GenomeNet

Database: UniProt/SWISS-PROT
Entry: HDAC2_HUMAN
LinkDB: HDAC2_HUMAN
Original site: HDAC2_HUMAN 
ID   HDAC2_HUMAN             Reviewed;         488 AA.
AC   Q92769; B3KRS5; B4DL58; E1P561; Q5SRI8; Q5SZ86; Q8NEH4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   05-DEC-2018, entry version 209.
DE   RecName: Full=Histone deacetylase 2;
DE            Short=HD2;
DE            EC=3.5.1.98;
GN   Name=HDAC2;
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] (ISOFORM 1), AND VARIANT CYS-230.
RC   TISSUE=Mammary gland;
RX   PubMed=8917507; DOI=10.1073/pnas.93.23.12845;
RA   Yang W.-M., Inouye C.J., Zeng Y., Bearss D., Seto E.;
RT   "Transcriptional repression by YY1 is mediated by interaction with a
RT   mammalian homolog of the yeast global regulator RPD3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   HIS-315.
RC   TISSUE=Testis;
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   [6]
RP   INTERACTION WITH ATR, AND IDENTIFICATION IN A COMPLEX CONTAINING ATR
RP   AND CHD4.
RX   PubMed=10545197; DOI=10.1021/bi991614n;
RA   Schmidt D.R., Schreiber S.L.;
RT   "Molecular association between ATR and two components of the
RT   nucleosome remodeling and deacetylating complex, HDAC2 and CHD4.";
RL   Biochemistry 38:14711-14717(1999).
RN   [7]
RP   INTERACTION WITH SNW1.
RX   PubMed=10644367; DOI=10.1128/JVI.74.4.1939-1947.2000;
RA   Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.;
RT   "A role for SKIP in EBNA2 activation of CBF1-repressed promoters.";
RL   J. Virol. 74:1939-1947(2000).
RN   [8]
RP   INTERACTION WITH DNMT1 AND DMAP1.
RX   PubMed=10888872; DOI=10.1038/77023;
RA   Rountree M.R., Bachman K.E., Baylin S.B.;
RT   "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
RT   replication foci.";
RL   Nat. Genet. 25:269-277(2000).
RN   [9]
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   [10]
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   [11]
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   [12]
RP   INTERACTION WITH HDAC10.
RX   PubMed=11739383; DOI=10.1074/jbc.M108055200;
RA   Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R.,
RA   Trogani N., Widmer R., Atadja P., Cohen D.;
RT   "Isolation and characterization of a novel class II histone
RT   deacetylase, HDAC10.";
RL   J. Biol. Chem. 277:6656-6666(2002).
RN   [13]
RP   INTERACTION WITH SP3.
RX   PubMed=12176973; DOI=10.1074/jbc.C200378200;
RA   Sun J.M., Chen H.Y., Moniwa M., Litchfield D.W., Seto E., Davie J.R.;
RT   "The transcriptional repressor Sp3 is associated with CK2-
RT   phosphorylated histone deacetylase 2.";
RL   J. Biol. Chem. 277:35783-35786(2002).
RN   [14]
RP   INTERACTION WITH DAXX AND DEK.
RX   PubMed=12140263;
RA   Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R.,
RA   Grosveld G.;
RT   "Daxx and histone deacetylase II associate with chromatin through an
RT   interaction with core histones and the chromatin-associated protein
RT   Dek.";
RL   J. Cell Sci. 115:3319-3330(2002).
RN   [15]
RP   INTERACTION WITH BCL6.
RX   PubMed=12402037; DOI=10.1038/ng1018;
RA   Bereshchenko O.R., Gu W., Dalla-Favera R.;
RT   "Acetylation inactivates the transcriptional repressor BCL6.";
RL   Nat. Genet. 32:606-613(2002).
RN   [16]
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   [17]
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   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE BHC
RP   COMPLEX WITH GSE1; GTF2I; HDAC1; HMG20B; KDM1A; PHF21A; RCOR1; ZMYM2;
RP   ZMYM3 AND ZNF217.
RX   PubMed=12493763; DOI=10.1074/jbc.M208992200;
RA   Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT   "A candidate X-linked mental retardation gene is a component of a new
RT   family of histone deacetylase-containing complexes.";
RL   J. Biol. Chem. 278:7234-7239(2003).
