ID HDAC1_DROME Reviewed; 521 AA.
AC Q94517; O17429; O77213; Q9VZA1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 27-MAR-2024, entry version 204.
DE RecName: Full=Histone deacetylase HDAC1 {ECO:0000303|PubMed:10655219};
DE Short=HD;
DE EC=3.5.1.98 {ECO:0000269|PubMed:11571273, ECO:0000269|PubMed:28245922};
GN Name=HDAC1 {ECO:0000303|PubMed:10655219, ECO:0000312|FlyBase:FBgn0015805};
GN Synonyms=Rpd3 {ECO:0000303|PubMed:8955276};
GN ORFNames=CG7471 {ECO:0000312|FlyBase:FBgn0015805};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=8955276; DOI=10.1038/384589a0;
RA de Rubertis F., Kadosh D., Henchoz S., Pauli D., Reuter G., Struhl K.,
RA Spierer P.;
RT "The histone deacetylase RPD3 counteracts genomic silencing in Drosophila
RT and yeast.";
RL Nature 384:589-591(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10655219; DOI=10.1093/genetics/154.2.657;
RA Mottus R., Sobel R.E., Grigliatti T.A.;
RT "Mutational analysis of a histone deacetylase in Drosophila melanogaster:
RT missense mutations suppress gene silencing associated with position effect
RT variegation.";
RL Genetics 154:657-668(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Johnson C.A., White D., O'Neill L.P., Turner B.M.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH SU(VAR)3-9.
RX PubMed=11571273; DOI=10.1093/embo-reports/kve210;
RA Czermin B., Schotta G., Huelsmann B.B., Brehm A., Becker P.B., Reuter G.,
RA Imhof A.;
RT "Physical and functional association of SU(VAR)3-9 and HDAC1 in
RT Drosophila.";
RL EMBO Rep. 2:915-919(2001).
RN [8]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC AND E(Z), AND
RP SUBCELLULAR LOCATION.
RX PubMed=12533794; DOI=10.1002/gene.10173;
RA Furuyama T., Tie F., Harte P.J.;
RT "Polycomb group proteins ESC and E(Z) are present in multiple distinct
RT complexes that undergo dynamic changes during development.";
RL Genesis 35:114-124(2003).
RN [9]
RP FUNCTION, IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; E(Z) AND
RP SU(Z)12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
RX PubMed=12408863; DOI=10.1016/s0092-8674(02)00975-3;
RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
RT "Drosophila Enhancer of zeste/ESC complexes have a histone H3
RT methyltransferase activity that marks chromosomal Polycomb sites.";
RL Cell 111:185-196(2002).
RN [10]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH CAF1-55; ESC; E(Z); PCL AND
RP SU(Z)12, AND SUBCELLULAR LOCATION.
RX PubMed=12697833; DOI=10.1128/mcb.23.9.3352-3362.2003;
RA Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
RT "A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike
RT and RPD3.";
RL Mol. Cell. Biol. 23:3352-3362(2003).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15545624; DOI=10.1101/gad.1255204;
RA Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J.,
RA Botchan M.R.;
RT "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor
RT complex.";
RL Genes Dev. 18:2929-2940(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH COREST.
RX PubMed=15306652; DOI=10.1523/jneurosci.0238-04.2004;
RA Dallman J.E., Allopenna J., Bassett A., Travers A., Mandel G.;
RT "A conserved role but different partners for the transcriptional
RT corepressor CoREST in fly and mammalian nervous system formation.";
RL J. Neurosci. 24:7186-7193(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-419; SER-421;
RP SER-455 AND THR-457, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [14]
RP INTERACTION WITH MI-2.
RX PubMed=18250149; DOI=10.1128/mcb.01839-07;
RA Murawska M., Kunert N., van Vugt J., Laengst G., Kremmer E., Logie C.,
RA Brehm A.;
RT "dCHD3, a novel ATP-dependent chromatin remodeler associated with sites of
RT active transcription.";
RL Mol. Cell. Biol. 28:2745-2757(2008).
RN [15] {ECO:0000305}
RP INTERACTION WITH RRP6.
RX PubMed=26389589; DOI=10.1371/journal.pgen.1005523;
RA Eberle A.B., Jordan-Pla A., Ganez-Zapater A., Hessle V., Silberberg G.,
RA von Euler A., Silverstein R.A., Visa N.;
RT "An Interaction between RRP6 and SU(VAR)3-9 Targets RRP6 to Heterochromatin
RT and Contributes to Heterochromatin Maintenance in Drosophila
RT melanogaster.";
RL PLoS Genet. 11:e1005523-e1005523(2015).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28245922; DOI=10.1016/j.devcel.2017.01.014;
RA Janssens D.H., Hamm D.C., Anhezini L., Xiao Q., Siller K.H., Siegrist S.E.,
RA Harrison M.M., Lee C.Y.;
RT "An Hdac1/Rpd3-poised circuit balances continual self-renewal and rapid
RT restriction of developmental potential during asymmetric stem cell
RT division.";
RL Dev. Cell 40:367-380(2017).
