HDAC1_HUMAN
ID HDAC1_HUMAN Reviewed; 482 AA.
AC Q13547; Q92534;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 244.
DE RecName: Full=Histone deacetylase 1 {ECO:0000305};
DE Short=HD1;
DE EC=3.5.1.98 {ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:28497810};
DE AltName: Full=Protein deacetylase HDAC1;
DE EC=3.5.1.- {ECO:0000305|PubMed:12837748, ECO:0000305|PubMed:16478997, ECO:0000305|PubMed:17996965};
DE AltName: Full=Protein decrotonylase HDAC1;
DE EC=3.5.1.- {ECO:0000269|PubMed:28497810};
GN Name=HDAC1 {ECO:0000303|PubMed:10846170, ECO:0000312|HGNC:HGNC:4852};
GN Synonyms=RPD3L1 {ECO:0000303|PubMed:8602529};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=T-cell;
RX PubMed=8602529; DOI=10.1126/science.272.5260.408;
RA Taunton J., Hassig C.A., Schreiber S.L.;
RT "A mammalian histone deacetylase related to the yeast transcriptional
RT regulator Rpd3p.";
RL Science 272:408-411(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal lung;
RX PubMed=8646880; DOI=10.1159/000134323;
RA Furukawa Y., Kawakami T., Sudo K., Inazawa J., Matsumine A., Akiyama T.,
RA Nakamura Y.;
RT "Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3,
RT a transcription factor in Saccharomyces cerevisiae.";
RL Cytogenet. Cell Genet. 73:130-133(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH HDAC9.
RX PubMed=10487760; DOI=10.1093/emboj/18.18.5085;
RA Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S.,
RA Towers N., Spohr G., Kouzarides T., Mohun T.J.;
RT "MEF-2 function is modified by a novel co-repressor, MITR.";
RL EMBO J. 18:5085-5098(1999).
RN [5]
RP INTERACTION WITH BCOR.
RX PubMed=10898795;
RA Huynh K.D., Fischle W., Verdin E., Bardwell V.J.;
RT "BCoR, a novel corepressor involved in BCL-6 repression.";
RL Genes Dev. 14:1810-1823(2000).
RN [6]
RP INTERACTION WITH THE 9-1-1 COMPLEX AND HUS1, AND SUBCELLULAR LOCATION.
RX PubMed=10846170; DOI=10.1074/jbc.m000168200;
RA Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.;
RT "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M
RT checkpoint Rad proteins.";
RL J. Biol. Chem. 275:27909-27916(2000).
RN [7]
RP INTERACTION WITH NRIP1.
RX PubMed=11006275; DOI=10.1074/jbc.m004821200;
RA Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.;
RT "Receptor-interacting protein 140 directly recruits histone deacetylases
RT for gene silencing.";
RL J. Biol. Chem. 275:40782-40787(2000).
RN [8]
RP INTERACTION WITH DAXX.
RX PubMed=10669754; DOI=10.1128/mcb.20.5.1784-1796.2000;
RA Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.;
RT "Sequestration and inhibition of Daxx-mediated transcriptional repression
RT by PML.";
RL Mol. Cell. Biol. 20:1784-1796(2000).
RN [9]
RP INTERACTION WITH HDAC9.
RX PubMed=10655483; DOI=10.1073/pnas.97.3.1056;
RA Zhou X., Richon V.M., Rifkind R.A., Marks P.A.;
RT "Identification of a transcriptional repressor related to the noncatalytic
RT domain of histone deacetylases 4 and 5.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000).
RN [10]
RP PHOSPHORYLATION AT SER-421 AND SER-423, MUTAGENESIS OF SER-421; SER-423;
RP GLU-424; GLU-425 AND GLU-426, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11602581; DOI=10.1074/jbc.m105590200;
RA Pflum M.K.H., Tong J.K., Lane W.S., Schreiber S.L.;
RT "Histone deacetylase 1 phosphorylation promotes enzymatic activity and
RT complex formation.";
RL J. Biol. Chem. 276:47733-47741(2001).
RN [11]
RP INTERACTION WITH MINT.
RX PubMed=11331609; DOI=10.1101/gad.871201;
RA Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M.,
RA Evans R.M.;
RT "Sharp, an inducible cofactor that integrates nuclear receptor repression
RT and activation.";
RL Genes Dev. 15:1140-1151(2001).
RN [12]
RP INTERACTION WITH MBD2 AND MBD3.
RX PubMed=11102443; DOI=10.1074/jbc.m007372200;
RA Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
RA Howard B.H.;
RT "Stable histone deacetylase complexes distinguished by the presence of SANT
RT domain proteins CoREST/kiaa0071 and Mta-L1.";
RL J. Biol. Chem. 276:6817-6824(2001).
RN [13]
RP INTERACTION WITH TGIF2.
RX PubMed=11427533; DOI=10.1074/jbc.m103377200;
RA Melhuish T.A., Gallo C.M., Wotton D.;
RT "TGIF2 interacts with histone deacetylase 1 and represses transcription.";
RL J. Biol. Chem. 276:32109-32114(2001).
RN [14]
RP INTERACTION WITH CBFA2T3.
RX PubMed=11533236; DOI=10.1128/mcb.21.19.6470-6483.2001;
RA Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA Downing J.R., Meyers S., Hiebert S.W.;
RT "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with
RT multiple histone deacetylases and binds mSin3A through its oligomerization
RT domain.";
RL Mol. Cell. Biol. 21:6470-6483(2001).
RN [15]
RP SUMOYLATION.
RX PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
RA Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
RA Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
RT "The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
RT deacetylase.";
RL EMBO J. 21:2682-2691(2002).
RN [16]
RP SUMOYLATION AT LYS-444 AND LYS-476.
RX PubMed=11960997; DOI=10.1074/jbc.m203690200;
RA David G., Neptune M.A., DePinho R.A.;
RT "SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its
RT biological activities.";
RL J. Biol. Chem. 277:23658-23663(2002).
RN [17]
RP INTERACTION WITH APEX1.
RX PubMed=14633989; DOI=10.1093/emboj/cdg595;
RA Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.;
RT "Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the
RT parathyroid hormone gene.";
RL EMBO J. 22:6299-6309(2003).
RN [18]
RP INTERACTION WITH HCFC1.
RX PubMed=12670868; DOI=10.1101/gad.252103;
RA Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT methyltransferase are tethered together selectively by the cell-
RT proliferation factor HCF-1.";
RL Genes Dev. 17:896-911(2003).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE BHC COMPLEX
RP WITH GSE1; GTF2I; HDAC2; HMG20B; KDM1A; PHF21A; RCOR1; ZMYM2; ZMYM3 AND
RP ZNF217.