RN   [19]
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   [20]
RP   INTERACTION WITH PELP1.
RX   PubMed=15456770; DOI=10.1074/jbc.M406831200;
RA   Choi Y.B., Ko J.K., Shin J.;
RT   "The transcriptional corepressor, PELP1, recruits HDAC2 and masks
RT   histones using two separate domains.";
RL   J. Biol. Chem. 279:50930-50941(2004).
RN   [21]
RP   INTERACTION WITH NRIP1.
RX   PubMed=15060175; DOI=10.1093/nar/gkh524;
RA   Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P.,
RA   Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
RT   "Multiple domains of the receptor-interacting protein 140 contribute
RT   to transcription inhibition.";
RL   Nucleic Acids Res. 32:1957-1966(2004).
RN   [22]
RP   INTERACTION WITH JMJD2A.
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   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, 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   [24]
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   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, 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   [26]
RP   IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC1.
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   [27]
RP   INTERACTION WITH BCL6.
RX   PubMed=18212045; DOI=10.1128/MCB.01400-07;
RA   Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A.,
RA   Ye B.H.;
RT   "CtBP is an essential corepressor for BCL6 autoregulation.";
RL   Mol. Cell. Biol. 28:2175-2186(2008).
RN   [28]
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   [29]
RP   INTERACTION WITH PIMREG.
RX   PubMed=18757745; DOI=10.1073/pnas.0709227105;
RA   Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III,
RA   Fang G.;
RT   "RCS1, a substrate of APC/C, controls the metaphase to anaphase
RT   transition.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008).
RN   [30]
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   [31]
RP   FUNCTION, AND INTERACTION WITH 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   [32]
RP   INTERACTION WITH CHFR.
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   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-422, 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   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, 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   [35]
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   [36]
RP   FUNCTION, AND INTERACTION WITH MTA1.
RX   PubMed=21965678; DOI=10.1074/jbc.M111.267237;
RA   Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT   "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor
RT   antigen 1 (MTA1) synergistically regulate its transcriptional
RT   repressor function.";
RL   J. Biol. Chem. 286:43793-43808(2011).
RN   [37]
RP   INTERACTION WITH BEND3.
RX   PubMed=21914818; DOI=10.1242/jcs.086603;
RA   Sathyan K.M., Shen Z., Tripathi V., Prasanth K.V., Prasanth S.G.;
RT   "A BEN-domain-containing protein associates with heterochromatin and
RT   represses transcription.";
RL   J. Cell Sci. 124:3149-3163(2011).
RN   [38]
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   [39]
RP   INTERACTION WITH DNTTIP1 AND ZNF541.
RX   PubMed=21573134; DOI=10.1371/journal.pgen.1002065;
RA   Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L.,
RA   Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.;
RT   "Nuclear cGMP-dependent kinase regulates gene expression via activity-
RT   dependent recruitment of a conserved histone deacetylase complex.";
RL   PLoS Genet. 7:E1002065-E1002065(2011).
RN   [40]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, 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   [41]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-407; SER-422
RP   AND SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [42]
RP   INTERACTION WITH NACC2.
RX   PubMed=22926524; DOI=10.1038/onc.2012.386;
RA   Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L.,
RA   Yao Z., Shang Y.;
RT   "RBB, a novel transcription repressor, represses the transcription of
RT   HDM2 oncogene.";
RL   Oncogene 32:3711-3721(2013).
RN   [43]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [44]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-462, AND IDENTIFICATION BY
RP   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   [45]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MTA1.
RX   PubMed=24970816;
RA   Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C.,
RA   Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.;
RT   "The subcellular distribution and function of MTA1 in cancer
RT   differentiation.";
RL   Oncotarget 5:5153-5164(2014).
RN   [46]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [47]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-462 AND LYS-481, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.O114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [48]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-452; LYS-458;
RP   LYS-462; LYS-478 AND LYS-481, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-374 IN COMPLEX WITH
RP   SUBSTITUTED N-(2-AMINOPHENYL)BENZAMIDE INHIBITORS.