CC -!- FUNCTION: Catalyzes the deacetylation of lysine residues on the N-
CC terminal part of the core histones (H2A, H2B, H3 and H4)
CC (PubMed:11571273, PubMed:28245922, PubMed:12408863). Histone
CC deacetylation may constitute a tag for epigenetic repression and plays
CC an important role in transcriptional regulation, cell cycle progression
CC and developmental events (PubMed:11571273, PubMed:8955276,
CC PubMed:15545624, PubMed:15306652). For instance, deacetylation of
CC histone H3 may be a prerequisite for the subsequent recruitment of the
CC histone methyltransferase Su(var)3-9 to histones (PubMed:11571273).
CC Involved in position-effect variegation (PEV) (PubMed:11571273). In the
CC larval brain, part of a regulatory network including the
CC transcriptional repressors klu, dpn and E(spl)mgamma-HLH which is
CC required for type II neuroblast self-renewal and for maintaining erm in
CC an inactive state in intermediate neural progenitors (INP)
CC (PubMed:28245922). {ECO:0000269|PubMed:11571273,
CC ECO:0000269|PubMed:12408863, ECO:0000269|PubMed:15306652,
CC ECO:0000269|PubMed:15545624, ECO:0000269|PubMed:28245922,
CC ECO:0000269|PubMed:8955276}.
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:0000269|PubMed:11571273, ECO:0000269|PubMed:28245922};
CC -!- SUBUNIT: Component of a form of the Esc/E(z) complex present
CC specifically during early embryogenesis which is composed of Caf1-55,
CC esc, E(z), Su(z)12, Pcl and HDAC1 (PubMed:12533794, PubMed:12408863,
CC PubMed:12697833). The Esc/E(z) complex may also associate with Pcl and
CC HDAC1 during early embryogenesis (PubMed:12697833). This complex is
CC distinct from the PRC1 complex, which contains many other PcG proteins
CC like Pc, Ph, Psc, Su(z)2 (PubMed:12533794). The 2 complexes however
CC cooperate and interact together during the first 3 hours of development
CC to establish PcG silencing (PubMed:12533794). Interacts with the
CC histone methyltransferase Su(var)3-9 (PubMed:11571273). Component of a
CC complex that contains at least HDAC1, CoRest and Su(var)3-3/Hdm
CC (PubMed:15306652). Component of the DREAM complex at least composed of
CC Myb, Caf1-55, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, HDAC1
CC and l(3)mbt (PubMed:15545624). Interacts with the chromatin-remodeler
CC Mi-2 (PubMed:18250149). Interacts with Rrp6 (PubMed:26389589).
CC {ECO:0000269|PubMed:11571273, ECO:0000269|PubMed:12408863,
CC ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:12697833,
CC ECO:0000269|PubMed:15306652, ECO:0000269|PubMed:15545624,
CC ECO:0000269|PubMed:18250149, ECO:0000269|PubMed:26389589}.
CC -!- INTERACTION:
CC Q94517; Q24572: Caf1-55; NbExp=4; IntAct=EBI-302197, EBI-75924;
CC Q94517; P42124: E(z); NbExp=9; IntAct=EBI-302197, EBI-112315;
CC Q94517; Q24338: esc; NbExp=11; IntAct=EBI-302197, EBI-88911;
CC Q94517; A1Z9E2: mip120; NbExp=2; IntAct=EBI-302197, EBI-75953;
CC Q94517; Q24459: Pcl; NbExp=5; IntAct=EBI-302197, EBI-430086;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12533794,
CC ECO:0000269|PubMed:12697833}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in loss of type
CC II neuroblasts. {ECO:0000269|PubMed:28245922}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; Y09258; CAA70455.1; -; mRNA.
DR EMBL; AF086715; AAC61494.1; -; Genomic_DNA.
DR EMBL; AF026949; AAC23917.1; -; mRNA.
DR EMBL; AE014296; AAF47924.1; -; Genomic_DNA.
DR EMBL; AY058487; AAL13716.1; -; mRNA.
DR RefSeq; NP_647918.2; NM_139661.4.
DR AlphaFoldDB; Q94517; -.