RX PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [20]
RP INTERACTION WITH SP3, AND FUNCTION.
RX PubMed=12837748; DOI=10.1074/jbc.m305961200;
RA Ammanamanchi S., Freeman J.W., Brattain M.G.;
RT "Acetylated SP3 is a transcriptional activator.";
RL J. Biol. Chem. 278:35775-35780(2003).
RN [21]
RP INTERACTION WITH MIER1.
RX PubMed=12482978; DOI=10.1128/mcb.23.1.250-258.2003;
RA Ding Z., Gillespie L.L., Paterno G.D.;
RT "Human MI-ER1 alpha and beta function as transcriptional repressors by
RT recruitment of histone deacetylase 1 to their conserved ELM2 domain.";
RL Mol. Cell. Biol. 23:250-258(2003).
RN [22]
RP IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3;
RP ARID4B; HDAC1 AND HDAC2.
RX PubMed=12724404; DOI=10.1128/mcb.23.10.3456-3467.2003;
RA Fleischer T.C., Yun U.J., Ayer D.E.;
RT "Identification and characterization of three new components of the mSin3A
RT corepressor complex.";
RL Mol. Cell. Biol. 23:3456-3467(2003).
RN [23]
RP INTERACTION WITH E4F1.
RX PubMed=12730668; DOI=10.1038/sj.onc.1206379;
RA Colombo R., Draetta G.F., Chiocca S.;
RT "Modulation of p120E4F transcriptional activity by the Gam1 adenoviral
RT early protein.";
RL Oncogene 22:2541-2547(2003).
RN [24]
RP INTERACTION WITH BRMS1L.
RX PubMed=15451426; DOI=10.1016/j.bbrc.2004.08.227;
RA Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.;
RT "Identification of a novel BRMS1-homologue protein p40 as a component of
RT the mSin3A/p33(ING1b)/HDAC1 deacetylase complex.";
RL Biochem. Biophys. Res. Commun. 323:1216-1222(2004).
RN [25]
RP INTERACTION WITH BCL6, AND IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=15454082; DOI=10.1016/j.cell.2004.09.014;
RA Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M.,
RA Wade P.A.;
RT "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte
RT differentiation.";
RL Cell 119:75-86(2004).
RN [26]
RP INTERACTION WITH NFE4.
RX PubMed=15273251; DOI=10.1074/jbc.m405129200;
RA Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.;
RT "Site-specific acetylation of the fetal globin activator NF-E4 prevents its
RT ubiquitination and regulates its interaction with the histone deacetylase,
RT HDAC1.";
RL J. Biol. Chem. 279:41477-41486(2004).
RN [27]
RP DESUMOYLATION BY SENP1.
RX PubMed=15199155; DOI=10.1128/mcb.24.13.6021-6028.2004;
RA Cheng J., Wang D., Wang Z., Yeh E.T.H.;
RT "SENP1 enhances androgen receptor-dependent transcription through
RT desumoylation of histone deacetylase 1.";
RL Mol. Cell. Biol. 24:6021-6028(2004).
RN [28]
RP INTERACTION WITH UHRF1 AND UHRF2.
RX PubMed=15361834; DOI=10.1038/sj.onc.1208053;
RA Unoki M., Nishidate T., Nakamura Y.;
RT "ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through
RT its SRA domain.";
RL Oncogene 23:7601-7610(2004).
RN [29]
RP REVIEW ON DEACETYLASE COMPLEXES.
RX PubMed=10904264; DOI=10.1016/s0168-9525(00)02066-7;
RA Ahringer J.;
RT "NuRD and SIN3 histone deacetylase complexes in development.";
RL Trends Genet. 16:351-356(2000).
RN [30]
RP INTERACTION WITH KDM4A.
RX PubMed=15927959; DOI=10.1074/jbc.m413687200;
RA Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H.,
RA Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
RT "Functional characterization of JMJD2A, a histone deacetylase- and
RT retinoblastoma-binding protein.";
RL J. Biol. Chem. 280:28507-28518(2005).
RN [31]
RP INTERACTION WITH BANP.
RX PubMed=16166625; DOI=10.1128/mcb.25.19.8415-8429.2005;
RA Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.;
RT "Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the
RT SIN3/histone deacetylase 1 complex.";
RL Mol. Cell. Biol. 25:8415-8429(2005).
RN [32]
RP INTERACTION WITH INSM1.
RX PubMed=16569215; DOI=10.1042/bj20051669;
RA Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.;
RT "INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene
RT through the recruitment of cyclin D1 and histone deacetylases.";
RL Biochem. J. 397:169-177(2006).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [34]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16762839; DOI=10.1016/j.molcel.2006.04.019;
RA Qiu Y., Zhao Y., Becker M., John S., Parekh B.S., Huang S., Hendarwanto A.,
RA Martinez E.D., Chen Y., Lu H., Adkins N.L., Stavreva D.A., Wiench M.,
RA Georgel P.T., Schiltz R.L., Hager G.L.;
RT "HDAC1 acetylation is linked to progressive modulation of steroid receptor-
RT induced gene transcription.";
RL Mol. Cell 22:669-679(2006).
RN [35]
RP INTERACTION WITH SP1, AND FUNCTION.
RX PubMed=16478997; DOI=10.1128/mcb.26.5.1770-1785.2006;
RA Hung J.J., Wang Y.T., Chang W.C.;
RT "Sp1 deacetylation induced by phorbol ester recruits p300 to activate
RT 12(S)-lipoxygenase gene transcription.";
RL Mol. Cell. Biol. 26:1770-1785(2006).
RN [36]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH BRMS1.
RX PubMed=17000776; DOI=10.1128/mcb.00940-06;
RA Liu Y., Smith P.W., Jones D.R.;
RT "Breast cancer metastasis suppressor 1 functions as a corepressor by
RT enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and
RT promoting apoptosis.";
RL Mol. Cell. Biol. 26:8683-8696(2006).
RN [37]
RP INTERACTION WITH SAP30L.
RX PubMed=16820529; DOI=10.1093/nar/gkl401;
RA Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K.,
RA Peterson P., Maeki M., Kainulainen H., Lohi O.;
RT "SAP30L interacts with members of the Sin3A corepressor complex and targets
RT Sin3A to the nucleolus.";
RL Nucleic Acids Res. 34:3288-3298(2006).
