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 11-NOV-2015, entry version 189. DE RecName: Full=Histone deacetylase 1; DE Short=HD1; DE EC=3.5.1.98; GN Name=HDAC1; Synonyms=RPD3L1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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; RA Furukawa Y., Kawakami T., Sudo K., Inazawa J., Matsumine A., RA Akiyama T., Nakamura Y.; RT "Isolation and mapping of a human gene (RPD3L1) that is homologous to RT RPD3, 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 RT project: 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 RT G2/M 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 RT deacetylases 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 RT repression 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 RT noncatalytic 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 AND RP SER-423, 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., RA Hon M., Evans R.M.; RT "Sharp, an inducible cofactor that integrates nuclear receptor RT repression 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 RT SANT 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 RT 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 RT with multiple histone deacetylases and binds mSin3A through its RT oligomerization 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 RT of the 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 RP COMPLEX WITH PHF21A; HDAC2; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217; RP ZMYM3; KIAA0182 AND GTF2I. 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; RP SUDS3; 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 RT mSin3A 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 RT of 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., RA Boss J.M., 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 RT prevents its ubiquitination and regulates its interaction with the RT histone deacetylase, 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 RT through 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., RA Jingu H., 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 RT of the 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 RT gene 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 RP SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [34] 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 [35] RP FUNCTION, 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 [36] 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 RT targets Sin3A to the nucleolus."; RL Nucleic Acids Res. 34:3288-3298(2006). RN [37] 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 RT cycle progression."; RL Biochem. Biophys. Res. Commun. 364:930-936(2007). RN [38] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION RP BY 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 RT cancer cells: identification of phosphoproteins in the LNCaP cell RT line."; RL Electrophoresis 28:2027-2034(2007). RN [39] 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 RT reverse transcriptase promoter via deacetylation of Sp3 by histone RT deacetylase 1."; RL FASEB J. 21:3386-3397(2007). RN [40] 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., RA Freemont P., Taylor-Papadimitriou J.; RT "Breast cancer associated transcriptional repressor PLU-1/JARID1B RT interacts directly with histone deacetylases."; RL Int. J. Cancer 121:265-275(2007). RN [41] 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 [42] 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 [43] 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 [44] 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 [45] RP FUNCTION, 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., RA 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 [46] 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., RA Fu L., Darnay B.G., Ford R.J.; RT "Nuclear tumor necrosis factor receptor-associated factor 6 in RT lymphoid cells negatively regulates c-Myb-mediated transactivation RT through small ubiquitin-related modifier-1 modification."; RL J. Biol. Chem. 283:5081-5089(2008). RN [47] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION RP BY 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [48] 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., RA Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., RA Shi Y.; RT "CDYL bridges REST and histone methyltransferases for gene repression RT and suppression of cellular transformation."; RL Mol. Cell 32:718-726(2008). RN [49] RP METHYLATION AT LYS-432. RX PubMed=18438403; DOI=10.1038/nchembio.88; RA Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., RA Jurkowska R., 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 [50] 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 RT