ID HDAC1_MOUSE Reviewed; 482 AA. AC O09106; P97476; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 229. DE RecName: Full=Histone deacetylase 1 {ECO:0000303|PubMed:9271381}; DE Short=HD1 {ECO:0000303|PubMed:9271381}; DE EC=3.5.1.98 {ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:21960634, ECO:0000305|PubMed:30279482}; DE AltName: Full=Protein deacetylase HDAC1; DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547}; DE AltName: Full=Protein decrotonylase HDAC1; DE EC=3.5.1.- {ECO:0000269|PubMed:30279482}; GN Name=Hdac1 {ECO:0000303|PubMed:12198165, ECO:0000312|MGI:MGI:108086}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fibroblast; RX PubMed=9271381; DOI=10.1128/mcb.17.9.5033; RA Bartl S., Taplick J., Lagger G., Khier H., Kuchler K., Seiser C.; RT "Identification of mouse histone deacetylase 1 as a growth factor-inducible RT gene."; RL Mol. Cell. Biol. 17:5033-5043(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Johnson C.A.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP INTERACTION WITH SAP30. RX PubMed=9702189; DOI=10.1016/s1097-2765(00)80111-2; RA Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., RA Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., RA Ayer D.E., Eisenman R.N.; RT "SAP30, a component of the mSin3 corepressor complex involved in N-CoR- RT mediated repression by specific transcription factors."; RL Mol. Cell 2:33-42(1998). RN [4] RP FUNCTION, INTERACTION WITH DNMT1, AND CATALYTIC ACTIVITY. RX PubMed=10615135; DOI=10.1038/71750; RA Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T.; RT "DNA methyltransferase Dnmt1 associates with histone deacetylase RT activity."; RL Nat. Genet. 24:88-91(2000). RN [5] RP INTERACTION WITH HDAC7. RX PubMed=10984530; DOI=10.1073/pnas.97.19.10330; RA Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.; RT "Identification of a nuclear domain with deacetylase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000). RN [6] RP INTERACTION WITH MSX3, AND SUBCELLULAR LOCATION. RX PubMed=11115394; RA Mehra-Chaudhary R., Matsui H., Raghow R.; RT "Msx3 protein recruits histone deacetylase to down-regulate the Msx1 RT promoter."; RL Biochem. J. 353:13-22(2001). RN [7] RP INTERACTION WITH HDAC9. RX PubMed=11022042; DOI=10.1074/jbc.m007364200; RA Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.; RT "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting RT transcription repressor (MITR) contributes to transcriptional repression of RT the MEF2 transcription factor."; RL J. Biol. Chem. 276:35-39(2001). RN [8] 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 [9] RP INTERACTION WITH BAZ2A. RX PubMed=12198165; DOI=10.1093/emboj/cdf460; RA Zhou Y., Santoro R., Grummt I.; RT "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene RT promoter and represses RNA polymerase I transcription."; RL EMBO J. 21:4632-4640(2002). RN [10] RP INTERACTION WITH SIN3B. RX PubMed=11909966; DOI=10.1128/mcb.22.8.2743-2750.2002; RA Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr., RA Chen K., DePinho R.A.; RT "Identification of mammalian Sds3 as an integral component of the RT Sin3/histone deacetylase corepressor complex."; RL Mol. Cell. Biol. 22:2743-2750(2002). RN [11] RP INTERACTION WITH SUV39H1. RX PubMed=11788710; DOI=10.1093/nar/30.2.475; RA Vaute O., Nicolas E., Vandel L., Trouche D.; RT "Functional and physical interaction between the histone methyl transferase RT Suv39H1 and histone deacetylases."; RL Nucleic Acids Res. 30:475-481(2002). RN [12] RP INTERACTION WITH SETDB1. RX PubMed=12398767; DOI=10.1042/bj20020854; RA Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L., RA Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.; RT "An ERG (ets-related gene)-associated histone methyltransferase interacts RT with histone deacetylases 1/2 and transcription co-repressors mSin3A/B."; RL Biochem. J. 369:651-657(2003). RN [13] RP IDENTIFICATION IN A COMPLEX WITH DNMT3A. RX PubMed=12616525; DOI=10.1002/jcb.10457; RA Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.; RT "Biochemical fractionation reveals association of DNA methyltransferase RT (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a histone H3 RT methyltransferase and Hdac1."; RL J. Cell. Biochem. 