RN [38]
RP INTERACTION WITH PPHLN1.
RX PubMed=17963697; DOI=10.1016/j.bbrc.2007.10.090;
RA Kurita M., Suzuki H., Kawano Y., Aiso S., Matsuoka M.;
RT "CR/periphilin is a transcriptional co-repressor involved in cell cycle
RT progression.";
RL Biochem. Biophys. Res. Commun. 364:930-936(2007).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [40]
RP INTERACTION WITH SP3.
RX PubMed=17548428; DOI=10.1096/fj.07-8621com;
RA Wooten-Blanks L.G., Song P., Senkal C.E., Ogretmen B.;
RT "Mechanisms of ceramide-mediated repression of the human telomerase reverse
RT transcriptase promoter via deacetylation of Sp3 by histone deacetylase 1.";
RL FASEB J. 21:3386-3397(2007).
RN [41]
RP INTERACTION WITH KDM5B.
RX PubMed=17373667; DOI=10.1002/ijc.22673;
RA Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K.,
RA Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P.,
RA Taylor-Papadimitriou J.;
RT "Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts
RT directly with histone deacetylases.";
RL Int. J. Cancer 121:265-275(2007).
RN [42]
RP INTERACTION WITH TRIM28, AND FUNCTION.
RX PubMed=17704056; DOI=10.1074/jbc.m704757200;
RA Wang C., Rauscher F.J. III, Cress W.D., Chen J.;
RT "Regulation of E2F1 function by the nuclear corepressor KAP1.";
RL J. Biol. Chem. 282:29902-29909(2007).
RN [43]
RP INTERACTION WITH DDIT3.
RX PubMed=17872950; DOI=10.1074/jbc.m703735200;
RA Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
RT "Critical and functional regulation of CHOP (C/EBP homologous protein)
RT through the N-terminal portion.";
RL J. Biol. Chem. 282:35687-35694(2007).
RN [44]
RP INTERACTION WITH SV40 LARGE T ANTIGEN.
RX PubMed=17341466; DOI=10.1093/nar/gkl1113;
RA Valls E., Blanco-Garcia N., Aquizu N., Piedra D., Estaras C.,
RA de la Cruz X., Martinez-Balbas M.A.;
RT "Involvement of chromatin and histone deacetylation in SV40 T antigen
RT transcription regulation.";
RL Nucleic Acids Res. 35:1958-1968(2007).
RN [45]
RP INTERACTION WITH DDX5.
RX PubMed=17369852; DOI=10.1038/sj.onc.1210387;
RA Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T.,
RA Fuller-Pace F.V.;
RT "SUMO modification of the DEAD box protein p68 modulates its
RT transcriptional activity and promotes its interaction with HDAC1.";
RL Oncogene 26:5866-5876(2007).
RN [46]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH NR1D2.
RX PubMed=17996965; DOI=10.1016/j.bbamcr.2007.09.004;
RA Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.;
RT "The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to
RT regulate apolipoprotein CIII promoter.";
RL Biochim. Biophys. Acta 1783:224-236(2008).
RN [47]
RP INTERACTION WITH DHX36.
RX PubMed=18279852; DOI=10.1016/j.yexcr.2008.01.006;
RA Iwamoto F., Stadler M., Chalupnikova K., Oakeley E., Nagamine Y.;
RT "Transcription-dependent nucleolar cap localization and possible nuclear
RT function of DExH RNA helicase RHAU.";
RL Exp. Cell Res. 314:1378-1391(2008).
RN [48]
RP INTERACTION WITH TRAF6.
RX PubMed=18093978; DOI=10.1074/jbc.m706307200;
RA Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L.,
RA Darnay B.G., Ford R.J.;
RT "Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid
RT cells negatively regulates c-Myb-mediated transactivation through small
RT ubiquitin-related modifier-1 modification.";
RL J. Biol. Chem. 283:5081-5089(2008).
RN [49]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [50]
RP IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC2.
RX PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
RA Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E.,
RA Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.;
RT "CDYL bridges REST and histone methyltransferases for gene repression and
RT suppression of cellular transformation.";
RL Mol. Cell 32:718-726(2008).
RN [51]
RP METHYLATION AT LYS-432.
RX PubMed=18438403; DOI=10.1038/nchembio.88;
RA Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R.,
RA Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
RT "Protein lysine methyltransferase G9a acts on non-histone targets.";
RL Nat. Chem. Biol. 4:344-346(2008).
RN [52]
RP FUNCTION, AND INTERACTION WITH RB1 AND SMARCA4/BRG1.
RX PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
RA Qiu Z., Ghosh A.;
RT "A calcium-dependent switch in a CREST-BRG1 complex regulates activity-
RT dependent gene expression.";
RL Neuron 60:775-787(2008).
RN [53]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [54]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [55]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [56]
RP INTERACTION WITH PRDM16 AND SMAD3.
RX PubMed=19049980; DOI=10.1074/jbc.m808989200;
RA Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M.,
RA Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K.,
RA Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T.;
RT "SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal
RT in gastric cancer cells.";
RL J. Biol. Chem. 284:3334-3344(2009).
RN [57]
RP INTERACTION WITH RUVBL2; APPL2; APPL1; CTNNB1 AND HDAC2.
RX PubMed=19433865; DOI=10.1074/jbc.m109.007237;
RA Rashid S., Pilecka I., Torun A., Olchowik M., Bielinska B., Miaczynska M.;
RT "Endosomal adaptor proteins APPL1 and APPL2 are novel activators of beta-
RT catenin/TCF-mediated transcription.";
RL J. Biol. Chem. 284:18115-18128(2009).
RN [58]
RP FUNCTION, INTERACTION WITH TSHZ3, AND IDENTIFICATION IN A TRIMERIC COMPLEX
RP WITH APBB1 AND TSHZ3.
RX PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT caspase-4.";
RL PLoS ONE 4:E5071-E5071(2009).
RN [59]
RP UBIQUITINATION, ACTIVE SITE, INTERACTION WITH CHFR, AND MUTAGENESIS OF
RP HIS-141; PHE-287 AND MET-297.
RX PubMed=19182791; DOI=10.1038/ncb1837;
RA Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J., Chung C.H.,
RA Deshaies R.J., Seol J.H.;
RT "Chfr is linked to tumour metastasis through the downregulation of HDAC1.";
RL Nat. Cell Biol. 11:295-302(2009).
RN [60]
RP INTERACTION WITH SPHK2.
