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 03-AUG-2022, entry version 232.
DE RecName: Full=Histone deacetylase 2 {ECO:0000305};
DE Short=HD2;
DE EC=3.5.1.98 {ECO:0000269|PubMed:28497810};
DE AltName: Full=Protein deacylase HDAC2 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000269|PubMed:28497810, ECO:0000269|PubMed:29192674};
GN Name=HDAC2 {ECO:0000303|PubMed:10545197, ECO:0000312|HGNC:HGNC:4853};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH YY1, AND VARIANT
RP 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 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 project:
RT 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 AND
RP 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 nucleosome
RT 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., Hon M.,
RA Evans R.M.;
RT "Sharp, an inducible cofactor that integrates nuclear receptor repression
RT 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 with
RT multiple histone deacetylases and binds mSin3A through its oligomerization
RT 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 deacetylase,
RT 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-phosphorylated
RT histone deacetylase 2.";
RL J. Biol. Chem. 277:35783-35786(2002).
RN [14]
RP INTERACTION WITH DAXX AND DEK.
RX PubMed=12140263; DOI=10.1242/jcs.115.16.3319;
RA Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.;
RT "Daxx and histone deacetylase II associate with chromatin through an
RT interaction with core histones and the chromatin-associated protein 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 of the
RT 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 COMPLEX
RP WITH GSE1; GTF2I; HDAC1; HMG20B; KDM1A; PHF21A; RCOR1; ZMYM2; ZMYM3 AND
RP 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 FUNCTION, AND IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A;
RP SAP130; 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 mSin3A
RT 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 histones
RT 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., 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 [22]
RP INTERACTION WITH KDM4A.
RX PubMed=15927959; DOI=10.1074/jbc.m413687200;
RA Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H.,
RA 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 SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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 targets
RT Sin3A to the nucleolus.";
RL Nucleic Acids Res. 34:3288-3298(2006).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP 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 the
RT 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., Macia E.,
RA Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.;
RT "CDYL bridges REST and histone methyltransferases for gene repression and
RT 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, 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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [31]
RP INTERACTION WITH RUVBL2; APPL2; APPL1; HDAC1 AND CTNNB1.
RX PubMed=19433865; DOI=10.1074/jbc.m109.007237;
RA Rashid S., Pilecka I., Torun A., Olchowik M., Bielinska B., Miaczynska M.;
RT "Endosomal adaptor proteins APPL1 and APPL2 are novel activators of beta-
RT catenin/TCF-mediated transcription.";
RL J. Biol. Chem. 284:18115-18128(2009).
RN [32]
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 [33]
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., Chung C.H.,
RA Deshaies R.J., Seol J.H.;
RT "Chfr is linked to tumour metastasis through the downregulation of HDAC1.";
RL Nat. Cell Biol. 11:295-302(2009).
RN [34]
RP INTERACTION WITH SPHK2.
RX PubMed=19729656; DOI=10.1126/science.1176709;
RA Hait N.C., Allegood J., Maceyka M., Strub G.M., Harikumar K.B., Singh S.K.,
RA Luo C., Marmorstein R., Kordula T., Milstien S., Spiegel S.;
RT "Regulation of histone acetylation in the nucleus by sphingosine-1-
RT phosphate.";
RL Science 325:1254-1257(2009).
RN [35]
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 [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [37]
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., Buerckstuemmer T.,
RA 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 [38]
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 antigen 1
RT (MTA1) synergistically regulate its transcriptional repressor function.";
RL J. Biol. Chem. 286:43793-43808(2011).
RN [39]
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 [40]
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., Hawkes N.,
RA Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P.,
RA Mermoud J.E.;
RT "Maintenance of silent chromatin through replication requires SWI/SNF-like
RT chromatin remodeler SMARCAD1.";
RL Mol. Cell 42:285-296(2011).
RN [41]
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 [42]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-407; SER-422 AND
RP SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [44]
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., Yao Z.,
RA Shang Y.;
RT "RBB, a novel transcription repressor, represses the transcription of HDM2
RT oncogene.";
RL Oncogene 32:3711-3721(2013).
RN [45]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [46]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-462, AND IDENTIFICATION BY MASS
RP 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 [47]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MTA1.