88:855-864(2003). RN [14] RP INTERACTION WITH RERE. RX PubMed=14645126; DOI=10.1242/dev.00908; RA Zoltewicz J.S., Stewart N.J., Leung R., Peterson A.S.; RT "Atrophin 2 recruits histone deacetylase and is required for the function RT of multiple signaling centers during mouse embryogenesis."; RL Development 131:3-14(2004). RN [15] RP INTERACTION WITH PHB2. RX PubMed=15140878; DOI=10.1074/jbc.m312300200; RA Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V., Seiser C.; RT "Transcriptional regulation by the repressor of estrogen receptor activity RT via recruitment of histone deacetylases."; RL J. Biol. Chem. 279:24834-24843(2004). RN [16] RP FUNCTION IN CIRCADIAN CLOCK, AND INTERACTION WITH CRY1. RX PubMed=15226430; DOI=10.1128/mcb.24.14.6278-6287.2004; RA Naruse Y., Oh-hashi K., Iijima N., Naruse M., Yoshioka H., Tanaka M.; RT "Circadian and light-induced transcription of clock gene Per1 depends on RT histone acetylation and deacetylation."; RL Mol. Cell. Biol. 24:6278-6287(2004). RN [17] RP INTERACTION WITH KLF1, AND FUNCTION. RX PubMed=15542849; DOI=10.1128/mcb.24.23.10416-10424.2004; RA Chen X., Bieker J.J.; RT "Stage-specific repression by the EKLF transcriptional activator."; RL Mol. Cell. Biol. 24:10416-10424(2004). RN [18] RP INTERACTION WITH NRIP1. RX PubMed=15060175; DOI=10.1093/nar/gkh524; RA Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., RA Khochbin S., Jalaguier S., Cavailles V.; RT "Multiple domains of the receptor-interacting protein 140 contribute to RT transcription inhibition."; RL Nucleic Acids Res. 32:1957-1966(2004). RN [19] RP INTERACTION WITH BAZ2A. RX PubMed=16085498; DOI=10.1016/j.cub.2005.06.057; RA Zhou Y., Grummt I.; RT "The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 RT and is sufficient for rDNA silencing."; RL Curr. Biol. 15:1434-1438(2005). RN [20] RP INTERACTION WITH MACROH2A1. RX PubMed=16107708; DOI=10.1128/mcb.25.17.7616-7624.2005; RA Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R., RA Khochbin S., Luger K.; RT "Structural characterization of the histone variant macroH2A."; RL Mol. Cell. Biol. 25:7616-7624(2005). RN [21] 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 [22] RP INTERACTION WITH HDAC9, AND TISSUE SPECIFICITY. RX PubMed=15711539; DOI=10.1038/nn1408; RA Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N., Schaeffer L.; RT "Histone deacetylase 9 couples neuronal activity to muscle chromatin RT acetylation and gene expression."; RL Nat. Neurosci. 8:313-321(2005). RN [23] RP INTERACTION WITH SMYD2. RX PubMed=16805913; DOI=10.1186/1476-4598-5-26; RA Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.; RT "Identification and characterization of Smyd2: a split SET/MYND domain- RT containing histone H3 lysine 36-specific methyltransferase that interacts RT with the Sin3 histone deacetylase complex."; RL Mol. Cancer 5:26-26(2006). RN [24] RP INTERACTION WITH PRDM6. RX PubMed=16537907; DOI=10.1128/mcb.26.7.2626-2636.2006; RA Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G., RA Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.; RT "PRISM/PRDM6, a transcriptional repressor that promotes the proliferative RT gene program in smooth muscle cells."; RL Mol. Cell. Biol. 26:2626-2636(2006). RN [25] RP INTERACTION WITH HDAC9. RX PubMed=16611996; DOI=10.1128/mcb.26.9.3550-3564.2006; RA Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R., RA Olson E.N., D'Mello S.R.; RT "Neuroprotection by histone deacetylase-related protein."; RL Mol. Cell. Biol. 26:3550-3564(2006). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY AS A COMPONENT OF A GFI-RCOR-KDM1A-HDAC RP COMPLEX, INTERACTION WITH GFI1 AND GFI1B, AND FUNCTION. RX PubMed=17707228; DOI=10.1016/j.molcel.2007.06.039; RA Saleque S., Kim J., Rooke H.M., Orkin S.H.; RT "Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b RT is mediated by the cofactors CoREST and LSD1."; RL Mol. Cell 27:562-572(2007). RN [27] RP INTERACTION WITH ZNF541. RX PubMed=18849567; DOI=10.1074/jbc.m805590200; RA Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H., Park Z.Y., RA Eddy E.M., Cho C.; RT "A novel germ cell-specific protein, SHIP1, forms a complex with chromatin RT remodeling activity during spermatogenesis."; RL J. Biol. Chem. 283:35283-35294(2008). RN [28] RP INTERACTION WITH ZNHIT1. RX PubMed=19501046; DOI=10.1016/j.bbrc.2009.05.139; RA Yang Z., Cao Y., Zhu X., Huang Y., Ding Y., Liu X.; RT "Znhit1 causes cell cycle arrest and down-regulates CDK6 expression."; RL Biochem. Biophys. Res. Commun. 386:146-152(2009). RN [29] RP INTERACTION WITH NR4A2. RX PubMed=19144721; DOI=10.1242/dev.029769; RA Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P., RA Smidt M.P.; RT "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation RT through release of SMRT-mediated repression."; RL Development 136:531-540(2009). RN [30] RP INTERACTION WITH NSD2. RX PubMed=19483677; DOI=10.1038/nature08086; RA Nimura K., Ura K., Shiratori H., Ikawa M., Okabe M., Schwartz R.J., RA Kaneda Y.; RT "A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf- RT Hirschhorn syndrome."; RL Nature 460:287-291(2009). RN [31] RP INTERACTION WITH SAMSN1. RX PubMed=20478393; DOI=10.1016/j.biocel.2010.05.004; RA Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A., RA Schmitz I., Beer-Hammer S.; RT "SLy2 targets