RX   PubMed=20392638; DOI=10.1016/j.bmcl.2010.03.091;
RA   Bressi J.C., Jennings A.J., Skene R., Wu Y., Melkus R., De Jong R.,
RA   O'Connell S., Grimshaw C.E., Navre M., Gangloff A.R.;
RT   "Exploration of the HDAC2 foot pocket: Synthesis and SAR of
RT   substituted N-(2-aminophenyl)benzamides.";
RL   Bioorg. Med. Chem. Lett. 20:3142-3145(2010).
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. Forms
CC       transcriptional repressor complexes by associating with MAD, SIN3,
CC       YY1 and N-COR. Interacts in the late S-phase of DNA-replication
CC       with DNMT1 in the other transcriptional repressor complex composed
CC       of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its
CC       transcriptional repressor 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. May be involved in the
CC       transcriptional repression of circadian target genes, such as
CC       PER1, mediated by CRY1 through histone deacetylation. Involved in
CC       MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.
CC       {ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21965678}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of an N(6)-acetyl-lysine residue of a histone
CC         to yield a deacetylated histone.; EC=3.5.1.98;
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, MBD3, MTA1L1, CHD3 and CHD4 to form the
CC       nucleosome remodeling and histone deacetylation (NuRD) complex, or
CC       with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex.
CC       Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly
CC       with GFI1 and GFI1B. Interacts with SNW1, HDAC7, PRDM6, SAP30,
CC       SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone
CC       region). Component of a BHC histone deacetylase complex that
CC       contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC
CC       complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC       Part of a complex containing the core histones H2A, H2B, H3 and
CC       H4, DEK and unphosphorylated DAXX. Part of a complex containing
CC       ATR and CHD4. Forms a heterologous complex at least with YY1.
CC       Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1,
CC       KDM4A and PELP1. Component of a mSin3A corepressor complex that
CC       contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts
CC       with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with
CC       SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with
CC       APEX1; the interaction is not dependent on the acetylated status
CC       of APEX1. Part of a complex composed of TRIM28, HDAC1, HDAC2 and
CC       EHMT2. Interacts with PIMREG. Interacts with BCL6 (non-acetylated
CC       form). Part of a complex containing at least CDYL, MIER1, MIER2,
CC       HDAC1 and HDAC2. Interacts with CRY1, INSM1 and ZNF431. Interacts
CC       with NACC2. Interacts with MTA1, with a preference for sumoylated
CC       MTA1. Interacts with SIX3 (By similarity). Interacts with BEND3.
CC       Component of a histone deacetylase complex containing DNTTIP1,
CC       ZNF541, HDAC1 and HDAC2 (PubMed:21573134).
CC       {ECO:0000250|UniProtKB:P70288, ECO:0000269|PubMed:10545197,
CC       ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:10888872,
CC       ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:11533236,
CC       ECO:0000269|PubMed:11739383, ECO:0000269|PubMed:12140263,
CC       ECO:0000269|PubMed:12176973, ECO:0000269|PubMed:12402037,
CC       ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:12670868,
CC       ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:14633989,
CC       ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15456770,
CC       ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16820529,
CC       ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:18757745,
CC       ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:19182791,
CC       ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:20392638,
CC       ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:21573134,
CC       ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:21965678,
CC       ECO:0000269|PubMed:22926524, ECO:0000269|PubMed:24970816}.
CC   -!- INTERACTION:
CC       Q9C0K0:BCL11B; NbExp=3; IntAct=EBI-301821, EBI-6597578;
CC       Q9HCU9:BRMS1; NbExp=4; IntAct=EBI-301821, EBI-714781;
CC       Q9UER7:DAXX; NbExp=2; IntAct=EBI-301821, EBI-77321;
CC       P51610:HCFC1; NbExp=2; IntAct=EBI-301821, EBI-396176;
CC       Q13547:HDAC1; NbExp=12; IntAct=EBI-301821, EBI-301834;
CC       Q2HR82:K8 (xeno); NbExp=7; IntAct=EBI-301821, EBI-9006943;
CC       Q9UIS9:MBD1; NbExp=2; IntAct=EBI-301821, EBI-867196;
CC       Q13330:MTA1; NbExp=5; IntAct=EBI-301821, EBI-714236;
CC       P01106:MYC; NbExp=2; IntAct=EBI-301821, EBI-447544;
CC       P06748:NPM1; NbExp=2; IntAct=EBI-301821, EBI-78579;
CC       P48382:RFX5; NbExp=4; IntAct=EBI-301821, EBI-923266;
CC       Q96ST3:SIN3A; NbExp=5; IntAct=EBI-301821, EBI-347218;
CC       O95863:SNAI1; NbExp=2; IntAct=EBI-301821, EBI-1045459;
CC       Q9HD15:SRA1; NbExp=2; IntAct=EBI-301821, EBI-727136;
CC       O43463:SUV39H1; NbExp=3; IntAct=EBI-301821, EBI-349968;
CC       Q17R98:ZNF827; NbExp=2; IntAct=EBI-301821, EBI-5564776;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24970816}.
