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Q4QQW4

- HDAC1_RAT

UniProt

Q4QQW4 - HDAC1_RAT

Protein

Histone deacetylase 1

Gene

Hdac1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation 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
    Active sitei141 – 1411By similarity

    GO - Molecular functioni

    1. deacetylase activity Source: UniProtKB
    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
    6. transcription regulatory region sequence-specific DNA binding Source: UniProtKB

    GO - Biological processi

    1. circadian regulation of gene expression Source: UniProtKB
    2. histone H4 deacetylation Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 1 (EC:3.5.1.98)
    Short name:
    HD1
    Gene namesi
    Name:Hdac1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 5

    Organism-specific databases

    RGDi619975. Hdac1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 482482Histone deacetylase 1PRO_0000304731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741N6-acetyllysineBy similarity
    Modified residuei220 – 2201N6-acetyllysineBy similarity
    Modified residuei393 – 3931Phosphoserine1 Publication
    Modified residuei421 – 4211PhosphoserineBy similarity
    Modified residuei423 – 4231PhosphoserineBy similarity
    Modified residuei432 – 4321N6-methylated lysine; by EHMT2By similarity
    Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki476 – 476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1 By similarity.By similarity
    Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5 By similarity.By similarity
    Ubiquitinated by CHFR and KCTD11, leading to its degradation by the proteasome.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ4QQW4.
    PRIDEiQ4QQW4.

    PTM databases

    PhosphoSiteiQ4QQW4.

    Expressioni

    Gene expression databases

    GenevestigatoriQ4QQW4.

    Interactioni

    Subunit structurei

    Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with the non-histone region of H2AFY. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Interacts with SP1; the interaction deacetylates SP1 and regulates its transcriptional activity. Interacts with SP3; the interaction deacetylates SP3 and regulates its transcriptional activity. In vitro, C(18) ceramides increase this interaction and the subsequent SP3 deacetylation and SP3-mediated repression of the TERT promoter. Interacts with TSHZ3 (via N-terminus); the interaction is direct. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with C10orf90/FATS (via its N-terminal); the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via C-terminus). Interacts with TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6, BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi255695. 5 interactions.
    IntActiQ4QQW4. 1 interaction.
    STRINGi10116.ENSRNOP00000012854.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4QQW4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni9 – 321313Histone deacetylaseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    GeneTreeiENSGT00530000062889.
    HOGENOMiHOG000225180.
    HOVERGENiHBG057112.
    InParanoidiQ4QQW4.
    KOiK06067.
    OMAiLRRDHQN.
    OrthoDBiEOG7DNNTW.
    PhylomeDBiQ4QQW4.
    TreeFamiTF106171.

    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.

    Q4QQW4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK    50
    MEIYRPHKAN AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC 100
    PVFDGLFEFC QLSTGGSVAS AVKLNKQQTD IAVNWAGGLH HAKKSEASGF 150
    CYVNDIVLAI LELLKYHQRV LYIDIDIHHG DGVEEAFYTT DRVMTVSFHK 200
    YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVMSKVME 250
    MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG 300
    GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM 350
    TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED 400
    PDKRISICSS DKRIACEEEF SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE 450
    KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK MA 482
    Length:482
    Mass (Da):55,093
    Last modified:July 19, 2005 - v1
    Checksum:i7F6563C17F5E4844
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC097943 mRNA. Translation: AAH97943.1.
    BC107476 mRNA. Translation: AAI07477.1.
    RefSeqiNP_001020580.1. NM_001025409.1.
    UniGeneiRn.1863.

    Genome annotation databases

    EnsembliENSRNOT00000012854; ENSRNOP00000012854; ENSRNOG00000009568.
    GeneIDi297893.
    KEGGirno:297893.
    UCSCiRGD:619975. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC097943 mRNA. Translation: AAH97943.1 .
    BC107476 mRNA. Translation: AAI07477.1 .
    RefSeqi NP_001020580.1. NM_001025409.1.
    UniGenei Rn.1863.

    3D structure databases

    ProteinModelPortali Q4QQW4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 255695. 5 interactions.
    IntActi Q4QQW4. 1 interaction.
    STRINGi 10116.ENSRNOP00000012854.

    Chemistry

    BindingDBi Q4QQW4.
    ChEMBLi CHEMBL2915.

    PTM databases

    PhosphoSitei Q4QQW4.

    Proteomic databases

    PaxDbi Q4QQW4.
    PRIDEi Q4QQW4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000012854 ; ENSRNOP00000012854 ; ENSRNOG00000009568 .
    GeneIDi 297893.
    KEGGi rno:297893.
    UCSCi RGD:619975. rat.

    Organism-specific databases

    CTDi 3065.
    RGDi 619975. Hdac1.

    Phylogenomic databases

    eggNOGi COG0123.
    GeneTreei ENSGT00530000062889.
    HOGENOMi HOG000225180.
    HOVERGENi HBG057112.
    InParanoidi Q4QQW4.
    KOi K06067.
    OMAi LRRDHQN.
    OrthoDBi EOG7DNNTW.
    PhylomeDBi Q4QQW4.
    TreeFami TF106171.

    Miscellaneous databases

    NextBioi 642799.
    PROi Q4QQW4.

    Gene expression databases

    Genevestigatori Q4QQW4.

    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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    2. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
      Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
      Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHDAC1_RAT
    AccessioniPrimary (citable) accession number: Q4QQW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 87 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