the nuclear SAP30/HDAC1 complex."; RL Int. J. Biochem. Cell Biol. 42:1472-1481(2010). RN [32] RP INTERACTION WITH TSC22D3. RC STRAIN=DBA/2J; TISSUE=Myoblast; RX PubMed=20124407; DOI=10.1074/jbc.m109.070136; RA Bruscoli S., Donato V., Velardi E., Di Sante M., Migliorati G., Donato R., RA Riccardi C.; RT "Glucocorticoid-induced leucine zipper (GILZ) and long GILZ inhibit RT myogenic differentiation and mediate anti-myogenic effects of RT glucocorticoids."; RL J. Biol. Chem. 285:10385-10396(2010). RN [33] RP INTERACTION WITH ZMYND15. RX PubMed=20675388; DOI=10.1074/jbc.m110.116418; RA Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A., RA Saunders L., Verdin E., Charo I.F.; RT "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor RT essential for spermiogenesis and male fertility."; RL J. Biol. Chem. 285:31418-31426(2010). RN [34] RP INTERACTION WITH C10ORF90/FATS AND CDKN1A/P21. RX PubMed=20154723; DOI=10.1038/onc.2010.19; RA Li Z., Zhang Q., Mao J.H., Weise A., Mrasek K., Fan X., Zhang X., Liehr T., RA Lu K.H., Balmain A., Cai W.W.; RT "An HDAC1-binding domain within FATS bridges p21 turnover to radiation- RT induced tumorigenesis."; RL Oncogene 29:2659-2671(2010). RN [35] RP INTERACTION WITH DDIT3. RX PubMed=22242125; DOI=10.1371/journal.pone.0029498; RA Alter J., Bengal E.; RT "Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription RT to delay myoblast differentiation."; RL PLoS ONE 6:E29498-E29498(2011). RN [36] RP INTERACTION WITH ZNF431. RX PubMed=21177534; DOI=10.1074/jbc.m110.178780; RA He Z., Cai J., Lim J.W., Kroll K., Ma L.; RT "A novel KRAB domain-containing zinc finger transcription factor ZNF431 RT directly represses Patched1 transcription."; RL J. Biol. Chem. 286:7279-7289(2011). RN [37] RP IDENTIFICATION IN A COMPLEX WITH YY1; SIN3A AND GON4L, AND SUBCELLULAR RP LOCATION. RX PubMed=21454521; DOI=10.1074/jbc.m110.133603; RA Lu P., Hankel I.L., Hostager B.S., Swartzendruber J.A., Friedman A.D., RA Brenton J.L., Rothman P.B., Colgan J.D.; RT "The developmental regulator protein Gon4l associates with protein YY1, co- RT repressor Sin3a, and histone deacetylase 1 and mediates transcriptional RT repression."; RL J. Biol. Chem. 286:18311-18319(2011). RN [38] RP FUNCTION, INTERACTION WITH KDM5A, AND CATALYTIC ACTIVITY. RX PubMed=21960634; DOI=10.1126/science.1206022; RA DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J., RA Panda S.; RT "Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences RT the circadian clock."; RL Science 333:1881-1885(2011). RN [39] RP INTERACTION WITH INSM1. RX PubMed=24227653; DOI=10.1242/dev.097642; RA Welcker J.E., Hernandez-Miranda L.R., Paul F.E., Jia S., Ivanov A., RA Selbach M., Birchmeier C.; RT "Insm1 controls development of pituitary endocrine cells and requires a RT SNAG domain for function and for recruitment of histone-modifying RT factors."; RL Development 140:4947-4958(2013). RN [40] RP IDENTIFICATION IN A LARGE PER COMPLEX. RX PubMed=24413057; DOI=10.1038/nsmb.2746; RA Duong H.A., Weitz C.J.; RT "Temporal orchestration of repressive chromatin modifiers by circadian RT clock Period complexes."; RL Nat. Struct. Mol. Biol. 21:126-132(2014). RN [41] RP FUNCTION, AND INTERACTION WITH CIART. RX PubMed=24736997; DOI=10.1371/journal.pbio.1001839; RA Goriki A., Hatanaka F., Myung J., Kim J.K., Yoritaka T., Tanoue S., Abe T., RA Kiyonari H., Fujimoto K., Kato Y., Todo T., Matsubara A., Forger D., RA Takumi T.; RT "A novel protein, CHRONO, functions as a core component of the mammalian RT circadian clock."; RL PLoS Biol. 12:E1001839-E1001839(2014). RN [42] RP IDENTIFICATION IN THE NURD COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=27806305; DOI=10.1016/j.celrep.2016.10.022; RA Nitarska J., Smith J.G., Sherlock W.T., Hillege M.M., Nott A., RA Barshop W.D., Vashisht A.A., Wohlschlegel J.A., Mitter R., Riccio A.; RT "A Functional Switch of NuRD Chromatin Remodeling Complex Subunits RT Regulates Mouse Cortical Development."; RL Cell Rep. 17:1683-1698(2016). RN [43] RP IDENTIFICATION IN A COMPLEX WITH SIN3A; SINHCAF; SAP30; RBBP4; OGT AND RP TET1, AND INTERACTION WITH SIN3A. RX PubMed=28554894; DOI=10.15252/embj.201696307; RA Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B., Das S., RA Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T., Jammula S., RA Hokamp K., O'Connor D.P., Pasini D., Cagney G., Bracken A.P.; RT "Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells RT required for self-renewal."; RL EMBO J. 36:2216-2232(2017). RN [44] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30279482; DOI=10.1038/s41598-018-32927-9; RA Kelly R.D.W., Chandru A., Watson P.J., Song Y., Blades M., Robertson N.S., RA Jamieson A.G., Schwabe J.W.R., Cowley S.M.; RT "Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone RT acetylation and crotonylation in vivo."; RL Sci. Rep. 8:14690-14690(2018). RN [45] RP INTERACTION WITH PWWP2A AND PWWP2B. RX PubMed=30228260; DOI=10.1038/s41467-018-06235-9; RA Zhang T., Wei G., Millard C.J., Fischer R., Konietzny R., Kessler B.M., RA Schwabe J.W.R., Brockdorff N.; RT "A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to regulate RT transcription at active genes."; RL Nat. Commun. 