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Q0VCB2

- HDAC8_BOVIN

UniProt

Q0VCB2 - HDAC8_BOVIN

Protein

Histone deacetylase 8

Gene

HDAC8

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      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. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 divalent metal cation per subunit.

    Enzyme regulationi

    Its activity is inhibited by trichostatin A (TSA) and butyrate, 2 well known histone deacetylase inhibitors.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei101 – 1011SubstrateBy similarity
    Active sitei143 – 1431Proton acceptorBy similarity
    Binding sitei151 – 1511Substrate; via carbonyl oxygenBy similarity
    Metal bindingi178 – 1781Divalent metal cationBy similarity
    Metal bindingi180 – 1801Divalent metal cationBy similarity
    Metal bindingi267 – 2671Divalent metal cationBy similarity
    Binding sitei306 – 3061SubstrateBy 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 cohesin localization to chromatin Source: UniProtKB
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. sister chromatid cohesion Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 8 (EC:3.5.1.98)
    Short name:
    HD8
    Gene namesi
    Name:HDAC8
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Histone deacetylase 8PRO_0000389507Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Interacts with CBFA2T3 By similarity. Interacts with phosphorylated SMG5/EST1B; this interaction protects SMG5 from ubiquitin-mediated degradation. Associates with alpha-SMA (smooth muscle alpha-actin).By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ0VCB2.
    SMRiQ0VCB2. Positions 14-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 324311Histone deacetylaseBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG057112.
    KOiK11405.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR003084. His_deacetylse_1.
    IPR023801. His_deacetylse_dom.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
    PRINTSiPR01270. HDASUPER.
    PR01271. HISDACETLASE.

    Sequencei

    Sequence statusi: Complete.

    Q0VCB2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEESEEPADA GQSLPPVYIY SPEYVSVCDS LAKVPKRASM VHSLIEAYAL    50
    HKQMRIVKPK VASMEEMASF HTDAYLQHLQ KVSEDGDDDH PDSIEYGLGY 100
    DCPATEGIFD YAAAVGGATI TAAQCLIDGM CKVAINWSGG WHHAKKDEAS 150
    GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL 200
    HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDCIQDERY YHICESVLKE 250
    VYIAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWELATLI 300
    LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP 350
    SCRPDRNEPH RVQQILNYIK GNLKHVV 377
    Length:377
    Mass (Da):41,683
    Last modified:September 5, 2006 - v1
    Checksum:i1120A71660F14E7D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC120257 mRNA. Translation: AAI20258.1.
    RefSeqiNP_001069699.1. NM_001076231.2.
    UniGeneiBt.90254.

    Genome annotation databases

    GeneIDi540666.
    KEGGibta:540666.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC120257 mRNA. Translation: AAI20258.1 .
    RefSeqi NP_001069699.1. NM_001076231.2.
    UniGenei Bt.90254.

    3D structure databases

    ProteinModelPortali Q0VCB2.
    SMRi Q0VCB2. Positions 14-377.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 540666.
    KEGGi bta:540666.

    Organism-specific databases

    CTDi 55869.

    Phylogenomic databases

    HOVERGENi HBG057112.
    KOi K11405.

    Miscellaneous databases

    NextBioi 20878759.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR003084. His_deacetylse_1.
    IPR023801. His_deacetylse_dom.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037913. His_deacetylse_1. 1 hit.
    PRINTSi PR01270. HDASUPER.
    PR01271. HISDACETLASE.
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Thymus.

    Entry informationi

    Entry nameiHDAC8_BOVIN
    AccessioniPrimary (citable) accession number: Q0VCB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 24, 2009
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 49 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3