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HDAC1_PONAB
ID   HDAC1_PONAB             Reviewed;         482 AA.
AC   Q5RAG0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Histone deacetylase 1;
DE            Short=HD1;
DE            EC=3.5.1.98 {ECO:0000250|UniProtKB:Q13547};
DE   AltName: Full=Protein deacetylase HDAC1;
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
DE   AltName: Full=Protein decrotonylase HDAC1;
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
GN   Name=HDAC1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone deacetylase that catalyzes the deacetylation of
CC       lysine residues on the N-terminal part of the core histones (H2A, H2B,
CC       H3 and H4). Histone deacetylation gives a tag for epigenetic repression
CC       and plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via the
CC       formation of large multiprotein complexes. Also functions as
CC       deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and
CC       TSHZ3. Deacetylates SP proteins, SP1 and SP3, and regulates their
CC       function. Component of the BRG1-RB1-HDAC1 complex, which negatively
CC       regulates the CREST-mediated transcription in resting neurons. Upon
CC       calcium stimulation, HDAC1 is released from the complex and CREBBP is
CC       recruited, which facilitates transcriptional activation. Deacetylates
CC       TSHZ3 and regulates its transcriptional repressor activity.
CC       Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional
CC       activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of
CC       KAT5-mediated relieving of NR1D2 transcription repression activity (By
CC       similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that
CC       suppresses, via histone deacetylase (HDAC) recruitment, a number of
CC       genes implicated in multilineage blood cell development. Involved in
CC       CIART-mediated transcriptional repression of the circadian
CC       transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for
CC       the transcriptional repression of circadian target genes, such as PER1,
CC       mediated by the large PER complex or CRY1 through histone deacetylation
CC       (By similarity). In addition to protein deacetylase activity, also has
CC       protein-lysine deacylase activity: acts as a protein decrotonylase by
CC       mediating decrotonylation ((2E)-butenoyl) of histones (By similarity).
CC       {ECO:0000250|UniProtKB:O09106, ECO:0000250|UniProtKB:Q13547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC         [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q13547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate
CC         + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC   -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex composed
CC       of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with
CC       MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome
CC       remodeling and histone deacetylation (NuRD) complex, or with SIN3,
CC       SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC
CC       histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35,
CC       KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain
CC       ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor
CC       complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1
CC       and HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the
CC       interaction between HDAC1 and APBB1 is mediated by TSHZ3. Component of
CC       a RCOR/GFI/KDM1A/HDAC complex. Part of a complex composed of TRIM28,
CC       HDAC1, HDAC2 and EHMT2. Part of a complex containing at least CDYL,
CC       MIER1, MIER2, HDAC1 and HDAC2. The large PER complex involved in the
CC       histone deacetylation is composed of at least HDAC1, PER2, SFPQ and
CC       SIN3A. Associates with the 9-1-1 complex; interacts with HUS1. Found in
CC       a complex with DNMT3A and HDAC7. Interacts with the non-histone region
CC       of MACROH2A1. Interacts with TRIM28; the interaction recruits HDAC1 to
CC       E2F1 and inhibits its acetylation. Interacts with SP1; the interaction
CC       deacetylates SP1 and regulates its transcriptional activity. Interacts
CC       with 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-terminus);
CC       the interaction is direct. Interacts with APEX1; the interaction is not
CC       dependent on the acetylated status of APEX1. Interacts with
CC       C10orf90/FATS (via its N-terminal); the interaction prevents binding of
CC       HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization
CC       of CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5 complexed
CC       to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B. Interacts with
CC       NR1D2 (via C-terminus). Interacts with TSC22D3 isoform 1; this
CC       interaction affects HDAC1 activity on MYOG promoter and thus inhibits
CC       MYOD1 transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6,
CC       BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX,
CC       DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4,
CC       NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6,
CC       PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2,
CC       SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541.
CC       Interacts with KDM5A; this interaction impairs histone deacetylation
CC       (By similarity). Interacts with DNTTIP1. Identified in a histone
CC       deacetylase complex that contains DNTTIP1, HDAC1 and MIDEAS; this
CC       complex assembles into a tetramer that contains four copies of each
CC       protein chain. Interacts with CCAR2. Interacts with PPHLN1. Found in a
CC       complex with YY1, SIN3A and GON4L. Interacts with CHD4. Found in a
CC       complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT
CC       and TET1. Interacts with SIN3A. Interacts with DHX36; this interaction
CC       occurs in a RNA-dependent manner (By similarity). Interacts with ZBTB7A
CC       (By similarity). Interacts with SMAD4; positively regulated by ZBTB7A
CC       (By similarity). Interacts with PACS2 (By similarity). Forms a complex
CC       comprising APPL1, RUVBL2, APPL2, CTNNB1 and HDAC2 (By similarity).
CC       Interacts with ZNF638 (By similarity). Interacts with SPHK2 (By
CC       similarity). Interacts with ERCC6 (By similarity). Interacts with SMYD4
CC       (via MYND-type zinc finger) (By similarity). Interacts with PWWP2A in a
CC       MTA1-dependent manner (By similarity). Interacts with PWWP2B (By
CC       similarity). Interacts with ZNF516 and BRCC3; these interactions are
CC       enhanced in the presence of PWWP2B (By similarity). Interacts with
CC       SANBR (via the BTB domain) (By similarity).
CC       {ECO:0000250|UniProtKB:O09106, 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 activity
CC       and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5.
CC       {ECO:0000250|UniProtKB:Q13547}.
CC   -!- PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation by
CC       the proteasome. {ECO:0000250|UniProtKB:Q13547}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR859057; CAH91250.1; -; mRNA.
DR   RefSeq; NP_001125738.1; NM_001132266.1.
DR   AlphaFoldDB; Q5RAG0; -.
DR   SMR; Q5RAG0; -.
DR   STRING; 9601.ENSPPYP00000001838; -.
DR   GeneID; 100172663; -.
DR   KEGG; pon:100172663; -.
DR   CTD; 3065; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   InParanoid; Q5RAG0; -.
DR   OrthoDB; 732770at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0160009; F:histone decrotonylase activity; ISS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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   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; Hydrolase;
KW   Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; S-nitrosylation; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..482
FT                   /note="Histone deacetylase 1"
FT                   /id="PRO_0000304730"
FT   REGION          9..321
FT                   /note="Histone deacetylase"
FT   REGION          390..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         74
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         220
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         261
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P70288"
FT   MOD_RES         273
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P70288"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92769"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         432
FT                   /note="N6-methylated lysine; by EHMT2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        74
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q92769"
FT   CROSSLNK        438
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        444
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        444
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        456
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92769"
FT   CROSSLNK        457
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        473
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92769"
FT   CROSSLNK        476
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        476
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        480
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
SQ   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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