DR SMR; Q94517; -.
DR BioGRID; 64037; 84.
DR ComplexPortal; CPX-2355; Mi2/NuRD nucleosome remodeling and deacetylase complex.
DR DIP; DIP-29512N; -.
DR IntAct; Q94517; 20.
DR MINT; Q94517; -.
DR STRING; 7227.FBpp0073173; -.
DR iPTMnet; Q94517; -.
DR PaxDb; 7227-FBpp0073173; -.
DR DNASU; 38565; -.
DR EnsemblMetazoa; FBtr0073317; FBpp0073173; FBgn0015805.
DR GeneID; 38565; -.
DR KEGG; dme:Dmel_CG7471; -.
DR AGR; FB:FBgn0015805; -.
DR CTD; 3065; -.
DR FlyBase; FBgn0015805; HDAC1.
DR VEuPathDB; VectorBase:FBgn0015805; -.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000155725; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; Q94517; -.
DR OMA; GKIMEWY; -.
DR OrthoDB; 1327607at2759; -.
DR PhylomeDB; Q94517; -.
DR Reactome; R-DME-1538133; G0 and Early G1.
DR Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
DR Reactome; R-DME-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-DME-3214815; HDACs deacetylate histones.
DR Reactome; R-DME-350054; Notch-HLH transcription pathway.
DR Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DME-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q94517; -.
DR BioGRID-ORCS; 38565; 1 hit in 3 CRISPR screens.
DR ChiTaRS; HDAC1; fly.
DR GenomeRNAi; 38565; -.
DR PRO; PR:Q94517; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0015805; Expressed in eye disc (Drosophila) and 37 other cell types or tissues.
DR ExpressionAtlas; Q94517; baseline and differential.
DR Genevisible; Q94517; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:FlyBase.
DR GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR GO; GO:0031523; C:Myb complex; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0016581; C:NuRD complex; IPI:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:FlyBase.
DR GO; GO:0070822; C:Sin3-type complex; IDA:FlyBase.
DR GO; GO:0017053; C:transcription repressor complex; IPI:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:FlyBase.
DR GO; GO:0045129; F:NAD-independent histone deacetylase activity; NAS:FlyBase.
DR GO; GO:0003714; F:transcription corepressor activity; IPI:FlyBase.
DR GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR GO; GO:0070983; P:dendrite guidance; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin formation; IMP:FlyBase.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IGI:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:2001229; P:negative regulation of response to gamma radiation; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:FlyBase.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:UniProtKB.
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; PTHR10625:SF13; HISTONE DEACETYLASE HDAC1; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-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 1: Evidence at protein level;
KW Chromatin regulator; Developmental protein; Hydrolase; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..521
FT /note="Histone deacetylase HDAC1"
FT /id="PRO_0000114718"
FT REGION 7..319
FT /note="Histone deacetylase"
FT REGION 376..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 50..52
FT /note="EIY -> DI (in Ref. 1; CAA70455)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="S -> C (in Ref. 1; CAA70455)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="D -> N (in Ref. 3; AAC23917)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="E -> D (in Ref. 3; AAC23917)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="V -> VV (in Ref. 3; AAC23917)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="N -> K (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="L -> V (in Ref. 3; AAC23917)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="S -> T (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 58331 MW; B0F6503D42A1BCE9 CRC64;
MQSHSKKRVC YYYDSDIGNY YYGQGHPMKP HRIRMTHNLL LNYGLYRKME IYRPHKATAD
EMTKFHSDEY VRFLRSIRPD NMSEYNKQMQ RFNVGEDCPV FDGLYEFCQL SAGGSVAAAV
KLNKQASEIC INWGGGLHHA KKSEASGFCY VNDIVLGILE LLKYHQRVLY IDIDVHHGDG
VEEAFYTTDR VMTVSFHKYG EYFPGTGDLR DIGAGKGKYY AVNIPLRDGM DDDAYESIFV
PIISKVMETF QPAAVVLQCG ADSLTGDRLG CFNLTVKGHG KCVEFVKKYN LPFLMVGGGG
YTIRNVSRCW TYETSVALAV EIANELPYND YFEYFGPDFK LHISPSNMTN QNTSEYLEKI
KNRLFENLRM LPHAPGVQIQ AIPEDAINDE SDDEDKVDKD DRLPQSDKDK RIVPENEYSD
SEDEGEGGRR DNRSYKGQRK RPRLDKDTNS NKASSETSSE IKDEKEKGDG ADGEESTASN
TNSNNNSNNK SDNDAGATAN AGSGSGSGSG AGAKGAKENN I
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