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Database: UniProt/SWISS-PROT
Entry: HDAC1_BOVIN
LinkDB: HDAC1_BOVIN
Original site: HDAC1_BOVIN 
ID   HDAC1_BOVIN             Reviewed;         482 AA.
AC   Q32PJ8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   23-MAY-2018, entry version 118.
DE   RecName: Full=Histone deacetylase 1;
DE            Short=HD1;
DE            EC=3.5.1.98;
GN   Name=HDAC1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Deacetylates SP
CC       proteins, SP1 and SP3, and regulates their function. Component of
CC       the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-
CC       mediated transcription in resting neurons. Upon calcium
CC       stimulation, HDAC1 is released from the complex and CREBBP is
CC       recruited, which facilitates transcriptional activation.
CC       Deacetylates TSHZ3 and regulates its transcriptional repressor
CC       activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the
CC       transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and
CC       abrogates the effect of KAT5-mediated relieving of NR1D2
CC       transcription repression activity. Component of a
CC       RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone
CC       deacetylase (HDAC) recruitment, a number of genes implicated in
CC       multilineage blood cell development. Involved in CIART-mediated
CC       transcriptional repression of the circadian transcriptional
CC       activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the
CC       transcriptional repression of circadian target genes, such as
CC       PER1, mediated by the large PER complex or CRY1 through histone
CC       deacetylation. {ECO:0000250|UniProtKB:O09106,
CC       ECO:0000250|UniProtKB:Q13547}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex
CC       composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex
CC       associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form
CC       the nucleosome remodeling and histone deacetylation (NuRD)
CC       complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC
CC       complex. Component of a BHC histone deacetylase complex that
CC       contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and
CC       PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217,
CC       ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex
CC       that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and
CC       HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the
CC       interaction between HDAC1 and APBB1 is mediated by TSHZ3.
CC       Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex
CC       composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex
CC       containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large
CC       PER complex involved in the histone deacetylation is composed of
CC       at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1
CC       complex; interacts with HUS1. Found in a complex with DNMT3A and
CC       HDAC7. Interacts with the non-histone region of H2AFY. Interacts
CC       with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits
CC       its acetylation. Interacts with SP1; the interaction deacetylates
CC       SP1 and regulates its transcriptional activity. Interacts with
CC       SP3; the interaction deacetylates SP3 and regulates its
CC       transcriptional activity. In vitro, C(18) ceramides increase this
CC       interaction and the subsequent SP3 deacetylation and SP3-mediated
CC       repression of the TERT promoter. Interacts with TSHZ3 (via N-
CC       terminus); the interaction is direct. Interacts with APEX1; the
CC       interaction is not dependent on the acetylated status of APEX1.
CC       Interacts with C10orf90/FATS (via its N-terminal); the interaction
CC       prevents binding of HDAC1 to CDKN1A/p21 and facilitates the
CC       acetylation and stabilization of CDKN1A/p21. Interacts with
CC       CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25).
CC       Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via
CC       C-terminus). Interacts with TSC22D3 isoform 1; this interaction
CC       affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1
CC       transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6,
CC       BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1,
CC       DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1,
CC       NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF,
CC       PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3,
CC       SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2,
CC       ZMYND15, ZNF431 and ZNF541. Interacts with KDM5A. Interacts with
CC       DNTTIP1. Identified in a histone deacetylase complex that contains
CC       DNTTIP1, HDAC1 and ELMSAN1; this complex assembles into a tetramer
CC       that contains four copies of each protein chain. Interacts with
CC       CCAR2. Interacts with PPHLN1. Found in a complex with YY1, SIN3A
CC       and GON4L. Interacts with CHD4. Found in a complex composed of at
CC       least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1. Interacts
CC       with SIN3A. {ECO:0000250|UniProtKB:O09106,
CC       ECO:0000250|UniProtKB:Q13547}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13547}.
CC   -!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic
CC       activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.
CC   -!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic
CC       activity and interactions with NuRD and SIN3 complexes.
CC       Phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q13547}.
CC   -!- PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation
CC       by the proteasome. {ECO:0000250|UniProtKB:Q13547}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
DR   EMBL; BT030718; ABS45034.1; -; mRNA.
DR   EMBL; BC108088; AAI08089.1; -; mRNA.
DR   RefSeq; NP_001032521.1; NM_001037444.2.
DR   UniGene; Bt.16500; -.
DR   ProteinModelPortal; Q32PJ8; -.
DR   SMR; Q32PJ8; -.
DR   STRING; 9913.ENSBTAP00000016877; -.
DR   PaxDb; Q32PJ8; -.
DR   PRIDE; Q32PJ8; -.
DR   Ensembl; ENSBTAT00000016877; ENSBTAP00000016877; ENSBTAG00000012698.
DR   GeneID; 404126; -.
DR   KEGG; bta:404126; -.
DR   CTD; 3065; -.
DR   VGNC; VGNC:49065; HDAC1.
DR   eggNOG; KOG1342; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00910000144047; -.
DR   HOGENOM; HOG000225180; -.
DR   HOVERGEN; HBG057112; -.
DR   InParanoid; Q32PJ8; -.
DR   KO; K06067; -.
DR   OMA; MDTSKPK; -.
DR   OrthoDB; EOG091G067J; -.
DR   TreeFam; TF106171; -.
DR   Reactome; R-BTA-1538133; G0 and Early G1.
DR   Reactome; R-BTA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-BTA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-BTA-3214815; HDACs deacetylate histones.
DR   Reactome; R-BTA-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-BTA-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-BTA-6804758; Regulation of TP53 Activity through Acetylation.
DR   Reactome; R-BTA-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-BTA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-BTA-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000012698; -.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016581; C:NuRD complex; IEA:Ensembl.
DR   GO; GO:0016580; C:Sin3 complex; IEA:Ensembl.
DR   GO; GO:0033613; F:activating transcription factor binding; IEA:Ensembl.
DR   GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR   GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IEA:Ensembl.
DR   GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR   GO; GO:0006346; P:methylation-dependent chromatin silencing; IEA:Ensembl.
DR   GO; GO:0043922; P:negative regulation by host of viral transcription; IEA:Ensembl.
DR   GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0010870; P:positive regulation of receptor biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625; PTHR10625; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Biological rhythms; Chromatin regulator;
KW   Complete proteome; Hydrolase; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; S-nitrosylation;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    482       Histone deacetylase 1.
FT                                /FTId=PRO_0000304729.
FT   REGION        9    321       Histone deacetylase.
FT   ACT_SITE    141    141       {ECO:0000250}.
FT   MOD_RES      74     74       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   MOD_RES     220    220       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   MOD_RES     261    261       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P70288}.
FT   MOD_RES     273    273       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P70288}.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   MOD_RES     406    406       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q92769}.
FT   MOD_RES     409    409       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   MOD_RES     421    421       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   MOD_RES     423    423       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   MOD_RES     432    432       N6-methylated lysine; by EHMT2.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   CROSSLNK     74     74       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q92769}.
FT   CROSSLNK    438    438       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   CROSSLNK    444    444       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   CROSSLNK    444    444       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   CROSSLNK    456    456       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q92769}.
FT   CROSSLNK    457    457       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   CROSSLNK    473    473       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q92769}.
FT   CROSSLNK    476    476       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   CROSSLNK    476    476       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   CROSSLNK    480    480       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q13547}.
SQ   SEQUENCE   482 AA;  55106 MW;  7F64D3C17E1B4844 CRC64;
     MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN
     AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS
     AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG
     DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI
     FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
     GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
     KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED PDKRISICSS DKRIACEEEF
     SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKQ EAKGVKEEVK
     LA
//
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