CC       Cytoplasm {ECO:0000269|PubMed:24970816}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q92769-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92769-3; Sequence=VSP_056175;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed; lower levels in brain and
CC       lung.
CC   -!- PTM: S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-
CC       262 and Cys-274 does not affect the enzyme activity but abolishes
CC       chromatin-binding, leading to increases acetylation of histones
CC       and activate genes that are associated with neuronal development.
CC       In embryonic cortical neurons, S-Nitrosylation regulates dendritic
CC       growth and branching. {ECO:0000250|UniProtKB:P70288}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31055.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAG59420.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/HDAC2ID40803ch6q22.html";
DR   EMBL; U31814; AAC50814.1; -; mRNA.
DR   EMBL; AK092156; BAG52487.1; -; mRNA.
DR   EMBL; AK296856; BAG59420.1; ALT_INIT; mRNA.
DR   EMBL; AL590398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL671967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FO393415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48252.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48253.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48254.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48255.1; -; Genomic_DNA.
DR   EMBL; BC031055; AAH31055.2; ALT_INIT; mRNA.
DR   CCDS; CCDS43493.2; -. [Q92769-1]
DR   RefSeq; NP_001518.3; NM_001527.3. [Q92769-1]
DR   RefSeq; XP_011534090.1; XM_011535788.1.
DR   RefSeq; XP_016866288.1; XM_017010799.1. [Q92769-3]
DR   UniGene; Hs.3352; -.
DR   PDB; 3MAX; X-ray; 2.05 A; A/B/C=9-374.
DR   PDB; 4LXZ; X-ray; 1.85 A; A/B/C=8-376.
DR   PDB; 4LY1; X-ray; 1.57 A; A/B/C=8-376.
DR   PDB; 5IWG; X-ray; 1.66 A; A/B/C=8-375.
DR   PDB; 5IX0; X-ray; 1.72 A; A/B/C=7-375.
DR   PDB; 6G3O; X-ray; 2.27 A; A/B/C=7-376.
DR   PDBsum; 3MAX; -.
DR   PDBsum; 4LXZ; -.
DR   PDBsum; 4LY1; -.
DR   PDBsum; 5IWG; -.
DR   PDBsum; 5IX0; -.
DR   PDBsum; 6G3O; -.
DR   ProteinModelPortal; Q92769; -.
DR   SMR; Q92769; -.
DR   BioGrid; 109316; 346.
DR   ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR   ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR   ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR   ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR   ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR   CORUM; Q92769; -.
DR   DIP; DIP-24220N; -.
DR   IntAct; Q92769; 171.
DR   MINT; Q92769; -.
DR   STRING; 9606.ENSP00000430432; -.
DR   BindingDB; Q92769; -.
DR   ChEMBL; CHEMBL1937; -.
DR   DrugBank; DB01223; Aminophylline.
DR   DrugBank; DB05015; Belinostat.
DR   DrugBank; DB00227; Lovastatin.
DR   DrugBank; DB05651; MGCD-0103.
DR   DrugBank; DB01303; Oxtriphylline.
DR   DrugBank; DB06603; Panobinostat.
DR   DrugBank; DB06176; Romidepsin.
DR   DrugBank; DB05223; SB939.
DR   DrugBank; DB00277; Theophylline.
DR   DrugBank; DB00313; Valproic Acid.
DR   DrugBank; DB02546; Vorinostat.
