ID HDAC1_RAT Reviewed; 482 AA. AC Q4QQW4; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 35. DE RecName: Full=Histone deacetylase 1; DE Short=HD1; DE EC=3.5.1.98; GN Name=Hdac1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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 (By similarity). 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, AOF2/LSD1, RCOR1/CoREST and CC PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, CC ZMYM3, GSE1 and GTF2I. Associates with the 9-1-1 complex; CC interacts with HUS1. Found in a complex with DNMT3A and HDAC7. CC Interacts with BCOR, BRMS1L, DAXX, DNMT1, EP300, HCFC1, NFE4, CC PCAF, PHB2, MIER1, KDM4A, MINT, NRIP1, PRDM6, RERE, SETDB1, CC SUV39H1, TGIF, TGIF2, UHRF1, UHRF2 and ZNF541. Interacts with the CC non-histone region of H2AFY. Component of a mSin3A corepressor CC complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, CC HDAC1 and HDAC2. Interacts with BANP, CBFA2T3 and KDM5B. Interacts CC with E4F1 and KLF1 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic CC activity. Desumoylated by SENP1 (By similarity). CC -!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic CC activity and interactions with NuRD and SIN3 complexes (By CC similarity). CC -!- SIMILARITY: Belongs to the histone deacetylase family. Type 1 CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC097943; AAH97943.1; -; mRNA. DR EMBL; BC107476; AAI07477.1; -; mRNA. DR IPI; IPI00364813; -. DR RefSeq; NP_001020580.1; -. DR UniGene; Rn.1863; -. DR PhosphoSite; Q4QQW4; -. DR Ensembl; ENSRNOG00000009568; Rattus norvegicus. DR GeneID; 297893; -. DR KEGG; rno:297893; -. DR NMPDR; fig|10116.3.peg.24004; -. DR RGD; 619975; Hdac1. DR HOVERGEN; Q4QQW4; -. DR NextBio; 642799; -. DR ArrayExpress; Q4QQW4; -. DR GO; GO:0000785; C:chromatin; IDA:RGD. DR GO; GO:0005634; C:nucleus; IDA:RGD. DR GO; GO:0043234; C:protein complex; IDA:RGD. DR GO; GO:0004407; F:histone deacetylase activity; IEA:InterPro. DR GO; GO:0032403; F:protein complex binding; IDA:RGD. DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:RGD. DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro. DR GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD. DR GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:RGD. DR GO; GO:0016481; P:negative regulation of transcription; IDA:RGD. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. DR GO; GO:0042493; P:response to drug; IEP:RGD. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR003084; His_deacetylse_1. DR Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1. DR PANTHER; PTHR10625; His_deacetylse; 1. DR PANTHER; PTHR10625:SF28; His_deacetylse_1; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037913; His_deacetylse_1; 1. DR PRINTS; PR01270; HDASUPER. DR PRINTS; PR01271; HISDACETLASE. PE 2: Evidence at transcript level; KW Chromatin regulator; Hydrolase; Isopeptide bond; Nucleus; KW Phosphoprotein; Repressor; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1 482 Histone deacetylase 1. FT /FTId=PRO_0000304731. FT REGION 9 321 Histone deacetylase. FT ACT_SITE 141 141 By similarity. FT MOD_RES 221 221 Phosphotyrosine (By similarity). FT MOD_RES 393 393 Phosphoserine (By similarity). FT MOD_RES 421 421 Phosphoserine (By similarity). FT MOD_RES 423 423 Phosphoserine (By similarity). FT CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO) (By FT similarity). FT CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO) (By FT similarity). SQ SEQUENCE 482 AA; 55093 MW; 7F6563C17F5E4844 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 EEEKTKEEKP EAKGVKEEVK MA //