RX PubMed=24970816; DOI=10.18632/oncotarget.2095;
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 [48]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481, AND IDENTIFICATION BY MASS
RP 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 [49]
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 replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [50]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28497810; DOI=10.1038/cr.2017.68;
RA Wei W., Liu X., Chen J., Gao S., Lu L., Zhang H., Ding G., Wang Z.,
RA Chen Z., Shi T., Li J., Yu J., Wong J.;
RT "Class I histone deacetylases are major histone decrotonylases: evidence
RT for critical and broad function of histone crotonylation in
RT transcription.";
RL Cell Res. 27:898-915(2017).
RN [51]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-452; LYS-458; LYS-462;
RP LYS-478 AND LYS-481, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [52]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
RN [53]
RP INTERACTION WITH ZNF263.
RX PubMed=32051553; DOI=10.1038/s41388-020-1206-7;
RA Yu Z., Feng J., Wang W., Deng Z., Zhang Y., Xiao L., Wang Z., Liu C.,
RA Liu Q., Chen S., Wu M.;
RT "The EGFR-ZNF263 signaling axis silences SIX3 in glioblastoma
RT epigenetically.";
RL Oncogene 39:3163-3178(2020).
RN [54]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-374 IN COMPLEX WITH SUBSTITUTED
RP 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 substituted N-
RT (2-aminophenyl)benzamides.";
RL Bioorg. Med. Chem. Lett. 20:3142-3145(2010).
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:28497810). Histone deacetylation gives a tag for
CC epigenetic repression and plays an important role in transcriptional
CC regulation, cell cycle progression and developmental events (By
CC similarity). Histone deacetylases act via the formation of large
CC multiprotein complexes (By similarity). Forms transcriptional repressor
CC complexes by associating with MAD, SIN3, YY1 and N-COR
CC (PubMed:12724404). 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 (By
CC similarity). Also deacetylates non-histone targets: deacetylates TSHZ3,
CC thereby regulating its transcriptional repressor activity
CC (PubMed:19343227). May be involved in the transcriptional repression of
CC circadian target genes, such as PER1, mediated by CRY1 through histone
CC deacetylation (By similarity). Involved in MTA1-mediated
CC transcriptional corepression of TFF1 and CDKN1A (PubMed:21965678). In
CC addition to protein deacetylase activity, also acts as protein-lysine
CC deacylase by recognizing other acyl groups: catalyzes removal of (2E)-
CC butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl
CC groups from lysine residues, leading to protein decrotonylation and de-
CC 2-hydroxyisobutyrylation, respectively (PubMed:28497810,
CC PubMed:29192674). {ECO:0000250|UniProtKB:P70288,
CC ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:19343227,
CC ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:28497810,
CC ECO:0000269|PubMed:29192674}.
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:28497810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000269|PubMed:28497810};
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:0000305|PubMed:19343227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000305|PubMed:19343227};
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:28497810};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000269|PubMed:28497810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] = 2-
CC hydroxy-2-methylpropanoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69176,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:19641, ChEBI:CHEBI:29969, ChEBI:CHEBI:144968;
CC Evidence={ECO:0000269|PubMed:29192674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69177;
CC Evidence={ECO:0000269|PubMed:29192674};
CC -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex composed
CC of HDAC1, HDAC2, RBBP4 and RBBP7 (PubMed:10904264). The core complex
CC associates with MTA2, 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:10904264).
CC Component of a RCOR/GFI/KDM1A/HDAC complex (By similarity). Component
CC of a BHC histone deacetylase complex that contains HDAC1, HDAC2,
CC HMG20B, KDM1A, RCOR1 and PHF21A (PubMed:12493763). The BHC complex may
CC also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I (PubMed:12493763).
CC Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK
CC and unphosphorylated DAXX (PubMed:12140263). Part of a complex
CC containing ATR and CHD4 (PubMed:10545197). Forms a heterologous complex
CC at least with YY1 (PubMed:8917507). Interacts in the late S-phase of
CC DNA-replication with DNMT1 in the other transcriptional repressor
CC complex composed of DNMT1, DMAP1, PCNA, CAF1 (PubMed:10888872).