RX PubMed=19729656; DOI=10.1126/science.1176709;
RA Hait N.C., Allegood J., Maceyka M., Strub G.M., Harikumar K.B., Singh S.K.,
RA Luo C., Marmorstein R., Kordula T., Milstien S., Spiegel S.;
RT "Regulation of histone acetylation in the nucleus by sphingosine-1-
RT phosphate.";
RL Science 325:1254-1257(2009).
RN [61]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [62]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-220, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [63]
RP INTERACTION WITH CCAR2.
RX PubMed=21030595; DOI=10.1074/jbc.m110.153270;
RA Chini C.C., Escande C., Nin V., Chini E.N.;
RT "HDAC3 is negatively regulated by the nuclear protein DBC1.";
RL J. Biol. Chem. 285:40830-40837(2010).
RN [64]
RP UBIQUITINATION BY KCTD11.
RX PubMed=20081843; DOI=10.1038/ncb2013;
RA Canettieri G., Di Marcotullio L., Greco A., Coni S., Antonucci L.,
RA Infante P., Pietrosanti L., De Smaele E., Ferretti E., Miele E.,
RA Pelloni M., De Simone G., Pedone E.M., Gallinari P., Giorgi A.,
RA Steinkuhler C., Vitagliano L., Pedone C., Schinin M.E., Screpanti I.,
RA Gulino A.;
RT "Histone deacetylase and Cullin3-REN(KCTD11) ubiquitin ligase interplay
RT regulates Hedgehog signalling through Gli acetylation.";
RL Nat. Cell Biol. 12:132-142(2010).
RN [65]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [66]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [67]
RP INTERACTION WITH SMARCAD1.
RX PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
RA Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N.,
RA Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P.,
RA Mermoud J.E.;
RT "Maintenance of silent chromatin through replication requires SWI/SNF-like
RT chromatin remodeler SMARCAD1.";
RL Mol. Cell 42:285-296(2011).
RN [68]
RP INTERACTION WITH BHLHE40.
RX PubMed=21829689; DOI=10.1371/journal.pone.0023046;
RA Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X.,
RA Chang A.K., Wu H.;
RT "SUMOylation of DEC1 protein regulates its transcriptional activity and
RT enhances its stability.";
RL PLoS ONE 6:E23046-E23046(2011).
RN [69]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [70]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-409; SER-421 AND
RP SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [71]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [72]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444; LYS-457 AND LYS-476, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [73]
RP INTERACTION WITH SMAD4 AND ZBTB7A.
RX PubMed=25514493; DOI=10.1016/j.bbagrm.2014.12.008;
RA Yang Y., Cui J., Xue F., Zhang C., Mei Z., Wang Y., Bi M., Shan D.,
RA Meredith A., Li H., Xu Z.Q.;
RT "Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced
RT transcriptional responses.";
RL Biochim. Biophys. Acta 1849:270-281(2015).
RN [74]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-476, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [75]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444 AND LYS-476, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [76]
RP INTERACTION WITH DNTTIP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25653165; DOI=10.1093/nar/gkv068;
RA Itoh T., Fairall L., Muskett F.W., Milano C.P., Watson P.J., Arnaudo N.,
RA Saleh A., Millard C.J., El-Mezgueldi M., Martino F., Schwabe J.W.;
RT "Structural and functional characterization of a cell cycle associated
RT HDAC1/2 complex reveals the structural basis for complex assembly and
RT nucleosome targeting.";
RL Nucleic Acids Res. 43:2033-2044(2015).
RN [77]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [78]
RP INTERACTION WITH CHD4.
RX PubMed=27616479; DOI=10.1016/j.ajhg.2016.08.001;
RG DDD Study;
RA Weiss K., Terhal P.A., Cohen L., Bruccoleri M., Irving M., Martinez A.F.,
RA Rosenfeld J.A., Machol K., Yang Y., Liu P., Walkiewicz M., Beuten J.,
RA Gomez-Ospina N., Haude K., Fong C.T., Enns G.M., Bernstein J.A., Fan J.,
RA Gotway G., Ghorbani M., van Gassen K., Monroe G.R., van Haaften G.,
RA Basel-Vanagaite L., Yang X.J., Campeau P.M., Muenke M.;
RT "De novo mutations in CHD4, an ATP-dependent chromatin remodeler gene,
RT cause an intellectual disability syndrome with distinctive dysmorphisms.";
RL Am. J. Hum. Genet. 99:934-941(2016).
RN [79]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 136-ALA--GLY-138; HIS-141
RP AND 424-GLU--GLU-426.
RX PubMed=28497810; DOI=10.1038/cr.2017.68;
RA Wei W., Liu X., Chen J., Gao S., Lu L., Zhang H., Ding G., Wang Z.,
RA Chen Z., Shi T., Li J., Yu J., Wong J.;
RT "Class I histone deacetylases are major histone decrotonylases: evidence
RT for critical and broad function of histone crotonylation in
RT transcription.";
RL Cell Res. 27:898-915(2017).
RN [80]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-438; LYS-476 AND LYS-480, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [81]
RP INTERACTION WITH PACS2.
RX PubMed=29656858; DOI=10.1016/j.ajhg.2018.03.005;
RG DDD Study;
RG C4RCD Research Group;
RA Olson H.E., Jean-Marcais N., Yang E., Heron D., Tatton-Brown K.,
RA van der Zwaag P.A., Bijlsma E.K., Krock B.L., Backer E., Kamsteeg E.J.,
RA Sinnema M., Reijnders M.R.F., Bearden D., Begtrup A., Telegrafi A.,
RA Lunsing R.J., Burglen L., Lesca G., Cho M.T., Smith L.A., Sheidley B.R.,
RA Moufawad El Achkar C., Pearl P.L., Poduri A., Skraban C.M., Tarpinian J.,
RA Nesbitt A.I., Fransen van de Putte D.E., Ruivenkamp C.A.L., Rump P.,
RA Chatron N., Sabatier I., De Bellescize J., Guibaud L., Sweetser D.A.,
RA Waxler J.L., Wierenga K.J., Donadieu J., Narayanan V., Ramsey K.M.,
RA Nava C., Riviere J.B., Vitobello A., Tran Mau-Them F., Philippe C.,
RA Bruel A.L., Duffourd Y., Thomas L., Lelieveld S.H., Schuurs-Hoeijmakers J.,
RA Brunner H.G., Keren B., Thevenon J., Faivre L., Thomas G.,
RA Thauvin-Robinet C.;
RT "A recurrent de novo PACS2 heterozygous missense variant causes neonatal-
RT onset developmental epileptic encephalopathy, facial dysmorphism, and
RT cerebellar dysgenesis.";
RL Am. J. Hum. Genet. 102:995-1007(2018).