activity-dependent gene expression."; RL Neuron 60:775-787(2008). RN [51] 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 [52] 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 RT enrichment and fractionation of phosphopeptides with strong anion RT exchange chromatography."; RL Proteomics 8:1346-1361(2008). RN [53] 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., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [54] 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., RA Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., RA Imamura T.; RT "SKI and MEL1 cooperate to inhibit transforming growth factor-beta RT signal in gastric cancer cells."; RL J. Biol. Chem. 284:3334-3344(2009). RN [55] RP FUNCTION, INTERACTION WITH TSHZ3, AND IDENTIFICATION IN A TRIMERIC RP COMPLEX 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 [56] RP UBIQUITINATION, INTERACTION WITH CHFR, AND MUTAGENESIS OF HIS-141; RP 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., RA Chung C.H., Deshaies R.J., Seol J.H.; RT "Chfr is linked to tumour metastasis through the downregulation of RT HDAC1."; RL Nat. Cell Biol. 11:295-302(2009). RN [57] 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 [58] 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., RA Walther T.C., 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 [59] 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 [60] 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 RT interplay regulates Hedgehog signalling through Gli acetylation."; RL Nat. Cell Biol. 12:132-142(2010). RN [61] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND RP SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [62] 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., RA Buerckstuemmer T., 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 [63] 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., RA Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., RA Varga-Weisz P., Mermoud J.E.; RT "Maintenance of silent chromatin through replication requires SWI/SNF- RT like chromatin remodeler SMARCAD1."; RL Mol. Cell 42:285-296(2011). RN [64] 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 RT and enhances its stability."; RL PLoS ONE 6:E23046-E23046(2011). RN [65] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND RP SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [66] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [67] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444; LYS-457 AND LYS-476, RP AND 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 [68] 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., RA Arnaudo N., Saleh A., Millard C.J., El-Mezgueldi M., Martino F., RA 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). CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on CC the N-terminal part of the core histones (H2A, H2B, H3 and H4). CC Histone deacetylation gives a tag for epigenetic repression and CC plays an important role in transcriptional regulation, cell cycle CC progression and developmental events. Histone deacetylases act via CC the formation of large multiprotein complexes. Deacetylates SP CC proteins, SP1 and SP3, and regulates their function. Component of CC the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST- CC mediated transcription in resting neurons. Upon calcium CC stimulation, HDAC1 is released from the complex and CREBBP is CC recruited, which facilitates transcriptional activation. CC Deacetylates TSHZ3 and regulates its transcriptional repressor CC activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the CC transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and CC abrogates the effect of KAT5-mediated relieving of NR1D2 CC transcription repression activity. Component of a CC RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone CC deacetylase (HDAC) recruitment, a number of genes implicated in CC multilineage blood cell development. Involved in CIART-mediated CC transcriptional repression of the circadian transcriptional CC activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the CC transcriptional repression of circadian target genes, such as CC PER1, mediated by the large PER complex or CRY1 through histone CC deacetylation. {ECO:0000269|PubMed:12837748, CC ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:17000776, CC ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17996965, CC ECO:0000269|PubMed:19081374, ECO:0000269|PubMed:19343227}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of CC a histone to yield a deacetylated histone. CC -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex CC composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex CC associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form CC the nucleosome remodeling