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Histone deacetylase 1 (HD1) (EC 3.5.1.98)

 HDAC1_PONAB             Reviewed;         482 AA.
Q5RAG0;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
27-SEP-2017, entry version 94.
RecName: Full=Histone deacetylase 1;
Short=HD1;
EC=3.5.1.98;
Name=HDAC1;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:O09106,
ECO:0000250|UniProtKB:Q13547}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: 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. Interacts with KDM5A. Interacts with
DNTTIP1. Identified in a histone deacetylase complex that contains
DNTTIP1, HDAC1 and ELMSAN1; this complex assembles into a tetramer
that contains four copies of each protein chain. Interacts with
CCAR2. Interacts with PPHLN1. Found in a complex with YY1, SIN3A
and GON4L. Interacts with CHD4. Found in a complex composed of at
least FAM60A, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1. Interacts
with SIN3A. {ECO:0000250|UniProtKB:O09106,
ECO:0000250|UniProtKB:Q13547}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13547}.
-!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic
activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.
-!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic
activity and interactions with NuRD and SIN3 complexes.
Phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q13547}.
-!- PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation
by the proteasome. {ECO:0000250|UniProtKB:Q13547}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
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EMBL; CR859057; CAH91250.1; -; mRNA.
RefSeq; NP_001125738.1; NM_001132266.1.
UniGene; Pab.6428; -.
ProteinModelPortal; Q5RAG0; -.
SMR; Q5RAG0; -.
STRING; 9601.ENSPPYP00000001838; -.
PRIDE; Q5RAG0; -.
GeneID; 100172663; -.
KEGG; pon:100172663; -.
CTD; 3065; -.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
HOVERGEN; HBG057112; -.
InParanoid; Q5RAG0; -.
KO; K06067; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
2: Evidence at transcript level;
Acetylation; Biological rhythms; Chromatin regulator;
Complete proteome; Hydrolase; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Repressor; S-nitrosylation;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 482 Histone deacetylase 1.
/FTId=PRO_0000304730.
REGION 9 321 Histone deacetylase.
ACT_SITE 141 141 {ECO:0000250}.
MOD_RES 74 74 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 220 220 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 261 261 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P70288}.
MOD_RES 273 273 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P70288}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:Q92769}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 432 432 N6-methylated lysine; by EHMT2.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 74 74 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 456 456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 457 457 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 473 473 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 480 480 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13547}.
SEQUENCE 482 AA; 55103 MW; 4D35B7C1ED7838D6 CRC64;
MAQTQGTRRK 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 EESGDEDEDD PDKRISICSS DKRIACEEEF
SDSEEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK
LA


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