RN [82]
RP INTERACTION WITH ZNF638.
RX PubMed=30487602; DOI=10.1038/s41586-018-0750-6;
RA Zhu Y., Wang G.Z., Cingoez O., Goff S.P.;
RT "NP220 mediates silencing of unintegrated retroviral DNA.";
RL Nature 564:278-282(2018).
RN [83]
RP INTERACTION WITH SMYD4.
RX PubMed=30110327; DOI=10.1371/journal.pgen.1007578;
RA Xiao D., Wang H., Hao L., Guo X., Ma X., Qian Y., Chen H., Ma J., Zhang J.,
RA Sheng W., Shou W., Huang G., Ma D.;
RT "The roles of SMYD4 in epigenetic regulation of cardiac development in
RT zebrafish.";
RL PLoS Genet. 14:e1007578-e1007578(2018).
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) (PubMed:16762839, PubMed:17704056, PubMed:28497810). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events (PubMed:16762839, PubMed:17704056). Histone
CC deacetylases act via the formation of large multiprotein complexes
CC (PubMed:16762839, PubMed:17704056). Also functions as deacetylase for
CC non-histone targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3
CC (PubMed:12837748, PubMed:16478997, PubMed:17996965, PubMed:19343227).
CC Deacetylates SP proteins, SP1 and SP3, and regulates their function
CC (PubMed:12837748, PubMed:16478997). Component of the BRG1-RB1-HDAC1
CC complex, which negatively regulates the CREST-mediated transcription in
CC resting neurons (PubMed:19081374). Upon calcium stimulation, HDAC1 is
CC released from the complex and CREBBP is recruited, which facilitates
CC transcriptional activation (PubMed:19081374). Deacetylates TSHZ3 and
CC regulates its transcriptional repressor activity (PubMed:19343227).
CC Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional
CC activity of NF-kappa-B (PubMed:17000776). Deacetylates NR1D2 and
CC abrogates the effect of KAT5-mediated relieving of NR1D2 transcription
CC repression activity (PubMed:17996965). Component of a
CC RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase
CC (HDAC) recruitment, a number of genes implicated in multilineage blood
CC cell development (By similarity). Involved in CIART-mediated
CC transcriptional repression of the circadian transcriptional activator:
CC CLOCK-ARNTL/BMAL1 heterodimer (By similarity). Required for the
CC 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
CC (PubMed:28497810). {ECO:0000250|UniProtKB:O09106,
CC ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:16478997,
CC ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:17000776,
CC ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17996965,
CC ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19343227,
CC ECO:0000269|PubMed:28497810}.
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:16762839, ECO:0000269|PubMed:28497810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000269|PubMed:16762839, ECO:0000269|PubMed:28497810};
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:0000305|PubMed:12837748,
CC ECO:0000305|PubMed:16478997, ECO:0000305|PubMed:17996965};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000305|PubMed:12837748, ECO:0000305|PubMed:16478997,
CC ECO:0000305|PubMed:17996965};
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:0000269|PubMed:28497810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000269|PubMed:28497810};
CC -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex composed
CC of HDAC1, HDAC2, RBBP4 and RBBP7 (PubMed:12493763, PubMed:12724404,
CC PubMed:19061646). The core complex associates with MTA2, MBD2, MBD3,
CC MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone
CC deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the
CC SIN3 HDAC complex (PubMed:11102443). Component of a BHC histone
CC deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A,
CC RCOR1/CoREST and PHF21A/BHC80 (PubMed:12493763). The BHC complex may
CC also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I (PubMed:12493763).
CC Component of a mSin3A corepressor complex that contains SIN3A, SAP130,
CC SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2 (PubMed:12724404). Found in
CC a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1
CC and APBB1 is mediated by TSHZ3 (PubMed:19343227). Interacts with TSHZ3
CC (via N-terminus); the interaction is direct (PubMed:19343227).
CC Component of a RCOR/GFI/KDM1A/HDAC complex (By similarity). Part of a
CC complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 (PubMed:17704056).
CC Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and
CC HDAC2 (PubMed:19061646). The large PER complex involved in the histone
CC deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A (By
CC similarity). Associates with the 9-1-1 complex; interacts with HUS1
CC (PubMed:10846170). Found in a complex with DNMT3A and HDAC7 (By
CC similarity). Interacts with the non-histone region of MACROH2A1 (By
CC similarity). Interacts with TRIM28; the interaction recruits HDAC1 to
CC E2F1 and inhibits its acetylation (PubMed:17704056). Interacts with
CC SP1; the interaction deacetylates SP1 and regulates its transcriptional
CC activity (PubMed:16478997). Interacts with SP3; the interaction
CC deacetylates SP3 and regulates its transcriptional activity
CC (PubMed:12837748, PubMed:17548428). In vitro, C(18) ceramides increase
CC this interaction and the subsequent SP3 deacetylation and SP3-mediated
CC repression of the TERT promoter (PubMed:12837748, PubMed:17548428).
CC Interacts with APEX1; the interaction is not dependent on the
CC acetylated status of APEX1 (PubMed:14633989). 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 (By similarity). Interacts with CDKN1A/p21 (By
CC similarity). Interacts with CDK5 complexed to CDK5R1 (p25) (By
CC similarity). Interacts directly with GFI1 and GFI1B (By similarity).
CC Interacts with NR1D2 (via C-terminus) (PubMed:17996965). Interacts with
CC TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG
CC promoter and thus inhibits MYOD1 transcriptional activity (By
CC similarity). Interacts with BAZ2A/TIP5, BANP, BCL6, BCOR, BHLHE40/DEC1,
CC BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX, DDIT3/CHOP, DDX5,
CC DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4, NR4A2/NURR1, MIER1,
CC KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6, PRDM16, RB1, RERE,
CC SAMSN1, SAP30L, SETDB1, SMAD3, SMARCAD1, SMARCA4/BRG1, SMYD2, SUV39H1,
CC TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541
CC (PubMed:10669754, PubMed:17369852, PubMed:19081374, PubMed:19182791,
CC PubMed:21549307, PubMed:11331609, PubMed:11006275, PubMed:10846170,
CC PubMed:12730668, PubMed:18093978, PubMed:11533236, PubMed:10898795,
CC PubMed:10655483, PubMed:16569215, PubMed:16820529, PubMed:17872950,
CC PubMed:12670868, PubMed:21829689, PubMed:10487760, PubMed:11427533,
CC PubMed:19049980, PubMed:15273251, PubMed:15361834, PubMed:17373667,
CC PubMed:16166625, PubMed:15454082, PubMed:17000776, PubMed:15927959,
CC PubMed:15451426, PubMed:12482978). Interacts with KDM5A; this
CC interaction impairs histone deacetylation (By similarity). Interacts
CC with DNTTIP1 (PubMed:25653165). Identified in a histone deacetylase
CC complex that contains DNTTIP1, HDAC1 and MIDEAS; this complex assembles
CC into a tetramer that contains four copies of each protein chain
CC (PubMed:25653165). Interacts with CCAR2 (PubMed:21030595). Interacts
CC with PPHLN1 (PubMed:17963697). Found in a complex with YY1, SIN3A and
CC GON4L (By similarity). Interacts with CHD4 (PubMed:27616479). Found in
CC a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT
CC and TET1 (By similarity). Interacts with SIN3A (By similarity).