9:3798-3798(2018). RN [46] RP INTERACTION WITH PWWP2B; BRCC2 AND ZNF516. RX PubMed=34180153; DOI=10.1002/advs.202102060; RA Yan L., Jin W., Zhao Q., Cui X., Shi T., Xu Y., Li F., Jin W., Zhang Z., RA Zhang Z., Tang Q.Q., Pan D.; RT "PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD RT Subcomplex."; RL Adv. Sci. 8:e2102060-e2102060(2021). RN [47] RP INTERACTION WITH SANBR. RX PubMed=33831416; DOI=10.1016/j.jbc.2021.100625; RA Zheng S., Matthews A.J., Rahman N., Herrick-Reynolds K., Sible E., RA Choi J.E., Wishnie A., Ng Y.K., Rhodes D., Elledge S.J., Vuong B.Q.; RT "The uncharacterized SANT and BTB domain-containing protein SANBR inhibits RT class switch recombination."; RL J. Biol. Chem. 296:100625-100625(2021). RN [48] RP IDENTIFICATION IN A COMPLEX WITH HDAC2; KCTD19; DNTTIP1 AND ZNF541. RX PubMed=34075040; DOI=10.1038/s41467-021-23378-4; RA Horisawa-Takada Y., Kodera C., Takemoto K., Sakashita A., Horisawa K., RA Maeda R., Shimada R., Usuki S., Fujimura S., Tani N., Matsuura K., RA Akiyama T., Suzuki A., Niwa H., Tachibana M., Ohba T., Katabuchi H., RA Namekawa S.H., Araki K., Ishiguro K.I.; RT "Meiosis-specific ZFP541 repressor complex promotes developmental RT progression of meiotic prophase towards completion during mouse RT spermatogenesis."; RL Nat. Commun. 12:3184-3184(2021). RN [49] RP IDENTIFICATION IN A COMPLEX WITH HDAC2; KCTD19; DNTTIP1 AND ZNF541. RX PubMed=35341968; DOI=10.1016/j.jgg.2022.03.005; RA Li Y., Meng R., Li S., Gu B., Xu X., Zhang H., Tan X., Shao T., Wang J., RA Xu D., Wang F.; RT "The ZFP541-KCTD19 complex is essential for pachytene progression by RT activating meiotic genes during mouse spermatogenesis."; RL J. Genet. Genomics 49:1029-1041(2022). 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:10615135, PubMed:15542849, PubMed:21960634, CC PubMed:30279482). Histone deacetylation gives a tag for epigenetic CC repression and plays an important role in transcriptional regulation, CC cell cycle progression and developmental events (PubMed:10615135, CC PubMed:15542849, PubMed:21960634). Histone deacetylases act via the CC formation of large multiprotein complexes (PubMed:10615135, CC PubMed:21960634). Acts as a component of the histone deacetylase NuRD CC complex which participates in the remodeling of chromatin (By CC similarity). As part of the SIN3B complex is recruited downstream of CC the constitutively active genes transcriptional start sites through CC interaction with histones and mitigates histone acetylation and RNA CC polymerase II progression within transcribed regions contributing to CC the regulation of transcription (By similarity). Also functions as a CC deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, CC STAT3 and TSHZ3 (By similarity). Deacetylates SP proteins, SP1 and SP3, CC and regulates their function (By similarity). Component of the BRG1- CC RB1-HDAC1 complex, which negatively regulates the CREST-mediated CC transcription in resting neurons (By similarity). Upon calcium CC stimulation, HDAC1 is released from the complex and CREBBP is CC recruited, which facilitates transcriptional activation (By CC similarity). Deacetylates TSHZ3 and regulates its transcriptional CC repressor activity (By similarity). Deacetylates 'Lys-310' in RELA and CC thereby inhibits the transcriptional activity of NF-kappa-B (By CC similarity). Deacetylates NR1D2 and abrogates the effect of KAT5- CC mediated relieving of NR1D2 transcription repression activity (By CC similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that CC suppresses, via histone deacetylase (HDAC) recruitment, a number of CC genes implicated in multilineage blood cell development CC (PubMed:17707228). Involved in CIART-mediated transcriptional CC repression of the circadian transcriptional activator: CLOCK-BMAL1 CC heterodimer (PubMed:15226430, PubMed:24736997). 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 (PubMed:15226430). In addition to protein deacetylase activity, also CC has protein-lysine deacylase activity: acts as a protein decrotonylase CC by mediating decrotonylation ((2E)-butenoyl) of histones CC (PubMed:30279482). {ECO:0000250|UniProtKB:Q13547, CC ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:15226430, CC ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:17707228, CC ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:24736997, CC ECO:0000269|PubMed:30279482}. 