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Histone deacetylase 2 (HD2) (EC 3.5.1.98)

 HDAC2_HUMAN             Reviewed;         488 AA.
Q92769; B3KRS5; B4DL58; E1P561; Q5SRI8; Q5SZ86; Q8NEH4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
22-NOV-2017, entry version 198.
RecName: Full=Histone deacetylase 2;
Short=HD2;
EC=3.5.1.98;
Name=HDAC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-230.
TISSUE=Mammary gland;
PubMed=8917507; DOI=10.1073/pnas.93.23.12845;
Yang W.-M., Inouye C.J., Zeng Y., Bearss D., Seto E.;
"Transcriptional repression by YY1 is mediated by interaction with a
mammalian homolog of the yeast global regulator RPD3.";
Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
HIS-315.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH ATR, AND IDENTIFICATION IN A COMPLEX CONTAINING ATR
AND CHD4.
PubMed=10545197; DOI=10.1021/bi991614n;
Schmidt D.R., Schreiber S.L.;
"Molecular association between ATR and two components of the
nucleosome remodeling and deacetylating complex, HDAC2 and CHD4.";
Biochemistry 38:14711-14717(1999).
[7]
INTERACTION WITH SNW1.
PubMed=10644367; DOI=10.1128/JVI.74.4.1939-1947.2000;
Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.;
"A role for SKIP in EBNA2 activation of CBF1-repressed promoters.";
J. Virol. 74:1939-1947(2000).
[8]
INTERACTION WITH DNMT1 AND DMAP1.
PubMed=10888872; DOI=10.1038/77023;
Rountree M.R., Bachman K.E., Baylin S.B.;
"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
replication foci.";
Nat. Genet. 25:269-277(2000).
[9]
REVIEW ON DEACETYLASE COMPLEXES.
PubMed=10904264; DOI=10.1016/S0168-9525(00)02066-7;
Ahringer J.;
"NuRD and SIN3 histone deacetylase complexes in development.";
Trends Genet. 16:351-356(2000).
[10]
INTERACTION WITH MINT.
PubMed=11331609; DOI=10.1101/gad.871201;
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C.,
Hon M., Evans R.M.;
"Sharp, an inducible cofactor that integrates nuclear receptor
repression and activation.";
Genes Dev. 15:1140-1151(2001).
[11]
INTERACTION WITH CBFA2T3.
PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
Downing J.R., Meyers S., Hiebert S.W.;
"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
with multiple histone deacetylases and binds mSin3A through its
oligomerization domain.";
Mol. Cell. Biol. 21:6470-6483(2001).
[12]
INTERACTION WITH HDAC10.
PubMed=11739383; DOI=10.1074/jbc.M108055200;
Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R.,
Trogani N., Widmer R., Atadja P., Cohen D.;
"Isolation and characterization of a novel class II histone
deacetylase, HDAC10.";
J. Biol. Chem. 277:6656-6666(2002).
[13]
INTERACTION WITH SP3.
PubMed=12176973; DOI=10.1074/jbc.C200378200;
Sun J.M., Chen H.Y., Moniwa M., Litchfield D.W., Seto E., Davie J.R.;
"The transcriptional repressor Sp3 is associated with CK2-
phosphorylated histone deacetylase 2.";
J. Biol. Chem. 277:35783-35786(2002).
[14]
INTERACTION WITH DAXX AND DEK.
PubMed=12140263;
Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R.,
Grosveld G.;
"Daxx and histone deacetylase II associate with chromatin through an
interaction with core histones and the chromatin-associated protein
Dek.";
J. Cell Sci. 115:3319-3330(2002).
[15]
INTERACTION WITH BCL6.
PubMed=12402037; DOI=10.1038/ng1018;
Bereshchenko O.R., Gu W., Dalla-Favera R.;
"Acetylation inactivates the transcriptional repressor BCL6.";
Nat. Genet. 32:606-613(2002).
[16]
INTERACTION WITH APEX1.
PubMed=14633989; DOI=10.1093/emboj/cdg595;
Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.;
"Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation
of the parathyroid hormone gene.";
EMBO J. 22:6299-6309(2003).
[17]
INTERACTION WITH HCFC1.
