HDAC1_MOUSE
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 03-AUG-2022, entry version 220.
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 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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).
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). Also functions as deacetylase for non-histone
CC targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3 (By similarity).
CC Deacetylates SP proteins, SP1 and SP3, and regulates their function (By
CC similarity). Component of the BRG1-RB1-HDAC1 complex, which negatively
CC regulates the CREST-mediated transcription in resting neurons (By
CC similarity). Upon calcium stimulation, HDAC1 is released from the
CC complex and CREBBP is recruited, which facilitates transcriptional
CC activation (By similarity). Deacetylates TSHZ3 and regulates its
CC transcriptional repressor activity (By similarity). Deacetylates 'Lys-
CC 310' in RELA and thereby inhibits the transcriptional activity of NF-
CC kappa-B (By similarity). Deacetylates NR1D2 and abrogates the effect of
CC KAT5-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-
CC ARNTL/BMAL1 heterodimer (PubMed:15226430, PubMed:24736997). Required
CC for the transcriptional repression of circadian target genes, such as
CC PER1, mediated by the large PER complex or CRY1 through histone
CC deacetylation (PubMed:15226430). In addition to protein deacetylase
CC activity, also has protein-lysine deacylase activity: acts as a protein
CC decrotonylase 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 (By similarity). The core complex
CC associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the
CC nucleosome remodeling and histone deacetylation (NuRD) complex, or with
CC SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex (PubMed:11909966,
CC PubMed:9702189). 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). Interacts with TSHZ3 (via N-
CC terminus); the interaction is direct (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). Interacts with the non-histone
CC region of MACROH2A1 (PubMed:16107708). Interacts with TRIM28; the
CC interaction recruits HDAC1 to E2F1 and inhibits its acetylation (By
CC similarity). Interacts with SP1; the interaction deacetylates SP1 and
CC regulates its transcriptional activity (By similarity). Interacts with
CC SP3; the interaction deacetylates SP3 and regulates its transcriptional
CC activity (By similarity). In vitro, C(18) ceramides increase this
CC interaction and the subsequent SP3 deacetylation and SP3-mediated
CC repression of the TERT promoter (By similarity). Interacts with APEX1;
CC the interaction is not dependent on the acetylated status of APEX1 (By
CC similarity). Interacts with C10orf90/FATS (via its N-terminal); the
CC interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the
CC acetylation and stabilization of CDKN1A/p21 (PubMed:20154723).
CC Interacts with CDKN1A/p21 (PubMed:20154723). Interacts with CDK5
CC complexed to CDK5R1 (p25) (PubMed:20154723). Interacts directly with
CC GFI1 and GFI1B (PubMed:17707228). Interacts with NR1D2 (via C-terminus)
CC (By similarity). Interacts with TSC22D3 isoform 1; this interaction
CC affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1
CC transcriptional activity (PubMed:20124407). Interacts with BAZ2A/TIP5,
CC BANP, BCL6, BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART,
CC CRY1, DAXX, DDIT3/CHOP, DDX5, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4,
CC NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, DNMT1, NRIP1, PCAF, PHB2,
CC PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCAD1,
CC SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2,
CC ZMYND15, ZNF431 and ZNF541 (PubMed:14645126, PubMed:11022042,
CC PubMed:12198165, PubMed:12398767, PubMed:11533236, PubMed:15711539,
CC PubMed:16611996, PubMed:11788710, PubMed:10615135, PubMed:16805913,
CC PubMed:24736997, PubMed:19144721, PubMed:18849567, PubMed:24227653,
CC PubMed:20675388, PubMed:20478393, PubMed:22242125, PubMed:15060175,
CC PubMed:16166625, PubMed:16537907, PubMed:16085498, PubMed:15140878,
CC PubMed:15542849, PubMed:15226430, PubMed:21177534). Interacts with
CC KDM5A; this interaction impairs histone deacetylation
CC (PubMed:21960634). Interacts with DNTTIP1 (By similarity). Identified
CC in a histone deacetylase complex that contains DNTTIP1, HDAC1 and
CC MIDEAS; this complex assembles into a tetramer that contains four
CC copies of each protein chain (By similarity). Interacts with CCAR2 (By
CC similarity). Interacts with PPHLN1 (By similarity). Found in a complex
CC with YY1, SIN3A and GON4L (PubMed:21454521). Interacts with CHD4 (By
CC similarity). Found in a complex composed of at least SINHCAF, SIN3A,
CC HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894). Interacts with
CC SIN3A (PubMed:28554894). Interacts with DHX36; this interaction occurs
CC in a RNA-dependent manner (By similarity). Interacts with ZBTB7A (By
CC similarity). Interacts with SMAD4; positively regulated by ZBTB7A (By
CC similarity). Interacts with PACS2 (By similarity). Forms a complex
CC comprising APPL1, RUVBL2, APPL2, CTNNB1 and HDAC2 (By similarity).