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:10615135, ECO:0000269|PubMed:21960634, CC ECO:0000305|PubMed:30279482}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; CC Evidence={ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:21960634, CC ECO:0000305|PubMed:30279482}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl- CC [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q13547}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109; CC Evidence={ECO:0000250|UniProtKB:Q13547}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate CC + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; CC Evidence={ECO:0000269|PubMed:30279482}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173; CC Evidence={ECO:0000269|PubMed:30279482}; CC -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex composed CC of HDAC1, HDAC2, RBBP4 and RBBP7, the core complex associates with CC SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex (PubMed:11909966, CC PubMed:9702189). Component of the nucleosome remodeling and deacetylase CC (NuRD) repressor complex, composed of core proteins MTA1, MTA2, MTA3, CC RBBP4, RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated CC proteins CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5 CC (PubMed:27806305). The exact stoichiometry of the NuRD complex is CC unknown, and some subunits such as MBD2 and MBD3, GATAD2A and GATAD2B, CC and CHD3, CHD4 and CHD5 define mutually exclusive NuRD complexes CC (PubMed:27806305). Component of a BHC histone deacetylase complex that CC contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and CC PHF21A/BHC80 (By similarity). The BHC complex may also contain ZMYM2, CC ZNF217, ZMYM3, GSE1 and GTF2I (By similarity). Component of a mSin3A CC corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, CC ARID4B/SAP180, HDAC1 and HDAC2 (By similarity). Found in a trimeric CC complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 CC is mediated by TSHZ3 (By similarity). Forms a complex comprising APPL1, CC RUVBL2, APPL2, CTNNB1 and HDAC2 (By similarity). Component of a CC RCOR/GFI/KDM1A/HDAC complex (PubMed:17707228). Part of a complex CC composed of TRIM28, HDAC1, HDAC2 and EHMT2 (By similarity). Part of a CC complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2 (By CC similarity). The large PER complex involved in the histone CC deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A CC (PubMed:24413057). Associates with the 9-1-1 complex; interacts with CC HUS1 (By similarity). Found in a complex with DNMT3A and HDAC7 CC (PubMed:10984530, PubMed:12616525). Found in a complex with YY1, SIN3A CC and GON4L (PubMed:21454521). 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 (By CC similarity). Found in a complex composed of at least SINHCAF, SIN3A, CC HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894). Component of the CC SIN3B complex, which includes SIN3B, HDAC1, PHF12 and MORF4L1 (By CC similarity). Interacts with GFI1; the interaction is direct CC (PubMed:17707228). Interacts directly with GFI1B (PubMed:17707228). CC Interacts with TSHZ3 (via N-terminus); the interaction is direct (By CC similarity). Interacts with APEX1; the interaction is not dependent on CC the acetylated status of APEX1 (By similarity). Interacts with BANP CC (PubMed:16166625). Interacts with BAZ2A/TIP5 (PubMed:12198165, CC PubMed:16085498). Interacts with BCL6 (By similarity). Interacts with CC BCOR (By similarity). Interacts with BHLHE40/DEC1 (By similarity). CC Interacts with BRCC3; this interaction is enhanced in the presence of CC PWWP2B (PubMed:34180153). Interacts with BRMS1 (By similarity). CC Interacts with BRMS1L (By similarity). Interacts with C10orf90/FATS CC (via its N-terminal); the interaction prevents binding of HDAC1 to CC CDKN1A/p21 and facilitates the acetylation and stabilization of CC CDKN1A/p21 (PubMed:20154723). Interacts with CBFA2T3 (PubMed:11533236). CC Interacts with CCAR2 (By similarity). Interacts with CDK2AP1 (By CC similarity). Interacts with CHD3 (By similarity). Interacts with CHD4 CC (By similarity). Interacts with CHFR (By similarity). Interacts with CC CIART (PubMed:24736997). Interacts with CDKN1A/p21 (PubMed:20154723). CC Interacts with CDK5 complexed to CDK5R1 (p25) (PubMed:20154723). CC Interacts with CRY1 (PubMed:15226430). Interacts with DAXX (By CC similarity). Interacts with DDIT3/CHOP (PubMed:22242125). Interacts CC with DDX5 (By similarity). Interacts with DHX36; this interaction CC occurs in a RNA-dependent manner (By similarity). Interacts with DNMT1 CC (PubMed:10615135). Interacts with DNTTIP1 (By similarity). Interacts CC with E4F1 (By similarity). Interacts with EP300 (By similarity). CC