and histone deacetylation (NuRD) CC complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC CC complex. Component of a BHC histone deacetylase complex that CC contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and CC PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, CC ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex CC that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and CC HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the CC interaction between HDAC1 and APBB1 is mediated by TSHZ3. CC Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex CC composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex CC containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large CC PER complex involved in the histone deacetylation is composed of CC at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1 CC complex; interacts with HUS1. Found in a complex with DNMT3A and CC HDAC7. Interacts with the non-histone region of H2AFY. Interacts CC with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits CC its acetylation. Interacts with SP1; the interaction deacetylates CC SP1 and regulates its transcriptional activity. Interacts with CC SP3; the interaction deacetylates SP3 and regulates its CC transcriptional activity. In vitro, C(18) ceramides increase this CC interaction and the subsequent SP3 deacetylation and SP3-mediated CC repression of the TERT promoter. Interacts with TSHZ3 (via N- CC terminus); the interaction is direct. Interacts with APEX1; the CC interaction is not dependent on the acetylated status of APEX1. CC Interacts with C10orf90/FATS (via its N-terminal); the interaction CC prevents binding of HDAC1 to CDKN1A/p21 and facilitates the CC acetylation and stabilization of CDKN1A/p21. Interacts with CC CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25). CC Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via CC C-terminus). Interacts with TSC22D3 isoform 1; this interaction CC affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 CC transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6, CC BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, CC DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, CC NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, CC PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, CC SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, CC ZMYND15, ZNF431 and ZNF541. Interacts with KDM5A (By similarity). CC Interacts with DNTTIP1 (PubMed:25653165). Identified in a histone CC deacetylase complex that contains DNTTIP1, HDAC1 and ELMSAN1; this CC complex assembles into a tetramer that contains four copies of CC each protein chain (PubMed:25653165). Interacts with CCAR2 CC (PubMed:21030595). Interacts with PPHLN1 (PubMed:17963697). 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:17341466, ECO:0000269|PubMed:17369852, CC ECO:0000269|PubMed:17373667, ECO:0000269|PubMed:17548428, CC ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:17872950, CC ECO:0000269|PubMed:17963697, ECO:0000269|PubMed:17996965, CC ECO:0000269|PubMed:18093978, 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:21030595, ECO:0000269|PubMed:21549307, CC ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:25653165}. CC -!- INTERACTION: CC Q9UKG1:APPL1; NbExp=2; IntAct=EBI-301834, EBI-741243; CC Q14865:ARID5B; NbExp=4; IntAct=EBI-301834, EBI-1210388; CC Q9C0K0:BCL11B; NbExp=3; IntAct=EBI-301834, EBI-6597578; CC Q9HCU9:BRMS1; NbExp=4; IntAct=EBI-301834, EBI-714781; CC Q6PH81:C16orf87; NbExp=3; IntAct=EBI-301834, EBI-6598617; CC Q14839:CHD4; NbExp=6; IntAct=EBI-301834, EBI-372916; CC P68400:CSNK2A1; NbExp=2; IntAct=EBI-301834, EBI-347804; CC Q9UER7:DAXX; NbExp=2; IntAct=EBI-301834, EBI-77321; CC Q92841-4:DDX17; NbExp=3; IntAct=EBI-301834, EBI-5280703; CC P17844:DDX5; NbExp=4; IntAct=EBI-301834, EBI-351962; CC Q7L2E3:DHX30; NbExp=3; IntAct=EBI-301834, EBI-1211456; CC Q9UJW3:DNMT3L; NbExp=3; IntAct=EBI-301834, EBI-740967; CC Q66K89:E4F1; NbExp=3; IntAct=EBI-301834, EBI-1227043; CC Q96KQ7:EHMT2; NbExp=3; IntAct=EBI-301834, EBI-744366; CC Q8N140:EID3; NbExp=2; IntAct=EBI-301834, EBI-744483; CC Q9NP50:FAM60A; NbExp=4; IntAct=EBI-301834, EBI-741906; CC Q99684:GFI1; NbExp=4; IntAct=EBI-301834, EBI-949368; CC P51610:HCFC1; NbExp=2; IntAct=EBI-301834, EBI-396176; CC Q92769:HDAC2; NbExp=10; IntAct=EBI-301834, EBI-301821; CC P62805:HIST2H4B; NbExp=2; IntAct=EBI-301834, EBI-302023; CC P43355:MAGEA1; NbExp=2; IntAct=EBI-301834, EBI-740978; CC Q9UIS9:MBD1; NbExp=2; IntAct=EBI-301834, EBI-867196; CC Q8N108:MIER1; NbExp=7; IntAct=EBI-301834, EBI-3504940; CC Q13330:MTA1; NbExp=4; IntAct=EBI-301834, EBI-714236; CC Q9Y618:NCOR2; NbExp=2; IntAct=EBI-301834, EBI-80830; CC P19838:NFKB1; NbExp=5; IntAct=EBI-301834, EBI-300010; CC