CC Interacts with ZNF638 (By similarity). Interacts with SPHK2. Interacts
CC with ERCC6 (By similarity). Interacts with NSD2 (PubMed:19483677).
CC Interacts with SMYD4 (via MYND-type zinc finger) (By similarity).
CC Interacts with isoform 1 and isoform 3 of PWWP2A in a MTA1-dependent
CC manner (PubMed:30228260). Interacts with PWWP2B (PubMed:30228260,
CC PubMed:34180153). Interacts with ZNF516 and BRCC3; these interactions
CC are enhanced in the presence of PWWP2B (PubMed:34180153). Interacts
CC with SANBR (via the BTB domain) (PubMed:33831416).
CC {ECO:0000250|UniProtKB:Q13547, ECO:0000269|PubMed:10615135,
CC ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11022042,
CC ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11788710,
CC ECO:0000269|PubMed:11909966, ECO:0000269|PubMed:12198165,
CC ECO:0000269|PubMed:12398767, ECO:0000269|PubMed:12616525,
CC ECO:0000269|PubMed:14645126, ECO:0000269|PubMed:15060175,
CC ECO:0000269|PubMed:15140878, ECO:0000269|PubMed:15226430,
CC ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:15711539,
CC ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:16107708,
CC ECO:0000269|PubMed:16166625, ECO:0000269|PubMed:16537907,
CC ECO:0000269|PubMed:16611996, ECO:0000269|PubMed:16805913,
CC ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:18849567,
CC ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:19483677,
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:28554894,
CC ECO:0000269|PubMed:30228260, ECO:0000269|PubMed:33831416,
CC ECO:0000269|PubMed:34180153, 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 -!- SUBCELLULAR LOCATION: Nucleus {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 ---------------------------------------------------------------------------
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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; 50.
DR MINT; O09106; -.
DR STRING; 10090.ENSMUSP00000099657; -.
DR BindingDB; O09106; -.
DR ChEMBL; CHEMBL4001; -.
DR DrugCentral; O09106; -.
DR iPTMnet; O09106; -.
DR PhosphoSitePlus; O09106; -.
DR SwissPalm; O09106; -.
DR EPD; O09106; -.
DR jPOST; O09106; -.
DR PaxDb; O09106; -.
DR PeptideAtlas; O09106; -.
DR PRIDE; O09106; -.
DR ProteomicsDB; 269727; -.
DR Antibodypedia; 3760; 1620 antibodies from 51 providers.
DR DNASU; 433759; -.
DR Ensembl; ENSMUST00000102597; ENSMUSP00000099657; ENSMUSG00000028800.
DR GeneID; 433759; -.
DR KEGG; mmu:433759; -.
DR UCSC; uc008uxg.1; mouse.
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; WAIHTAT; -.
DR OrthoDB; 732770at2759; -.
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-9018519; Estrogen-dependent gene expression.
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 77 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 121 other tissues.
DR ExpressionAtlas; O09106; baseline and differential.
DR Genevisible; O09106; MM.
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:0043005; C:neuron projection; ISO: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:0016580; C:Sin3 complex; ISO:MGI.
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; IDA:UniProtKB.
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:0047485; F:protein N-terminus binding; 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 assembly; 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:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0070932; P:histone H3 deacetylation; IDA:UniProtKB.
DR GO; GO:0070933; P:histone H4 deacetylation; IDA:UniProtKB.
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:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IGI: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; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0030182; P:neuron differentiation; 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:0048714; P:positive regulation of oligodendrocyte differentiation; IGI:MGI.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006476; P:protein deacetylation; ISO:MGI.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:MGI.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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 InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW 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