Interacts with ERCC6 (By similarity). Interacts with GATAD2A (By CC similarity). Interacts with HCFC1 (By similarity). Interacts with HDAC9 CC (PubMed:11022042, PubMed:15711539, PubMed:16611996). Interacts with CC HUS1 (By similarity). Interacts with INSM1 (PubMed:24227653). Interacts CC with KDM4A (By similarity). Interacts with KDM5A; this interaction CC impairs histone deacetylation (PubMed:21960634). Interacts with KDM5B CC (By similarity). Interacts with KLF1 (PubMed:15542849). Interacts with CC MBD3L2 (By similarity). Interacts with MIER1 (By similarity). Interacts CC with NFE4 (By similarity). Interacts with NR4A2/NURR1 CC (PubMed:19144721). Interacts with NR1D2 (via C-terminus) (By CC similarity). Interacts with NRIP1 (PubMed:15060175). Interacts with CC NSD2 (PubMed:19483677). Interacts with PACS2 (By similarity). Interacts CC with PHB2 (PubMed:15140878). Interacts with PPHLN1 (By similarity). CC Interacts with PRDM6 (PubMed:16537907). Interacts with PRDM16 (By CC similarity). Interacts with PWWP2A in a MTA1-dependent manner CC (PubMed:30228260). Interacts with PWWP2B (PubMed:30228260, CC PubMed:34180153). Interacts with RB1 (By similarity). Interacts with CC RERE (PubMed:14645126). Interacts with SANBR (via the BTB domain) CC (PubMed:33831416). Interacts with SAMSN1 (PubMed:20478393). Interacts CC with SAP30L (By similarity). Interacts with SETDB1 (PubMed:12398767). CC Interacts with SIN3A (By similarity). Interacts with SMAD3 (By CC similarity). Interacts with SMAD4; positively regulated by ZBTB7A (By CC similarity). Interacts with SMARCAD1 (By similarity). Interacts with CC SMARCA4/BRG1 (By similarity). Interacts with SMYD2 (PubMed:16805913). CC Interacts with SMYD4 (via MYND-type zinc finger) (By similarity). CC Interacts with SP1; the interaction deacetylates SP1 and regulates its CC transcriptional activity (By similarity). Interacts with SP3; the CC interaction deacetylates SP3 and regulates its transcriptional activity CC (By similarity). In vitro, C(18) ceramides increase this interaction CC and the subsequent SP3 deacetylation and SP3-mediated repression of the CC TERT promoter (By similarity). Interacts with SPEN/MINT (By CC similarity). Interacts with SPHK2 (By similarity). Interacts with CC SUV39H1 (PubMed:11788710). Interacts with TGIF (By similarity). CC Interacts with TGIF2 (By similarity). Interacts with TRAF6 (By CC similarity). Interacts with TRIM28; the interaction recruits HDAC1 to CC E2F1 and inhibits its acetylation (By similarity). Interacts with CC TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG CC promoter and thus inhibits MYOD1 transcriptional activity CC (PubMed:20124407). Interacts with UHRF1 (By similarity). Interacts with CC UHRF2 (By similarity). Interacts with ZBTB7A (By similarity). Interacts CC with ZMYND8 (By similarity). Interacts with ZMYND15 (PubMed:20675388). CC Interacts with ZNF431 (PubMed:21177534). Interacts with ZNF516; this CC interaction is enhanced in the presence of PWWP2B (PubMed:34180153). CC Interacts with ZNF541 (PubMed:18849567). Interacts with ZNF638 (By CC similarity). Interacts with ZNHIT1 (PubMed:19501046). Interacts with CC the non-histone region of MACROH2A1 (PubMed:16107708). Identified in a CC complex with HDAC2, KCTD19, DNTTIP1 and ZNF541 (PubMed:34075040, CC PubMed:35341968). Interacts with MSX3 (PubMed:11115394). CC {ECO:0000250|UniProtKB:Q13547, ECO:0000269|PubMed:10615135, CC ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11022042, CC ECO:0000269|PubMed:11115394, ECO:0000269|PubMed:11533236, CC ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:11909966, CC ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:12398767, CC ECO:0000269|PubMed:12616525, ECO:0000269|PubMed:14645126, CC ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15140878, CC ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:15542849, CC ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16085498, CC ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16166625, CC ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:16611996, CC ECO:0000269|PubMed:16805913, ECO:0000269|PubMed:17707228, CC ECO:0000269|PubMed:18849567, ECO:0000269|PubMed:19144721, CC ECO:0000269|PubMed:19483677, ECO:0000269|PubMed:19501046, CC ECO:0000269|PubMed:20124407, ECO:0000269|PubMed:20154723, CC ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:20675388, CC ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:21454521, CC ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:22242125, CC ECO:0000269|PubMed:24227653, ECO:0000269|PubMed:24413057, CC ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:27806305, CC ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:30228260, CC ECO:0000269|PubMed:33831416, ECO:0000269|PubMed:34075040, CC ECO:0000269|PubMed:34180153, ECO:0000269|PubMed:35341968, CC ECO:0000269|PubMed:9702189}. CC -!