CC Interacts with DHX36; this interaction occurs in a RNA-dependent manner
CC (PubMed:18279852). Interacts with ZBTB7A (PubMed:25514493). Interacts
CC with SMAD4; positively regulated by ZBTB7A (PubMed:25514493). Interacts
CC with PACS2 (PubMed:29656858). Forms a complex comprising APPL1, RUVBL2,
CC APPL2, CTNNB1 and HDAC2 (PubMed:19433865). Interacts with ZNF638
CC (PubMed:30487602). Interacts with SPHK2 (PubMed:19729656). Interacts
CC with ERCC6 (PubMed:26030138). Interacts with NSD2 (By similarity).
CC Interacts with SMYD4 (via MYND-type zinc finger) (PubMed:30110327).
CC Interacts with PWWP2A in a MTA1-dependent manner (By similarity).
CC Interacts with PWWP2B (By similarity). Interacts with ZNF516 and BRCC3;
CC these interactions are enhanced in the presence of PWWP2B (By
CC similarity). Interacts with SANBR (via the BTB domain) (By similarity).
CC {ECO:0000250|UniProtKB:O09106, ECO:0000269|PubMed:10487760,
CC ECO:0000269|PubMed:10655483, ECO:0000269|PubMed:10669754,
CC ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:10898795,
CC ECO:0000269|PubMed:11006275, ECO:0000269|PubMed:11102443,
CC ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:11427533,
CC ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:12482978,
CC ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:12670868,
CC ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:12730668,
CC ECO:0000269|PubMed:12837748, ECO:0000269|PubMed:14633989,
CC ECO:0000269|PubMed:15273251, ECO:0000269|PubMed:15361834,
CC ECO:0000269|PubMed:15451426, ECO:0000269|PubMed:15454082,
CC ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16166625,
CC ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16569215,
CC ECO:0000269|PubMed:16820529, ECO:0000269|PubMed:17000776,
CC ECO:0000269|PubMed:17369852, ECO:0000269|PubMed:17373667,
CC ECO:0000269|PubMed:17548428, ECO:0000269|PubMed:17704056,
CC ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:17963697,
CC ECO:0000269|PubMed:17996965, ECO:0000269|PubMed:18093978,
CC ECO:0000269|PubMed:18279852, ECO:0000269|PubMed:19049980,
CC ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:19081374,
CC ECO:0000269|PubMed:19182791, ECO:0000269|PubMed:19343227,
CC ECO:0000269|PubMed:19433865, ECO:0000269|PubMed:19729656,
CC ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:21549307,
CC ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:25514493,
CC ECO:0000269|PubMed:25653165, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:27616479, ECO:0000269|PubMed:29656858,
CC ECO:0000269|PubMed:30110327, ECO:0000269|PubMed:30487602}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 large T antigen.
CC {ECO:0000269|PubMed:17341466}.
CC -!- INTERACTION:
CC Q13547; Q14865: ARID5B; NbExp=6; IntAct=EBI-301834, EBI-1210388;
CC Q13547; Q9C0K0: BCL11B; NbExp=3; IntAct=EBI-301834, EBI-6597578;
CC Q13547; Q9HCU9: BRMS1; NbExp=5; IntAct=EBI-301834, EBI-714781;
CC Q13547; Q6PH81: C16orf87; NbExp=4; IntAct=EBI-301834, EBI-6598617;
CC Q13547; Q14839: CHD4; NbExp=11; IntAct=EBI-301834, EBI-372916;
CC Q13547; P68400: CSNK2A1; NbExp=3; IntAct=EBI-301834, EBI-347804;
CC Q13547; Q9UER7: DAXX; NbExp=2; IntAct=EBI-301834, EBI-77321;
CC Q13547; Q92841-4: DDX17; NbExp=3; IntAct=EBI-301834, EBI-5280703;
CC Q13547; P17844: DDX5; NbExp=4; IntAct=EBI-301834, EBI-351962;
CC Q13547; Q9UJW3: DNMT3L; NbExp=3; IntAct=EBI-301834, EBI-740967;
CC Q13547; Q01094: E2F1; NbExp=2; IntAct=EBI-301834, EBI-448924;
CC Q13547; Q66K89: E4F1; NbExp=3; IntAct=EBI-301834, EBI-1227043;
CC Q13547; Q96KQ7: EHMT2; NbExp=7; IntAct=EBI-301834, EBI-744366;
CC Q13547; Q96D98: EID2B; NbExp=2; IntAct=EBI-301834, EBI-724968;
CC Q13547; Q99684: GFI1; NbExp=4; IntAct=EBI-301834, EBI-949368;
CC Q13547; Q13227: GPS2; NbExp=2; IntAct=EBI-301834, EBI-713355;
CC Q13547; P62805: H4C9; NbExp=3; IntAct=EBI-301834, EBI-302023;
CC Q13547; P51610: HCFC1; NbExp=2; IntAct=EBI-301834, EBI-396176;
CC Q13547; Q92769: HDAC2; NbExp=16; IntAct=EBI-301834, EBI-301821;
CC Q13547; P43355: MAGEA1; NbExp=2; IntAct=EBI-301834, EBI-740978;
CC Q13547; Q9UIS9: MBD1; NbExp=2; IntAct=EBI-301834, EBI-867196;
CC Q13547; O95983: MBD3; NbExp=6; IntAct=EBI-301834, EBI-1783068;
CC Q13547; Q8N108: MIER1; NbExp=8; IntAct=EBI-301834, EBI-3504940;
CC Q13547; Q13330: MTA1; NbExp=12; IntAct=EBI-301834, EBI-714236;