PubMed=12670868; DOI=10.1101/gad.252103;
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
methyltransferase are tethered together selectively by the cell-
proliferation factor HCF-1.";
Genes Dev. 17:896-911(2003).
[18]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE BHC
COMPLEX WITH GSE1; GTF2I; HDAC1; HMG20B; KDM1A; PHF21A; RCOR1; ZMYM2;
ZMYM3 AND ZNF217.
PubMed=12493763; DOI=10.1074/jbc.M208992200;
Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
"A candidate X-linked mental retardation gene is a component of a new
family of histone deacetylase-containing complexes.";
J. Biol. Chem. 278:7234-7239(2003).
[19]
IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130;
SUDS3; ARID4B; HDAC1 AND HDAC2.
PubMed=12724404; DOI=10.1128/MCB.23.10.3456-3467.2003;
Fleischer T.C., Yun U.J., Ayer D.E.;
"Identification and characterization of three new components of the
mSin3A corepressor complex.";
Mol. Cell. Biol. 23:3456-3467(2003).
[20]
INTERACTION WITH PELP1.
PubMed=15456770; DOI=10.1074/jbc.M406831200;
Choi Y.B., Ko J.K., Shin J.;
"The transcriptional corepressor, PELP1, recruits HDAC2 and masks
histones using two separate domains.";
J. Biol. Chem. 279:50930-50941(2004).
[21]
INTERACTION WITH NRIP1.
PubMed=15060175; DOI=10.1093/nar/gkh524;
Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P.,
Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
"Multiple domains of the receptor-interacting protein 140 contribute
to transcription inhibition.";
Nucleic Acids Res. 32:1957-1966(2004).
[22]
INTERACTION WITH JMJD2A.
PubMed=15927959; DOI=10.1074/jbc.M413687200;
Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S.,
Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
"Functional characterization of JMJD2A, a histone deacetylase- and
retinoblastoma-binding protein.";
J. Biol. Chem. 280:28507-28518(2005).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[24]
INTERACTION WITH SAP30L.
PubMed=16820529; DOI=10.1093/nar/gkl401;
Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K.,
Peterson P., Maeki M., Kainulainen H., Lohi O.;
"SAP30L interacts with members of the Sin3A corepressor complex and
targets Sin3A to the nucleolus.";
Nucleic Acids Res. 34:3288-3298(2006).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[26]
IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC1.
PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B.,
Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J.,
Shi Y.;
"CDYL bridges REST and histone methyltransferases for gene repression
and suppression of cellular transformation.";
Mol. Cell 32:718-726(2008).
[27]
INTERACTION WITH BCL6.
PubMed=18212045; DOI=10.1128/MCB.01400-07;
Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A.,
Ye B.H.;
"CtBP is an essential corepressor for BCL6 autoregulation.";
Mol. Cell. Biol. 28:2175-2186(2008).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
INTERACTION WITH PIMREG.
PubMed=18757745; DOI=10.1073/pnas.0709227105;
Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III,
Fang G.;
"RCS1, a substrate of APC/C, controls the metaphase to anaphase
transition.";
Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[31]
FUNCTION, AND INTERACTION WITH TSHZ3.
PubMed=19343227; DOI=10.1371/journal.pone.0005071;
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
"FE65 binds Teashirt, inhibiting expression of the primate-specific
caspase-4.";
PLoS ONE 4:E5071-E5071(2009).
[32]
INTERACTION WITH CHFR.
PubMed=19182791; DOI=10.1038/ncb1837;
Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J.,
Chung C.H., Deshaies R.J., Seol J.H.;
"Chfr is linked to tumour metastasis through the downregulation of
HDAC1.";
Nat. Cell Biol. 11:295-302(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-422, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[36]
FUNCTION, AND INTERACTION WITH MTA1.
PubMed=21965678; DOI=10.1074/jbc.M111.267237;
Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
"SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor
antigen 1 (MTA1) synergistically regulate its transcriptional
repressor function.";
J. Biol. Chem. 286:43793-43808(2011).
[37]
INTERACTION WITH BEND3.
PubMed=21914818; DOI=10.1242/jcs.086603;
Sathyan K.M., Shen Z., Tripathi V., Prasanth K.V., Prasanth S.G.;
"A BEN-domain-containing protein associates with heterochromatin and
represses transcription.";
J. Cell Sci. 124:3149-3163(2011).
[38]
INTERACTION WITH SMARCAD1.
PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W.,
Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M.,
Varga-Weisz P., Mermoud J.E.;
"Maintenance of silent chromatin through replication requires SWI/SNF-
like chromatin remodeler SMARCAD1.";
Mol. Cell 42:285-296(2011).
[39]
INTERACTION WITH DNTTIP1 AND ZNF541.
PubMed=21573134; DOI=10.1371/journal.pgen.1002065;
Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L.,
Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.;
"Nuclear cGMP-dependent kinase regulates gene expression via activity-
dependent recruitment of a conserved histone deacetylase complex.";
PLoS Genet. 7:E1002065-E1002065(2011).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-407; SER-422
AND SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[42]
INTERACTION WITH NACC2.
PubMed=22926524; DOI=10.1038/onc.2012.386;
Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L.,
Yao Z., Shang Y.;
"RBB, a novel transcription repressor, represses the transcription of
HDM2 oncogene.";
Oncogene 32:3711-3721(2013).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-462, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[45]
SUBCELLULAR LOCATION, AND INTERACTION WITH MTA1.
PubMed=24970816;
Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C.,
Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.;
"The subcellular distribution and function of MTA1 in cancer
differentiation.";
Oncotarget 5:5153-5164(2014).
[46]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[47]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-462 AND LYS-481, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[48]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-452; LYS-458;
LYS-462; LYS-478 AND LYS-481, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[49]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-374 IN COMPLEX WITH
SUBSTITUTED N-(2-AMINOPHENYL)BENZAMIDE INHIBITORS.
PubMed=20392638; DOI=10.1016/j.bmcl.2010.03.091;
Bressi J.C., Jennings A.J., Skene R., Wu Y., Melkus R., De Jong R.,
O'Connell S., Grimshaw C.E., Navre M., Gangloff A.R.;
"Exploration of the HDAC2 foot pocket: Synthesis and SAR of
substituted N-(2-aminophenyl)benzamides.";
Bioorg. Med. Chem. Lett. 20:3142-3145(2010).
-!- FUNCTION: Responsible for the deacetylation of lysine residues on
the N-terminal part of the core histones (H2A, H2B, H3 and H4).
Histone deacetylation gives a tag for epigenetic repression and
plays an important role in transcriptional regulation, cell cycle
progression and developmental events. Histone deacetylases act via
the formation of large multiprotein complexes. Forms
transcriptional repressor complexes by associating with MAD, SIN3,
YY1 and N-COR. Interacts in the late S-phase of DNA-replication
with DNMT1 in the other transcriptional repressor complex composed
of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its
transcriptional repressor activity. Component of a
RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone
deacetylase (HDAC) recruitment, a number of genes implicated in
multilineage blood cell development. May be involved in the
transcriptional repression of circadian target genes, such as
PER1, mediated by CRY1 through histone deacetylation. Involved in
MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.
{ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21965678}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex
composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex
associates with MTA2, MBD3, MTA1L1, CHD3 and CHD4 to form the
nucleosome remodeling and histone deacetylation (NuRD) complex, or
with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex.
Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly
with GFI1 and GFI1B. Interacts with SNW1, HDAC7, PRDM6, SAP30,
SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone
region). Component of a BHC histone deacetylase complex that
contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC
complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
Part of a complex containing the core histones H2A, H2B, H3 and
H4, DEK and unphosphorylated DAXX. Part of a complex containing
ATR and CHD4. Forms a heterologous complex at least with YY1.
Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1,
KDM4A and PELP1. Component of a mSin3A corepressor complex that
contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts
with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with
SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with
APEX1; the interaction is not dependent on the acetylated status
of APEX1. Part of a complex composed of TRIM28, HDAC1, HDAC2 and
EHMT2. Interacts with PIMREG. Interacts with BCL6 (non-acetylated
form). Part of a complex containing at least CDYL, MIER1, MIER2,
HDAC1 and HDAC2. Interacts with CRY1, INSM1 and ZNF431. Interacts
with NACC2. Interacts with MTA1, with a preference for sumoylated
MTA1. Interacts with SIX3 (By similarity). Interacts with BEND3.
