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Q99P96

- HDAC7_RAT

UniProt

Q99P96 - HDAC7_RAT

Protein

Histone deacetylase 7

Gene

Hdac7

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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 factors such as MEF2A, MEF2B and 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.

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: UniProtKB
    2. histone deacetylase activity Source: UniProtKB
    3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    5. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    7. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. B cell activation Source: UniProtKB
    2. B cell differentiation Source: UniProtKB
    3. chromatin modification Source: UniProtKB
    4. chromatin organization Source: UniProtKB
    5. histone deacetylation Source: GOC
    6. inflammatory response Source: UniProtKB
    7. negative regulation of striated muscle tissue development Source: UniProtKB
    8. negative regulation of transcription, DNA-templated Source: UniProtKB
    9. nervous system development Source: UniProtKB
    10. 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 7 (EC:3.5.1.98)
    Short name:
    HD7
    Alternative name(s):
    Histone deacetylase 7A
    Short name:
    HD7a
    Gene namesi
    Name:Hdac7
    Synonyms:Hdac7a
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi619982. Hdac7.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity
    Note: In the nucleus, it associates with distinct subnuclear dot-like structures. 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 the 14-3-3 protein YWHAE and is due to its phosphorylation By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›238›238Histone deacetylase 7PRO_0000114707Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei118 – 1181PhosphoserineBy similarity
    Modified residuei164 – 1641Phosphoserine; by MARK2, MARK3 and PKD/PRKD1By similarity
    Modified residuei190 – 1901Phosphoserine; by PKD/PRKD2By similarity

    Post-translational modificationi

    May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-164 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-164 is a prerequisite for phosphorylation at Ser-190 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ99P96.

    Expressioni

    Gene expression databases

    GenevestigatoriQ99P96.

    Interactioni

    Subunit structurei

    Interacts with KAT5 and EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C. Interacts with KDM5B By similarity. Interacts with ZMYND15 By similarity. Interacts with PML By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000011322.

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000232065.

    Family and domain databases

    InterProiIPR000286. His_deacetylse.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    Q99P96-1 [UniParc]FASTAAdd to Basket

    « Hide

    TPGSQPQPMD LRVGQRPTVE PPPEPALLTL QHPQRLHRHL FLAGLQQQQR    50
    SAEPMRLSMD PPLPELQGGQ QEQELRQLLN KDKSKRSAVA SSVVKQKLAE 100
    VILKKQQAAL ERTVHPSSPS IPYRTLEPLD TEGAARSVLS SFLPPVPSLP 150
    TEPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES APPSLRRRPA 200
    ETLGDSSPSS SSTPASGCSS PNDSEHGPNP ALGSEADG 238
    Length:238
    Mass (Da):26,101
    Last modified:June 1, 2001 - v1
    Checksum:iB8869B96FBD040C5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei238 – 2381

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF321135 mRNA. Translation: AAK11188.1.
    UniGeneiRn.203327.

    Genome annotation databases

    UCSCiRGD:619982. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF321135 mRNA. Translation: AAK11188.1 .
    UniGenei Rn.203327.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000011322.

    Chemistry

    ChEMBLi CHEMBL2095943.

    Proteomic databases

    PaxDbi Q99P96.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:619982. rat.

    Organism-specific databases

    RGDi 619982. Hdac7.

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000232065.

    Gene expression databases

    Genevestigatori Q99P96.

    Family and domain databases

    InterProi IPR000286. His_deacetylse.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Expression pattern of rat histone deacetylases."
      Wilquet V., Chavez M., Korbers R., Geerts A.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Testis.

    Entry informationi

    Entry nameiHDAC7_RAT
    AccessioniPrimary (citable) accession number: Q99P96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3