DR   GuidetoPHARMACOLOGY; 2616; -.
DR   iPTMnet; Q92769; -.
DR   PhosphoSitePlus; Q92769; -.
DR   BioMuta; HDAC2; -.
DR   DMDM; 68068066; -.
DR   EPD; Q92769; -.
DR   MaxQB; Q92769; -.
DR   PaxDb; Q92769; -.
DR   PeptideAtlas; Q92769; -.
DR   PRIDE; Q92769; -.
DR   ProteomicsDB; 75454; -.
DR   DNASU; 3066; -.
DR   Ensembl; ENST00000368632; ENSP00000357621; ENSG00000196591. [Q92769-3]
DR   Ensembl; ENST00000519065; ENSP00000430432; ENSG00000196591. [Q92769-1]
DR   Ensembl; ENST00000519108; ENSP00000430008; ENSG00000196591. [Q92769-3]
DR   GeneID; 3066; -.
DR   KEGG; hsa:3066; -.
DR   UCSC; uc003pwc.3; human. [Q92769-1]
DR   CTD; 3066; -.
DR   DisGeNET; 3066; -.
DR   EuPathDB; HostDB:ENSG00000196591.11; -.
DR   GeneCards; HDAC2; -.
DR   HGNC; HGNC:4853; HDAC2.
DR   HPA; CAB005054; -.
DR   HPA; HPA011727; -.
DR   MIM; 605164; gene.
DR   neXtProt; NX_Q92769; -.
DR   OpenTargets; ENSG00000196591; -.
DR   PharmGKB; PA29227; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00940000155725; -.
DR   HOGENOM; HOG000225180; -.
DR   HOVERGEN; HBG057112; -.
DR   InParanoid; Q92769; -.
DR   KO; K06067; -.
DR   OMA; CDIAINY; -.
DR   OrthoDB; EOG091G067J; -.
DR   PhylomeDB; Q92769; -.
DR   TreeFam; TF106171; -.
DR   BRENDA; 3.5.1.98; 2681.
DR   Reactome; R-HSA-193670; p75NTR negatively regulates cell cycle via SC1.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain 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-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR   Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR   Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR   Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR   SABIO-RK; Q92769; -.
DR   SIGNOR; Q92769; -.
DR   ChiTaRS; HDAC2; human.
DR   EvolutionaryTrace; Q92769; -.
DR   GeneWiki; Histone_deacetylase_2; -.
DR   GenomeRNAi; 3066; -.
DR   PRO; PR:Q92769; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000196591; Expressed in 232 organ(s), highest expression level in cerebral cortex.
DR   CleanEx; HS_HDAC2; -.
DR   ExpressionAtlas; Q92769; baseline and differential.
DR   Genevisible; Q92769; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR   GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR   GO; GO:0000790; C:nuclear chromatin; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
DR   GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
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:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR   GO; GO:0033558; F:protein deacetylase activity; IMP:BHF-UCL.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; HDA:UniProtKB.
DR   GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
DR   GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
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:0016358; P:dendrite development; 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:0060789; P:hair follicle placode formation; ISS:BHF-UCL.
DR   GO; GO:0016575; P:histone deacetylation; IMP:BHF-UCL.
DR   GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR   GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR   GO; GO:0006344; P:maintenance of chromatin silencing; IMP:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
DR   GO; GO:0061000; P:negative regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IC:BHF-UCL.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:BHF-UCL.
DR   GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
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:0032967; P:positive regulation of collagen biosynthetic process; IC:BHF-UCL.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:Ensembl.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045862; P:positive regulation of proteolysis; 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 by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:BHF-UCL.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
DR   GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR   GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
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   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.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW   Chromatin regulator; Complete proteome; Cytoplasm; Hydrolase;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repressor; S-nitrosylation; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    488       Histone deacetylase 2.
FT                                /FTId=PRO_0000114693.
FT   REGION        9    322       Histone deacetylase.
FT   COMPBIAS    300    303       Poly-Gly.
FT   ACT_SITE    142    142       {ECO:0000250}.
FT   MOD_RES      75     75       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   MOD_RES     221    221       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   MOD_RES     262    262       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P70288}.
FT   MOD_RES     274    274       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P70288}.