CC Q13547; O94776: MTA2; NbExp=14; IntAct=EBI-301834, EBI-1783035;
CC Q13547; Q9Y618: NCOR2; NbExp=2; IntAct=EBI-301834, EBI-80830;
CC Q13547; P19838: NFKB1; NbExp=5; IntAct=EBI-301834, EBI-300010;
CC Q13547; P06748: NPM1; NbExp=2; IntAct=EBI-301834, EBI-78579;
CC Q13547; Q15466: NR0B2; NbExp=2; IntAct=EBI-301834, EBI-3910729;
CC Q13547; Q9NQX1: PRDM5; NbExp=3; IntAct=EBI-301834, EBI-4292031;
CC Q13547; Q96N64: PWWP2A; NbExp=5; IntAct=EBI-301834, EBI-6597774;
CC Q13547; P06400: RB1; NbExp=16; IntAct=EBI-301834, EBI-491274;
CC Q13547; Q09028: RBBP4; NbExp=8; IntAct=EBI-301834, EBI-620823;
CC Q13547; Q16576: RBBP7; NbExp=7; IntAct=EBI-301834, EBI-352227;
CC Q13547; Q9UKL0: RCOR1; NbExp=11; IntAct=EBI-301834, EBI-926563;
CC Q13547; Q04206: RELA; NbExp=6; IntAct=EBI-301834, EBI-73886;
CC Q13547; O00422: SAP18; NbExp=2; IntAct=EBI-301834, EBI-1044156;
CC Q13547; Q96ST3: SIN3A; NbExp=9; IntAct=EBI-301834, EBI-347218;
CC Q13547; Q9NP50: SINHCAF; NbExp=6; IntAct=EBI-301834, EBI-741906;
CC Q13547; O95863: SNAI1; NbExp=3; IntAct=EBI-301834, EBI-1045459;
CC Q13547; P08047: SP1; NbExp=2; IntAct=EBI-301834, EBI-298336;
CC Q13547; O43463: SUV39H1; NbExp=3; IntAct=EBI-301834, EBI-349968;
CC Q13547; P04637: TP53; NbExp=7; IntAct=EBI-301834, EBI-366083;
CC Q13547; Q05516: ZBTB16; NbExp=2; IntAct=EBI-301834, EBI-711925;
CC Q13547; O95365: ZBTB7A; NbExp=2; IntAct=EBI-301834, EBI-2795384;
CC Q13547; Q92618: ZNF516; NbExp=8; IntAct=EBI-301834, EBI-2799490;
CC Q13547; P29128: BICP0; Xeno; NbExp=2; IntAct=EBI-301834, EBI-11292028;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10846170}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart, pancreas
CC and testis, and lower levels in kidney and brain.
CC -!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic
CC activity. Desumoylated by SENP1. {ECO:0000269|PubMed:11960997,
CC ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15199155}.
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:0000269|PubMed:11602581}.
CC -!- PTM: Ubiquitinated by CHFR, leading to its degradation by the
CC proteasome. Ubiquitinated by KCTD11, leading to proteasomal
CC degradation. {ECO:0000269|PubMed:19182791,
CC ECO:0000269|PubMed:20081843}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; U50079; AAC50475.1; -; mRNA.
DR EMBL; D50405; BAA08909.1; -; mRNA.
DR EMBL; BC000301; AAH00301.1; -; mRNA.
DR CCDS; CCDS360.1; -.
DR RefSeq; NP_004955.2; NM_004964.2.
DR PDB; 4BKX; X-ray; 3.00 A; B=1-482.
DR PDB; 5ICN; X-ray; 3.30 A; B=1-376.
DR PDB; 6Z2J; EM; 4.00 A; C/E=1-482.
DR PDB; 6Z2K; EM; 4.50 A; C/E/I/K=1-482.
DR PDB; 7AO8; EM; 4.50 A; B/E=1-482.
DR PDB; 7AO9; EM; 6.10 A; B/E=1-482.
DR PDB; 7AOA; EM; 19.40 A; B/E=1-482.
DR PDBsum; 4BKX; -.
DR PDBsum; 5ICN; -.
DR PDBsum; 6Z2J; -.
DR PDBsum; 6Z2K; -.
DR PDBsum; 7AO8; -.
DR PDBsum; 7AO9; -.
DR PDBsum; 7AOA; -.
DR AlphaFoldDB; Q13547; -.
DR SASBDB; Q13547; -.
DR SMR; Q13547; -.
DR BioGRID; 109315; 722.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q13547; -.
DR DIP; DIP-24184N; -.
DR IntAct; Q13547; 350.
DR MINT; Q13547; -.
DR STRING; 9606.ENSP00000362649; -.
DR BindingDB; Q13547; -.
DR ChEMBL; CHEMBL325; -.
DR DrugBank; DB12565; Abexinostat.
DR DrugBank; DB01169; Arsenic trioxide.
DR DrugBank; DB05015; Belinostat.
DR DrugBank; DB08868; Fingolimod.
DR DrugBank; DB11830; Mocetinostat.
DR DrugBank; DB06603; Panobinostat.
DR DrugBank; DB05223; Pracinostat.
DR DrugBank; DB06176; Romidepsin.
DR DrugBank; DB02546; Vorinostat.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugCentral; Q13547; -.
DR GuidetoPHARMACOLOGY; 2658; -.
DR GlyGen; Q13547; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q13547; -.
DR MetOSite; Q13547; -.
DR PhosphoSitePlus; Q13547; -.
DR SwissPalm; Q13547; -.
DR BioMuta; HDAC1; -.
DR DMDM; 2498443; -.
DR CPTAC; CPTAC-1248; -.
DR CPTAC; CPTAC-2607; -.
DR EPD; Q13547; -.
DR jPOST; Q13547; -.
DR MassIVE; Q13547; -.
DR PaxDb; Q13547; -.
DR PeptideAtlas; Q13547; -.
DR PRIDE; Q13547; -.
DR ProteomicsDB; 59529; -.
DR TopDownProteomics; Q13547; -.
DR Antibodypedia; 3760; 1620 antibodies from 51 providers.
DR DNASU; 3065; -.
DR Ensembl; ENST00000373548.8; ENSP00000362649.3; ENSG00000116478.12.
DR GeneID; 3065; -.
DR KEGG; hsa:3065; -.
DR MANE-Select; ENST00000373548.8; ENSP00000362649.3; NM_004964.3; NP_004955.2.
