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Database: UniProt/TrEMBL
Entry: K7D1J2_PANTR
LinkDB: K7D1J2_PANTR
Original site: K7D1J2_PANTR 
ID   K7D1J2_PANTR            Unreviewed;       482 AA.
AC   K7D1J2; A0A2J8IYW8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Histone deacetylase 1 {ECO:0000256|ARBA:ARBA00040350, ECO:0000256|PIRNR:PIRNR037913};
DE            Short=HD1 {ECO:0000256|PIRNR:PIRNR037913};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037913};
GN   Name=HDAC1 {ECO:0000313|EMBL:JAA26107.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000075891.1,
GN   ECO:0000313|VGNC:VGNC:111884};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA26107.1};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000075891.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA26107.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA01310.1}, Skeletal muscle
RC   {ECO:0000313|EMBL:JAA34765.1}, Skin {ECO:0000313|EMBL:JAA26107.1}, and
RC   Smooth vascular {ECO:0000313|EMBL:JAA13928.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000075891.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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 proteins. {ECO:0000256|PIRNR:PIRNR037913}.
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:0000256|ARBA:ARBA00029357};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC         Evidence={ECO:0000256|ARBA:ARBA00029357};
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:0000256|ARBA:ARBA00029372};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC         Evidence={ECO:0000256|ARBA:ARBA00029372};
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:0000256|ARBA:ARBA00029349};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC         Evidence={ECO:0000256|ARBA:ARBA00029349};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR   EMBL; AACZ04072183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABC01010028; JAA01310.1; -; mRNA.
DR   EMBL; GABF01008217; JAA13928.1; -; mRNA.
DR   EMBL; GABD01006993; JAA26107.1; -; mRNA.
DR   EMBL; GABE01009974; JAA34765.1; -; mRNA.
DR   RefSeq; XP_016815100.1; XM_016959611.1.
DR   RefSeq; XP_519834.3; XM_519834.6.
DR   STRING; 9598.ENSPTRP00000075891; -.
DR   PaxDb; 9598-ENSPTRP00000060659; -.
DR   Ensembl; ENSPTRT00000082134.1; ENSPTRP00000075891.1; ENSPTRG00000044722.1.
DR   GeneID; 107966150; -.
DR   CTD; 3065; -.
DR   VGNC; VGNC:111884; HDAC1.
DR   GeneTree; ENSGT00940000154301; -.
DR   OMA; GYNPWSV; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000002277; Chromosome 1.
DR   Bgee; ENSPTRG00000044722; Expressed in fibroblast and 21 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016581; C:NuRD complex; IBA:GO_Central.
DR   GO; GO:0016580; C:Sin3 complex; IEA:Ensembl.
DR   GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl.
DR   GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0160009; F:histone decrotonylase activity; IEA:Ensembl.
DR   GO; GO:0035851; F:Krueppel-associated box domain binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; IEA:Ensembl.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR   GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR   GO; GO:0009913; P:epidermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0061198; P:fungiform papilla formation; IEA:Ensembl.
DR   GO; GO:0060789; P:hair follicle placode formation; IEA:Ensembl.
DR   GO; GO:0021766; P:hippocampus development; 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:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   CDD; cd10010; HDAC1; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 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; PTHR48252:SF36; HISTONE DEACETYLASE 1; 1.
DR   PANTHER; PTHR48252; HISTONE DEACETYLASE 2-RELATED; 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; Arginase/deacetylase; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|PIRNR:PIRNR037913}; Hydrolase {ECO:0000256|PIRNR:PIRNR037913};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT   DOMAIN          28..317
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
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                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT   BINDING         176
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         178
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         264
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ   SEQUENCE   482 AA;  55117 MW;  AC24B7C037D3490C 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 EESGDEDEED PDKRISICSS DKRIACEEEF
     SDSEEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK
     LA
//
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