P06748:NPM1; NbExp=2; IntAct=EBI-301834, EBI-78579; CC Q9Y5X4:NR2E3; NbExp=2; IntAct=EBI-301834, EBI-7216962; CC Q9NQX1:PRDM5; NbExp=3; IntAct=EBI-301834, EBI-4292031; CC Q96N64:PWWP2A; NbExp=4; IntAct=EBI-301834, EBI-6597774; CC P06400:RB1; NbExp=4; IntAct=EBI-301834, EBI-491274; CC Q09028:RBBP4; NbExp=6; IntAct=EBI-301834, EBI-620823; CC Q16576:RBBP7; NbExp=5; IntAct=EBI-301834, EBI-352227; CC Q04206:RELA; NbExp=6; IntAct=EBI-301834, EBI-73886; CC O00422:SAP18; NbExp=2; IntAct=EBI-301834, EBI-1044156; CC O95863:SNAI1; NbExp=3; IntAct=EBI-301834, EBI-1045459; CC O43463:SUV39H1; NbExp=3; IntAct=EBI-301834, EBI-349968; CC P04637:TP53; NbExp=7; IntAct=EBI-301834, EBI-366083; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10846170}. CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart, CC pancreas 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 CC activity and interactions with NuRD and SIN3 complexes. CC Phosphorylated by CDK5. {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.88556; -. DR PDB; 1TYI; Model; -; A=1-482. DR PDB; 4BKX; X-ray; 3.00 A; B=1-482. DR PDBsum; 1TYI; -. DR PDBsum; 4BKX; -. DR ProteinModelPortal; Q13547; -. DR SMR; Q13547; 8-376. DR BioGrid; 109315; 494. DR DIP; DIP-24184N; -. DR IntAct; Q13547; 174. DR MINT; MINT-90475; -. DR STRING; 9606.ENSP00000362649; -. DR BindingDB; Q13547; -. DR ChEMBL; CHEMBL2093865; -. DR DrugBank; DB02546; Vorinostat. DR GuidetoPHARMACOLOGY; 2658; -. DR PhosphoSite; Q13547; -. DR BioMuta; HDAC1; -. DR DMDM; 2498443; -. DR MaxQB; Q13547; -. DR PaxDb; Q13547; -. DR PeptideAtlas; Q13547; -. DR PRIDE; Q13547; -. DR DNASU; 3065; -. DR Ensembl; ENST00000373548; ENSP00000362649; ENSG00000116478. DR GeneID; 3065; -. DR KEGG; hsa:3065; -. DR UCSC; uc001bvb.1; human. DR CTD; 3065; -. DR GeneCards; HDAC1; -. DR HGNC; HGNC:4852; HDAC1. DR HPA; CAB005017; -. DR HPA; CAB068191; -. DR HPA; HPA029693; -. DR MIM; 601241; gene. DR neXtProt; NX_Q13547; -. DR PharmGKB; PA29226; -. DR eggNOG; KOG1342; Eukaryota. DR eggNOG; COG0123; LUCA. DR HOGENOM; HOG000225180; -. DR HOVERGEN; HBG057112; -. DR InParanoid; Q13547; -. DR KO; K06067; -. DR OMA; HASCVKF; -. DR OrthoDB; EOG7DNNTW; -. DR PhylomeDB; Q13547; -. DR TreeFam; TF106171; -. DR BRENDA; 3.5.1.98; 2681. 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-3769402; deactivation of the beta-catenin transactivating complex. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-4641265; repression of WNT target genes. DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SABIO-RK; Q13547; -. DR ChiTaRS; HDAC1; human. DR GeneWiki; HDAC1; -. DR GenomeRNAi; 3065; -. DR NextBio; 12125; -. DR PRO; PR:Q13547; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; Q13547; -. DR CleanEx; HS_HDAC1; -. 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:0000118; C:histone deacetylase complex; TAS:UniProtKB. DR GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB. 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:0043234; C:protein complex; IDA:UniProtKB. DR GO; GO:0016580; C:Sin3 complex; IDA:BHF-UCL. DR GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB. DR GO; GO:0001047; F:core promoter binding; IDA:UniProtKB. DR GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0004407; F:histone deacetylase activity; IMP:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL. DR GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC. DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB. DR GO; GO:0033558; F:protein deacetylase activity; IDA:UniProtKB. DR GO; GO:0047485; F:protein N-terminus binding; IDA:MGI. DR GO; GO:0070491; F:repressing transcription factor binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL. DR GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB. DR GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0016568; P:chromatin modification; TAS:UniProtKB. DR GO; GO:0006325; P:chromatin organization; TAS:Reactome. DR GO; GO:0006338; P:chromatin remodeling; IC:BHF-UCL. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0042733; P:embryonic digit morphogenesis; ISS:BHF-UCL. 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:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0060789; P:hair follicle placode formation; ISS:BHF-UCL. DR GO; GO:0016575; P:histone deacetylation; IMP:UniProtKB. 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:0000278; P:mitotic cell cycle; TAS:Reactome. 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:0045786; P:negative regulation of cell cycle; TAS:Reactome. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO. DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:BHF-UCL. DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL. DR GO; GO:0010870; P:positive regulation of receptor biosynthetic process; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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:0040029; P:regulation of gene expression, epigenetic; TAS:Reactome. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR GO; GO:0006351; P:transcription, DNA-templated; TAS:Reactome. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 3.40.800.20; -; 1. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR003084; His_deacetylse_1. DR InterPro; IPR023801; His_deacetylse_dom. DR PANTHER; PTHR10625; PTHR10625; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037913; His_deacetylse_1; 1. DR PRINTS; PR01270; HDASUPER. DR PRINTS; PR01271; HISDACETLASE. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Biological rhythms; Chromatin regulator; KW Complete proteome; Host-virus interaction; Hydrolase; Isopeptide bond; KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1 482 Histone deacetylase 1. FT /FTId=PRO_0000114687. FT REGION 9 321 Histone deacetylase. FT ACT_SITE 141 141 FT MOD_RES 74 74 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 220 220 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 393 393 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:17487921, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 421 421 Phosphoserine; by CK2. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18318008, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000269|PubMed:11602581}. FT MOD_RES 423 423 Phosphoserine; by CK2. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18318008, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000269|PubMed:11602581}. FT MOD_RES 432 432 N6-methylated lysine; by EHMT2. FT {ECO:0000269|PubMed:18438403}. FT CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO); FT alternate. {ECO:0000269|PubMed:11960997}. FT CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT CROSSLNK 457 457 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO); FT alternate. {ECO:0000269|PubMed:11960997}. FT CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT MUTAGEN 141 141 H->A: Abolishes histone deacetylase FT activity. {ECO:0000269|PubMed:19182791}. FT MUTAGEN 287 287 F->Y: Abolishes interaction with CHFR; FT when associated with I-297. FT {ECO:0000269|PubMed:19182791}. FT MUTAGEN 297 297 M->I: Abolishes interaction with CHFR; FT when associated with Y-287. FT {ECO:0000269|PubMed:19182791}. FT MUTAGEN 391 482 Missing: Strongly decreases deacetylase FT activity, and disrupts interaction with FT NuRD and SIN3 complexes. FT MUTAGEN 421 421 S->A: Strongly decreases deacetylase FT activity, and disrupts interaction with FT NuRD and SIN3 complexes. FT {ECO:0000269|PubMed:11602581}. FT MUTAGEN 421 421 S->D,E: Slightly decreases deacetylase FT activity. {ECO:0000269|PubMed:11602581}. FT MUTAGEN 423 423 S->A: Strongly decreases deacetylase FT activity, and disrupts interaction with FT NuRD and SIN3 complexes. FT {ECO:0000269|PubMed:11602581}. FT MUTAGEN 423 423 S->D,E: Decreases deacetylase activity. FT {ECO:0000269|PubMed:11602581}. FT MUTAGEN 424 424 E->A: Slightly decreases deacetylase FT activity, no effect on interaction with FT NuRD and SIN3 complexes. FT MUTAGEN 425 425 E->A: No effect on deacetylase activity, FT no effect on interaction with NuRD and FT SIN3 complexes. FT MUTAGEN 426 426 E->A: Decreases deacetylase activity, and FT disrupts interaction with NuRD and SIN3 FT complexes. FT CONFLICT 312 312 W -> R (in Ref. 2; BAA08909). FT {ECO:0000305}. FT STRAND 11 14 {ECO:0000244|PDB:4BKX}. FT HELIX 19 21 {ECO:0000244|PDB:4BKX}. FT HELIX 33 44 {ECO:0000244|PDB:4BKX}. FT HELIX 48 50 {ECO:0000244|PDB:4BKX}. FT STRAND 51 56 {ECO:0000244|PDB:4BKX}. FT HELIX 61 64 {ECO:0000244|PDB:4BKX}. FT TURN 65 67 {ECO:0000244|PDB:4BKX}. FT HELIX 70 78 {ECO:0000244|PDB:4BKX}. FT TURN 83 86 {ECO:0000244|PDB:4BKX}. FT HELIX 88 94 {ECO:0000244|PDB:4BKX}. FT TURN 97 99 {ECO:0000244|PDB:4BKX}. FT HELIX 106 125 {ECO:0000244|PDB:4BKX}. FT STRAND 130 136 {ECO:0000244|PDB:4BKX}. FT STRAND 151 153 {ECO:0000244|PDB:4BKX}. FT HELIX 155 163 {ECO:0000244|PDB:4BKX}. FT TURN 164 166 {ECO:0000244|PDB:4BKX}. FT STRAND 170 174 {ECO:0000244|PDB:4BKX}. FT STRAND 176 178 {ECO:0000244|PDB:4BKX}. FT HELIX 181 186 {ECO:0000244|PDB:4BKX}. FT TURN 187 189 {ECO:0000244|PDB:4BKX}. FT STRAND 191 200 {ECO:0000244|PDB:4BKX}. FT STRAND 205 207 {ECO:0000244|PDB:4BKX}. FT HELIX 217 219 {ECO:0000244|PDB:4BKX}. FT STRAND 223 228 {ECO:0000244|PDB:4BKX}. FT HELIX 234 252 {ECO:0000244|PDB:4BKX}. FT STRAND 255 260 {ECO:0000244|PDB:4BKX}. FT HELIX 263 265 {ECO:0000244|PDB:4BKX}. FT HELIX 278 289 {ECO:0000244|PDB:4BKX}. FT STRAND 295 298 {ECO:0000244|PDB:4BKX}. FT HELIX 305 319 {ECO:0000244|PDB:4BKX}. FT HELIX 334 336 {ECO:0000244|PDB:4BKX}. FT TURN 338 340 {ECO:0000244|PDB:4BKX}. FT HELIX 356 371 {ECO:0000244|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 //