DR CTD; 3065; -.
DR DisGeNET; 3065; -.
DR GeneCards; HDAC1; -.
DR HGNC; HGNC:4852; HDAC1.
DR HPA; ENSG00000116478; Low tissue specificity.
DR MIM; 601241; gene.
DR neXtProt; NX_Q13547; -.
DR OpenTargets; ENSG00000116478; -.
DR PharmGKB; PA29226; -.
DR VEuPathDB; HostDB:ENSG00000116478; -.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000154301; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; Q13547; -.
DR OMA; HFGMTHP; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; Q13547; -.
DR TreeFam; TF106171; -.
DR BRENDA; 3.5.1.98; 2681.
DR PathwayCommons; Q13547; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR Reactome; R-HSA-1538133; G0 and Early G1.
DR Reactome; R-HSA-193670; p75NTR negatively regulates cell cycle via SC1.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4641265; Repression of WNT target genes.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9022538; Loss of MECP2 binding ability to 5mC-DNA.
DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR Reactome; R-HSA-9022702; MECP2 regulates transcription of neuronal ligands.
DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SABIO-RK; Q13547; -.
DR SignaLink; Q13547; -.
DR SIGNOR; Q13547; -.
DR BioGRID-ORCS; 3065; 42 hits in 1101 CRISPR screens.
DR ChiTaRS; HDAC1; human.
DR GeneWiki; HDAC1; -.
DR GenomeRNAi; 3065; -.
DR Pharos; Q13547; Tclin.
DR PRO; PR:Q13547; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13547; protein.
DR Bgee; ENSG00000116478; Expressed in colonic mucosa and 209 other tissues.
DR ExpressionAtlas; Q13547; baseline and differential.
DR Genevisible; Q13547; HS.
DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; IDA:BHF-UCL.
DR GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0160009; F:histone decrotonylase activity; IDA:UniProtKB.
DR GO; GO:0035851; F:Krueppel-associated box domain binding; IEA:Ensembl.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:CAFA.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IGI:UniProtKB.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISS:BHF-UCL.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IGI:BHF-UCL.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISS:BHF-UCL.
DR GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR GO; GO:0009913; P:epidermal cell differentiation; ISS:BHF-UCL.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0061198; P:fungiform papilla formation; ISS:BHF-UCL.
DR GO; GO:0060789; P:hair follicle placode formation; ISS:BHF-UCL.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0070932; P:histone H3 deacetylation; IDA:BHF-UCL.
DR GO; GO:0070933; P:histone H4 deacetylation; IDA:BHF-UCL.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IMP:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:BHF-UCL.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; IMP:BHF-UCL.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
DR GO; GO:1900221; P:regulation of amyloid-beta clearance; IC:ARUK-UCL.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:0052548; P:regulation of endopeptidase activity; IMP:ARUK-UCL.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:ARUK-UCL.
DR DisProt; DP02233; -.
DR Gene3D; 3.40.800.20; -; 1.
DR IDEAL; IID00565; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Biological rhythms; Chromatin regulator;
KW Hydrolase; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; S-nitrosylation; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..482
FT /note="Histone deacetylase 1"
FT /id="PRO_0000114687"
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:0000269|PubMed:19182791,
FT ECO:0000269|PubMed:28497810"
FT MOD_RES 74
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
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:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 421
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:11602581,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 423
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:11602581,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="N6-methylated lysine; by EHMT2"
FT /evidence="ECO:0000269|PubMed:18438403"
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:0007744|PubMed:28112733"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:11960997"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297"
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:0007744|PubMed:25218447"
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:0000269|PubMed:11960997"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 136..138
FT /note="AGG->VRPP: Impaired protein deacetylase activity
FT without affecting the protein decrotonylase activity."
FT /evidence="ECO:0000269|PubMed:28497810"
FT MUTAGEN 141
FT /note="H->A: Abolishes histone deacetylase and
FT decrotonylase activities."
FT /evidence="ECO:0000269|PubMed:19182791,
FT ECO:0000269|PubMed:28497810"
FT MUTAGEN 287
FT /note="F->Y: Abolishes interaction with CHFR; when
FT associated with I-297."
FT /evidence="ECO:0000269|PubMed:19182791"
FT MUTAGEN 297
FT /note="M->I: Abolishes interaction with CHFR; when
FT associated with Y-287."
FT /evidence="ECO:0000269|PubMed:19182791"
FT MUTAGEN 391..482
FT /note="Missing: Strongly decreases deacetylase activity,
FT and disrupts interaction with NuRD and SIN3 complexes."
FT MUTAGEN 421
FT /note="S->A: Strongly decreases deacetylase activity, and
FT disrupts interaction with NuRD and SIN3 complexes."
FT /evidence="ECO:0000269|PubMed:11602581"
FT MUTAGEN 421
FT /note="S->D,E: Slightly decreases deacetylase activity."
FT /evidence="ECO:0000269|PubMed:11602581"
FT MUTAGEN 423
FT /note="S->A: Strongly decreases deacetylase activity, and
FT disrupts interaction with NuRD and SIN3 complexes."
FT /evidence="ECO:0000269|PubMed:11602581"
FT MUTAGEN 423
FT /note="S->D,E: Decreases deacetylase activity."
FT /evidence="ECO:0000269|PubMed:11602581"
FT MUTAGEN 424..426
FT /note="EEE->AEA: Abolished histone deacetylase and
FT decrotonylase activities."
FT /evidence="ECO:0000269|PubMed:28497810"
FT MUTAGEN 424
FT /note="E->A: Slightly decreases deacetylase activity, no
FT effect on interaction with NuRD and SIN3 complexes."
FT /evidence="ECO:0000269|PubMed:11602581"
FT MUTAGEN 425
FT /note="E->A: No effect on deacetylase activity, no effect
FT on interaction with NuRD and SIN3 complexes."
FT /evidence="ECO:0000269|PubMed:11602581"
FT MUTAGEN 426
FT /note="E->A: Decreases deacetylase activity, and disrupts
FT interaction with NuRD and SIN3 complexes."
FT /evidence="ECO:0000269|PubMed:11602581"
FT CONFLICT 312
FT /note="W -> R (in Ref. 2; BAA08909)"
FT /evidence="ECO:0000305"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:5ICN"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 106..125
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 234..252
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:4BKX"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 305..319
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4BKX"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:4BKX"
FT HELIX 356..371
FT /evidence="ECO:0007829|PDB:4BKX"
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