Component of a histone deacetylase complex containing DNTTIP1,
ZNF541, HDAC1 and HDAC2 (PubMed:21573134).
{ECO:0000250|UniProtKB:P70288, ECO:0000269|PubMed:10545197,
ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:10888872,
ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:11533236,
ECO:0000269|PubMed:11739383, ECO:0000269|PubMed:12140263,
ECO:0000269|PubMed:12176973, ECO:0000269|PubMed:12402037,
ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:12670868,
ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:14633989,
ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15456770,
ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16820529,
ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:18757745,
ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:19182791,
ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:20392638,
ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:21573134,
ECO:0000269|PubMed:21914818, ECO:0000269|PubMed:21965678,
ECO:0000269|PubMed:22926524, ECO:0000269|PubMed:24970816}.
-!- INTERACTION:
Q9C0K0:BCL11B; NbExp=3; IntAct=EBI-301821, EBI-6597578;
Q9HCU9:BRMS1; NbExp=4; IntAct=EBI-301821, EBI-714781;
Q9UER7:DAXX; NbExp=2; IntAct=EBI-301821, EBI-77321;
P51610:HCFC1; NbExp=2; IntAct=EBI-301821, EBI-396176;
Q13547:HDAC1; NbExp=12; IntAct=EBI-301821, EBI-301834;
Q2HR82:K8 (xeno); NbExp=7; IntAct=EBI-301821, EBI-9006943;
Q9UIS9:MBD1; NbExp=2; IntAct=EBI-301821, EBI-867196;
Q13330:MTA1; NbExp=5; IntAct=EBI-301821, EBI-714236;
P01106:MYC; NbExp=2; IntAct=EBI-301821, EBI-447544;
P06748:NPM1; NbExp=2; IntAct=EBI-301821, EBI-78579;
P48382:RFX5; NbExp=4; IntAct=EBI-301821, EBI-923266;
Q96ST3:SIN3A; NbExp=5; IntAct=EBI-301821, EBI-347218;
O95863:SNAI1; NbExp=2; IntAct=EBI-301821, EBI-1045459;
Q9HD15:SRA1; NbExp=2; IntAct=EBI-301821, EBI-727136;
O43463:SUV39H1; NbExp=3; IntAct=EBI-301821, EBI-349968;
Q17R98:ZNF827; NbExp=2; IntAct=EBI-301821, EBI-5564776;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24970816}.
Cytoplasm {ECO:0000269|PubMed:24970816}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92769-1; Sequence=Displayed;
Name=2;
IsoId=Q92769-3; Sequence=VSP_056175;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed; lower levels in brain and
lung.
-!- PTM: S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-
262 and Cys-274 does not affect the enzyme activity but abolishes
chromatin-binding, leading to increases acetylation of histones
and activate genes that are associated with neuronal development.
In embryonic cortical neurons, S-Nitrosylation regulates dendritic
growth and branching. {ECO:0000250|UniProtKB:P70288}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH31055.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAG59420.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HDAC2ID40803ch6q22.html";
-----------------------------------------------------------------------
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EMBL; U31814; AAC50814.1; -; mRNA.
EMBL; AK092156; BAG52487.1; -; mRNA.
EMBL; AK296856; BAG59420.1; ALT_INIT; mRNA.
EMBL; AL590398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL671967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; FO393415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48252.1; -; Genomic_DNA.
EMBL; CH471051; EAW48253.1; -; Genomic_DNA.
EMBL; CH471051; EAW48254.1; -; Genomic_DNA.
EMBL; CH471051; EAW48255.1; -; Genomic_DNA.
EMBL; BC031055; AAH31055.2; ALT_INIT; mRNA.
CCDS; CCDS43493.2; -. [Q92769-1]
RefSeq; NP_001518.3; NM_001527.3. [Q92769-1]
RefSeq; XP_011534090.1; XM_011535788.1. [Q92769-3]
RefSeq; XP_016866288.1; XM_017010799.1. [Q92769-3]
UniGene; Hs.3352; -.
PDB; 3MAX; X-ray; 2.05 A; A/B/C=9-374.
PDB; 4LXZ; X-ray; 1.85 A; A/B/C=8-376.
PDB; 4LY1; X-ray; 1.57 A; A/B/C=8-376.