FT   MOD_RES     394    394       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     407    407       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     422    422       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     424    424       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   CROSSLNK     75     75       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    439    439       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q13547}.
FT   CROSSLNK    452    452       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    458    458       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    462    462       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    478    478       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    481    481       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1     30       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056175.
FT   VARIANT     230    230       R -> C (in dbSNP:rs1042903).
FT                                {ECO:0000269|PubMed:8917507}.
FT                                /FTId=VAR_025311.
FT   VARIANT     315    315       Y -> H (in dbSNP:rs17852888).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_025312.
FT   CONFLICT     93     94       QR -> HI (in Ref. 1; AAC50814).
FT                                {ECO:0000305}.
FT   CONFLICT    103    103       V -> A (in Ref. 1; AAC50814).
FT                                {ECO:0000305}.
FT   CONFLICT    146    146       S -> Y (in Ref. 1; AAC50814).
FT                                {ECO:0000305}.
FT   CONFLICT    248    248       K -> M (in Ref. 2; BAG59420).
FT                                {ECO:0000305}.
FT   CONFLICT    281    281       G -> D (in Ref. 2; BAG59420).
FT                                {ECO:0000305}.
FT   STRAND       12     15       {ECO:0000244|PDB:4LY1}.
FT   HELIX        20     22       {ECO:0000244|PDB:4LY1}.
FT   HELIX        34     45       {ECO:0000244|PDB:4LY1}.
FT   HELIX        48     51       {ECO:0000244|PDB:4LY1}.
FT   STRAND       52     55       {ECO:0000244|PDB:4LY1}.
FT   HELIX        62     65       {ECO:0000244|PDB:4LY1}.
FT   TURN         66     68       {ECO:0000244|PDB:4LY1}.
FT   HELIX        71     79       {ECO:0000244|PDB:4LY1}.
FT   TURN         82     84       {ECO:0000244|PDB:4LY1}.
FT   HELIX        85     88       {ECO:0000244|PDB:4LY1}.
FT   HELIX        89     95       {ECO:0000244|PDB:4LY1}.
FT   STRAND       98    101       {ECO:0000244|PDB:4LY1}.
FT   HELIX       107    126       {ECO:0000244|PDB:4LY1}.
FT   STRAND      131    135       {ECO:0000244|PDB:4LY1}.
FT   STRAND      152    154       {ECO:0000244|PDB:5IWG}.
FT   HELIX       156    164       {ECO:0000244|PDB:4LY1}.
FT   TURN        165    167       {ECO:0000244|PDB:4LY1}.
FT   STRAND      171    175       {ECO:0000244|PDB:4LY1}.
FT   STRAND      177    179       {ECO:0000244|PDB:4LY1}.
FT   HELIX       182    187       {ECO:0000244|PDB:4LY1}.
FT   TURN        188    190       {ECO:0000244|PDB:4LY1}.
FT   STRAND      192    201       {ECO:0000244|PDB:4LY1}.
FT   HELIX       218    220       {ECO:0000244|PDB:4LY1}.
FT   STRAND      224    229       {ECO:0000244|PDB:4LY1}.
FT   HELIX       235    253       {ECO:0000244|PDB:4LY1}.
FT   STRAND      256    261       {ECO:0000244|PDB:4LY1}.
FT   HELIX       264    266       {ECO:0000244|PDB:4LY1}.
FT   HELIX       279    291       {ECO:0000244|PDB:4LY1}.
FT   STRAND      296    299       {ECO:0000244|PDB:4LY1}.
FT   HELIX       306    320       {ECO:0000244|PDB:4LY1}.
FT   HELIX       335    338       {ECO:0000244|PDB:4LY1}.
FT   TURN        339    341       {ECO:0000244|PDB:4LY1}.
FT   STRAND      343    345       {ECO:0000244|PDB:4LY1}.
FT   HELIX       357    371       {ECO:0000244|PDB:4LY1}.
SQ   SEQUENCE   488 AA;  55364 MW;  775419CCCDAE07FA CRC64;
     MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA
     TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA
     GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH
     GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ
     IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG
     GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
     EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE
     FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKTD VKEEDKSKDN SGEKTDTKGT
     KSEQLSNP
//
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