLPQH RALPLDSSPN 350
    QFSLYTSPSL PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ 400
    GGTLTGKFMS TSSIPGCLLG VTLEGDTSPH GHASLLQHVL LLEQARQQST 450
    LIAVPLHGQS PLVTGERVAT SMRTVGKLPR HRPLSRTQSS PLPQSPQALQ 500
    QLVMQQQHQQ FLEKQKQQQM QLGKILTKTG ELPRQPTTHP EETEEELTEQ 550
    QEALLGEGAL TMPREGSTES ESTQEDLEEE EDEEEEDEDC IQVKDEEGES 600
    GPDEGPDLEE SSAGYKKLFT DAQQLQPLQV YQAPLSLATV PHQALGRTQS 650
    SPAAPGSMKS PPDQPTKHLF TTGVVYDTFM LKHQCMCGNT HVHPEHAGRI 700
    QSIWSRLQET GLLSKCERIR GRKATLDEIQ TVHSEYHTLL YGTSPLNRQK 750
    LDSKKLLGPI SQKMYAMLPC GGIGVDSDTV WNEMHSSSAV RMAVGCLVEL 800
    AFKVAAGELK NGFAIIRPPG HHAEESTAMG FCFFNSVAIT AKLLQQKLNV 850
    GKVLIVDWDI HHGNGTQQAF YDDPSVLYIS LHRYDNGNFF PGSGAPEEVG 900
    GGPGMGYNVN VAWTGGVDPP IGDVEYLTAF RTVVMPIAHE FSPDVVLVSA 950
    GFDAVEGHLS PLGGYSVTAR CFGHLTRQLM TLAGGRVVLA LEGGHDLTAI 1000
    CDASEACVSA LLSVELQPLD EAVLQQKPSI NAVATLEKVI EIQSKHWSCV 1050
    QRFATGLGCS LQEAQAGETE EAETVSAMAL LSVGAEQAQA VATQEHSPRP 1100
    AEEPMEQEPT L 1111
    Length:1,111
    Mass (Da):120,988
    Last modified:June 1, 2003 - v1
    Checksum:i52559AE959E190E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY145846 mRNA. Translation: AAN46420.1.
    RefSeqiNP_001233710.1. NM_001246781.1.
    XP_007643219.1. XM_007645029.1.

    Genome annotation databases

    GeneIDi100689350.
    KEGGicge:100689350.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY145846 mRNA. Translation: AAN46420.1 .
    RefSeqi NP_001233710.1. NM_001246781.1.
    XP_007643219.1. XM_007645029.1.

    3D structure databases

    ProteinModelPortali Q80ZH1.
    SMRi Q80ZH1. Positions 68-132, 670-1052.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100689350.
    KEGGi cge:100689350.

    Organism-specific databases

    CTDi 10014.

    Phylogenomic databases

    HOVERGENi HBG057100.
    KOi K11406.

    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. "Suppressors of alpha(1,3)fucosylation identified by expression cloning in the LEC11B gain-of-function CHO mutant."
      Chen W., Tang J., Stanley P.
      Glycobiology 15:259-269(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.

    Entry informationi

    Entry nameiHDAC5_CRIGR
    AccessioniPrimary (citable) accession number: Q80ZH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 64 of the entry and version 1 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