- INTERACTION: CC O09106; Q3TQ03: Ciart; NbExp=2; IntAct=EBI-301912, EBI-16101489; CC O09106; P27699: Crem; NbExp=3; IntAct=EBI-301912, EBI-8744406; CC O09106; P13864: Dnmt1; NbExp=3; IntAct=EBI-301912, EBI-301927; CC O09106; Q02591: Gsc; NbExp=2; IntAct=EBI-301912, EBI-7457485; CC O09106; Q6ZQ88: Kdm1a; NbExp=7; IntAct=EBI-301912, EBI-1216284; CC O09106; Q9R190: Mta2; NbExp=7; IntAct=EBI-301912, EBI-904134; CC O09106; P25799: Nfkb1; NbExp=2; IntAct=EBI-301912, EBI-643958; CC O09106; Q04207: Rela; NbExp=2; IntAct=EBI-301912, EBI-644400; CC O09106; Q8VI24: Satb2; NbExp=4; IntAct=EBI-301912, EBI-5737999; CC O09106; Q60520: Sin3a; NbExp=9; IntAct=EBI-301912, EBI-349034; CC O09106; Q3TKT4: Smarca4; NbExp=2; IntAct=EBI-301912, EBI-1210244; CC O09106; P22091: Tal1; NbExp=3; IntAct=EBI-301912, EBI-8006437; CC O09106; O88939: Zbtb7a; NbExp=3; IntAct=EBI-301912, EBI-595063; CC O09106; E9QAG8: Znf431; NbExp=3; IntAct=EBI-301912, EBI-9549639; CC O09106; O15379: HDAC3; Xeno; NbExp=2; IntAct=EBI-301912, EBI-607682; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11115394, CC ECO:0000269|PubMed:21454521}. CC -!- TISSUE SPECIFICITY: Widely expressed with higher levels in thymus and CC testis and lower levels in liver. Present in muscle (at protein level). CC {ECO:0000269|PubMed:15711539}. CC -!- INDUCTION: By interleukin-2. CC -!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic CC activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}. CC -!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity CC and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5. CC {ECO:0000250|UniProtKB:Q13547}. CC -!- PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation by CC the proteasome. {ECO:0000250|UniProtKB:Q13547}. CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1 CC subfamily. {ECO:0000305}. 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; X98207; CAA66870.1; -; mRNA. DR EMBL; U80780; AAB68398.1; -; mRNA. DR CCDS; CCDS18696.1; -. DR RefSeq; NP_032254.1; NM_008228.2. DR AlphaFoldDB; O09106; -. DR SMR; O09106; -. DR BioGRID; 241423; 104. DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant. DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex. DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex. DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex. DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex. DR CORUM; O09106; -. DR DIP; DIP-31499N; -. DR IntAct; O09106; 53. DR MINT; O09106; -. DR STRING; 10090.ENSMUSP00000099657; -. DR BindingDB; O09106; -. DR ChEMBL; CHEMBL4001; -. DR DrugCentral; O09106; -. DR GlyGen; O09106; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O09106; -. DR PhosphoSitePlus; O09106; -. DR SwissPalm; O09106; -. DR EPD; O09106; -. DR jPOST; O09106; -. DR PaxDb; 10090-ENSMUSP00000099657; -. DR PeptideAtlas; O09106; -. DR ProteomicsDB; 269727; -. DR Pumba; O09106; -. DR Antibodypedia; 3760; 1825 antibodies from 51 providers. DR DNASU; 433759; -. DR Ensembl; ENSMUST00000102597.5; ENSMUSP00000099657.5; ENSMUSG00000028800.16. DR GeneID; 433759; -. DR KEGG; mmu:433759; -. DR UCSC; uc008uxg.1; mouse. DR AGR; MGI:108086; -. DR CTD; 3065; -. DR MGI; MGI:108086; Hdac1. DR VEuPathDB; HostDB:ENSMUSG00000028800; -. DR eggNOG; KOG1342; Eukaryota. DR GeneTree; ENSGT00940000154301; -. DR HOGENOM; CLU_007727_7_4_1; -. DR InParanoid; O09106; -. DR OMA; GKIMEWY; -. DR OrthoDB; 1327607at2759; -. DR PhylomeDB; O09106; -. DR TreeFam; TF106171; -. DR BRENDA; 3.5.1.98; 3474. DR Reactome; R-MMU-1538133; G0 and Early G1. DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR Reactome; R-MMU-3214815; HDACs deacetylate histones. DR Reactome; R-MMU-350054; Notch-HLH transcription pathway. DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation. DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription. DR Reactome; R-MMU-9022692; Regulation of MECP2 expression and activity. DR Reactome; R-MMU-9701898; STAT3 nuclear events downstream of ALK signaling. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR SABIO-RK; O09106; -. DR BioGRID-ORCS; 433759; 13 hits in 83 CRISPR screens. DR ChiTaRS; Hdac1; mouse. DR PRO; PR:O09106; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; O09106; Protein. DR Bgee; ENSMUSG00000028800; Expressed in embryonic post-anal tail and 124 other cell types or tissues. DR ExpressionAtlas; O09106; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0000792; C:heterochromatin; IDA:MGI. DR GO; GO:0000118; C:histone deacetylase complex; IPI:MGI. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0016581; C:NuRD complex; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0070822; C:Sin3-type complex; IEA:Ensembl. DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB. DR GO; GO:0017053; C:transcription repressor complex; IPI:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI. DR GO; GO:0019213; F:deacetylase activity; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI. DR GO; GO:0160009; F:histone decrotonylase activity; IDA:UniProtKB. DR GO; GO:0035851; F:Krueppel-associated box domain binding; IPI:UniProtKB. DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI. DR GO; GO:0002039; F:p53 binding; ISO:MGI. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI. DR GO; GO:0033558; F:protein lysine deacetylase activity; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI. DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI. DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI. DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB. DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; ISO:MGI. DR GO; GO:0042733; P:embryonic digit morphogenesis; IGI:BHF-UCL. DR GO; GO:0007492; P:endoderm development; IDA:MGI. DR GO; GO:0009913; P:epidermal cell differentiation; IGI:BHF-UCL. DR GO; GO:0061029; P:eyelid development in camera-type eye; IGI:BHF-UCL. DR GO; GO:0061198; P:fungiform papilla formation; IGI:BHF-UCL. DR GO; GO:0060789; P:hair follicle placode formation; IGI:BHF-UCL. DR GO; GO:0021766; P:hippocampus development; IGI:MGI. DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISO:MGI. DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:BHF-UCL. DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IGI:MGI. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI. DR GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IGI:MGI. DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; NAS:ComplexPortal. DR GO; GO:0030182; P:neuron differentiation; IGI:MGI. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:BHF-UCL. DR GO; GO:0048709; P:oligodendrocyte differentiation; IGI:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IGI:MGI. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0042659; P:regulation of cell fate specification; NAS:ComplexPortal. DR GO; GO:2000736; P:regulation of stem cell differentiation; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI. DR CDD; cd10010; HDAC1; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR003084; His_deacetylse_1. DR InterPro; IPR023801; His_deacetylse_dom. DR InterPro; IPR037138; His_deacetylse_dom_sf. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR PANTHER; PTHR10625:SF21; HISTONE DEACETYLASE 1; 1. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037913; His_deacetylse_1; 1. DR PRINTS; PR01270; HDASUPER. DR PRINTS; PR01271; HISDACETLASE. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. DR Genevisible; O09106; MM. PE 1: Evidence at protein level; KW Acetylation; Biological rhythms; Chromatin regulator; Hydrolase; KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; S-nitrosylation; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..482 FT /note="Histone deacetylase 1" FT /id="PRO_0000114688" FT REGION 9..321 FT /note="Histone deacetylase" FT REGION 390..482 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 400..482 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 141 FT /evidence="ECO:0000250|UniProtKB:Q13547" FT MOD_RES 74 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT MOD_RES 220 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT MOD_RES 261 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P70288" FT MOD_RES 273 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P70288" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92769" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT MOD_RES 423 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT MOD_RES 432 FT /note="N6-methylated lysine; by EHMT2" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT CROSSLNK 74 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q92769" FT CROSSLNK 438 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT CROSSLNK 444 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT CROSSLNK 444 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT CROSSLNK 456 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q92769" FT CROSSLNK 457 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT CROSSLNK 473 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q92769" FT CROSSLNK 476 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT CROSSLNK 476 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q13547" FT CROSSLNK 480 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q13547" SQ SEQUENCE 482 AA; 55075 MW; 7F64D3C17F5E4844 CRC64; MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED PDKRISICSS DKRIACEEEF SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK LA //