PDB; 5IWG; X-ray; 1.66 A; A/B/C=8-375.
PDB; 5IX0; X-ray; 1.72 A; A/B/C=7-375.
PDBsum; 3MAX; -.
PDBsum; 4LXZ; -.
PDBsum; 4LY1; -.
PDBsum; 5IWG; -.
PDBsum; 5IX0; -.
ProteinModelPortal; Q92769; -.
SMR; Q92769; -.
BioGrid; 109316; 331.
CORUM; Q92769; -.
DIP; DIP-24220N; -.
IntAct; Q92769; 168.
MINT; MINT-90593; -.
STRING; 9606.ENSP00000430432; -.
BindingDB; Q92769; -.
ChEMBL; CHEMBL1937; -.
DrugBank; DB01223; Aminophylline.
DrugBank; DB05015; Belinostat.
DrugBank; DB00227; Lovastatin.
DrugBank; DB05651; MGCD-0103.
DrugBank; DB01303; Oxtriphylline.
DrugBank; DB06603; Panobinostat.
DrugBank; DB06176; Romidepsin.
DrugBank; DB05223; SB939.
DrugBank; DB00277; Theophylline.
DrugBank; DB00313; Valproic Acid.
DrugBank; DB02546; Vorinostat.
GuidetoPHARMACOLOGY; 2616; -.
iPTMnet; Q92769; -.
PhosphoSitePlus; Q92769; -.
BioMuta; HDAC2; -.
DMDM; 68068066; -.
EPD; Q92769; -.
MaxQB; Q92769; -.
PaxDb; Q92769; -.
PeptideAtlas; Q92769; -.
PRIDE; Q92769; -.
DNASU; 3066; -.
Ensembl; ENST00000368632; ENSP00000357621; ENSG00000196591. [Q92769-3]
Ensembl; ENST00000519065; ENSP00000430432; ENSG00000196591. [Q92769-1]
Ensembl; ENST00000519108; ENSP00000430008; ENSG00000196591. [Q92769-3]
GeneID; 3066; -.
KEGG; hsa:3066; -.
UCSC; uc003pwc.3; human. [Q92769-1]
CTD; 3066; -.
DisGeNET; 3066; -.
EuPathDB; HostDB:ENSG00000196591.11; -.
GeneCards; HDAC2; -.
HGNC; HGNC:4853; HDAC2.
HPA; CAB005054; -.
HPA; HPA011727; -.
MIM; 605164; gene.
neXtProt; NX_Q92769; -.
OpenTargets; ENSG00000196591; -.
PharmGKB; PA29227; -.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062889; -.
HOGENOM; HOG000225180; -.
HOVERGEN; HBG057112; -.
InParanoid; Q92769; -.
KO; K06067; -.
OMA; KRVCYFF; -.
OrthoDB; EOG091G067J; -.
PhylomeDB; Q92769; -.
TreeFam; TF106171; -.
BRENDA; 3.5.1.98; 2681.
Reactome; R-HSA-193670; p75NTR negatively regulates cell cycle via SC1.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SABIO-RK; Q92769; -.
SIGNOR; Q92769; -.
ChiTaRS; HDAC2; human.
EvolutionaryTrace; Q92769; -.
GeneWiki; Histone_deacetylase_2; -.
GenomeRNAi; 3066; -.
PRO; PR:Q92769; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000196591; -.
CleanEx; HS_HDAC2; -.
ExpressionAtlas; Q92769; baseline and differential.
Genevisible; Q92769; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0001047; F:core promoter binding; IEA:Ensembl.
GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0033558; F:protein deacetylase activity; IMP:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; IC:BHF-UCL.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; ISS:BHF-UCL.
GO; GO:0009913; P:epidermal cell differentiation; ISS:BHF-UCL.
GO; GO:0061029; P:eyelid development in camera-type eye; ISS:BHF-UCL.
GO; GO:0061198; P:fungiform papilla formation; ISS:BHF-UCL.
GO; GO:0060789; P:hair follicle placode formation; ISS:BHF-UCL.
GO; GO:0016575; P:histone deacetylation; IMP:BHF-UCL.
GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
GO; GO:0006344; P:maintenance of chromatin silencing; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
GO; GO:0061000; P:negative regulation of dendritic spine development; IEA:Ensembl.
GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IC:BHF-UCL.
GO; GO:0010977; P:negative regulation of neuron projection development; ISS:BHF-UCL.
GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; IEA:Ensembl.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IC:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:Ensembl.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0045862; P:positive regulation of proteolysis; IMP:BHF-UCL.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Biological rhythms;
Chromatin regulator; Complete proteome; Cytoplasm; Hydrolase;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; S-nitrosylation; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 488 Histone deacetylase 2.
/FTId=PRO_0000114693.
REGION 9 322 Histone deacetylase.
COMPBIAS 300 303 Poly-Gly.
ACT_SITE 142 142 {ECO:0000250}.
MOD_RES 75 75 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 221 221 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13547}.
MOD_RES 262 262 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P70288}.
MOD_RES 274 274 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P70288}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CROSSLNK 75 75 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 439 439 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13547}.
CROSSLNK 452 452 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 458 458 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 462 462 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 478 478 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 481 481 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 30 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056175.
VARIANT 230 230 R -> C (in dbSNP:rs1042903).
{ECO:0000269|PubMed:8917507}.
/FTId=VAR_025311.
VARIANT 315 315 Y -> H (in dbSNP:rs17852888).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_025312.
CONFLICT 93 94 QR -> HI (in Ref. 1; AAC50814).
{ECO:0000305}.
CONFLICT 103 103 V -> A (in Ref. 1; AAC50814).
{ECO:0000305}.
CONFLICT 146 146 S -> Y (in Ref. 1; AAC50814).
{ECO:0000305}.
CONFLICT 248 248 K -> M (in Ref. 2; BAG59420).
{ECO:0000305}.
CONFLICT 281 281 G -> D (in Ref. 2; BAG59420).
{ECO:0000305}.
STRAND 12 15 {ECO:0000244|PDB:4LY1}.
HELIX 20 22 {ECO:0000244|PDB:4LY1}.
HELIX 34 45 {ECO:0000244|PDB:4LY1}.
HELIX 48 51 {ECO:0000244|PDB:4LY1}.
STRAND 52 55 {ECO:0000244|PDB:4LY1}.
HELIX 62 65 {ECO:0000244|PDB:4LY1}.
TURN 66 68 {ECO:0000244|PDB:4LY1}.
HELIX 71 79 {ECO:0000244|PDB:4LY1}.
TURN 82 84 {ECO:0000244|PDB:4LY1}.
HELIX 85 88 {ECO:0000244|PDB:4LY1}.
HELIX 89 95 {ECO:0000244|PDB:4LY1}.
STRAND 98 101 {ECO:0000244|PDB:4LY1}.
HELIX 107 126 {ECO:0000244|PDB:4LY1}.
STRAND 131 135 {ECO:0000244|PDB:4LY1}.
STRAND 152 154 {ECO:0000244|PDB:5IWG}.
HELIX 156 164 {ECO:0000244|PDB:4LY1}.
TURN 165 167 {ECO:0000244|PDB:4LY1}.
STRAND 171 175 {ECO:0000244|PDB:4LY1}.
STRAND 177 179 {ECO:0000244|PDB:4LY1}.
HELIX 182 187 {ECO:0000244|PDB:4LY1}.
TURN 188 190 {ECO:0000244|PDB:4LY1}.
STRAND 192 201 {ECO:0000244|PDB:4LY1}.
HELIX 218 220 {ECO:0000244|PDB:4LY1}.
STRAND 224 229 {ECO:0000244|PDB:4LY1}.
HELIX 235 253 {ECO:0000244|PDB:4LY1}.
STRAND 256 261 {ECO:0000244|PDB:4LY1}.
HELIX 264 266 {ECO:0000244|PDB:4LY1}.
HELIX 279 291 {ECO:0000244|PDB:4LY1}.
STRAND 296 299 {ECO:0000244|PDB:4LY1}.
HELIX 306 320 {ECO:0000244|PDB:4LY1}.
HELIX 335 338 {ECO:0000244|PDB:4LY1}.
TURN 339 341 {ECO:0000244|PDB:4LY1}.
STRAND 343 345 {ECO:0000244|PDB:4LY1}.
HELIX 357 371 {ECO:0000244|PDB:4LY1}.
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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