CC Component of a mSin3A corepressor complex that contains SIN3A, SAP130,
CC SUDS3, ARID4B, HDAC1 and HDAC2 (PubMed:12724404). Part of a complex
CC composed of TRIM28, HDAC1, HDAC2 and EHMT2 (PubMed:10904264). Part of a
CC complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2
CC (PubMed:19061646). Component of a histone deacetylase complex
CC containing DNTTIP1, ZNF541, HDAC1 and HDAC2 (PubMed:21573134). Forms a
CC complex comprising APPL1, RUVBL2, APPL2, CTNNB1 and HDAC1
CC (PubMed:19433865). Interacts with SPHK2 (PubMed:19729656). Interacts
CC directly with GFI1 and GFI1B (By similarity). Interacts with SNW1,
CC HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1 (PubMed:10644367). Interacts
CC with the MACROH2A1 (via the non-histone region) (By similarity).
CC Interacts with ATR, CBFA2T3, DNMT1, SMARCAD1, MINT, HDAC10, HCFC1,
CC NRIP1, KDM4A and PELP1 (PubMed:15927959, PubMed:15456770,
CC PubMed:15060175, PubMed:11331609, PubMed:21549307, PubMed:12670868,
CC PubMed:11533236, PubMed:11739383, PubMed:10888872). Interacts with CHFR
CC and SAP30L (PubMed:19182791, PubMed:16820529). Interacts (CK2
CC phosphorylated form) with SP3 (PubMed:12176973). Interacts with TSHZ3
CC (via its N-terminus) (PubMed:19343227). Interacts with APEX1; the
CC interaction is not dependent on the acetylated status of APEX1
CC (PubMed:14633989). Interacts with PIMREG (PubMed:18757745). Interacts
CC with BCL6 (non-acetylated form) (PubMed:18212045, PubMed:12402037).
CC Interacts with CRY1, INSM1 and ZNF431 (By similarity). Interacts with
CC NACC2 (PubMed:22926524). Interacts with MTA1, with a preference for
CC sumoylated MTA1 (PubMed:21965678, PubMed:24970816). Interacts with SIX3
CC (By similarity). Interacts with BEND3 (PubMed:21914818). Interacts with
CC ZNF263; recruited to the SIX3 promoter along with other proteins
CC involved in chromatin modification and transcriptional corepression
CC where it contributes to transcriptional repression (PubMed:32051553).
CC Interacts with PWWP2B (By similarity). {ECO:0000250|UniProtKB:P70288,
CC ECO:0000269|PubMed:10545197, ECO:0000269|PubMed:10644367,
CC ECO:0000269|PubMed:10888872, ECO:0000269|PubMed:11331609,
CC ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11739383,
CC ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:12176973,
CC ECO:0000269|PubMed:12402037, ECO:0000269|PubMed:12493763,
CC ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:12724404,
CC ECO:0000269|PubMed:14633989, ECO:0000269|PubMed:15060175,
CC ECO:0000269|PubMed:15456770, ECO:0000269|PubMed:15927959,
CC ECO:0000269|PubMed:16820529, ECO:0000269|PubMed:18212045,
CC ECO:0000269|PubMed:18757745, ECO:0000269|PubMed:19061646,
CC ECO:0000269|PubMed:19182791, ECO:0000269|PubMed:19343227,
CC ECO:0000269|PubMed:19433865, ECO:0000269|PubMed:19729656,
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 ECO:0000269|PubMed:32051553, ECO:0000269|PubMed:8917507,
CC ECO:0000303|PubMed:10904264}.
CC -!- INTERACTION:
CC Q92769; Q9C0K0: BCL11B; NbExp=3; IntAct=EBI-301821, EBI-6597578;
CC Q92769; Q9HCU9: BRMS1; NbExp=4; IntAct=EBI-301821, EBI-714781;
CC Q92769; Q9UER7: DAXX; NbExp=2; IntAct=EBI-301821, EBI-77321;
CC Q92769; P51610: HCFC1; NbExp=2; IntAct=EBI-301821, EBI-396176;
CC Q92769; Q13547: HDAC1; NbExp=16; IntAct=EBI-301821, EBI-301834;
CC Q92769; Q9UIS9: MBD1; NbExp=2; IntAct=EBI-301821, EBI-867196;
CC Q92769; Q13330: MTA1; NbExp=6; IntAct=EBI-301821, EBI-714236;
CC Q92769; P01106: MYC; NbExp=2; IntAct=EBI-301821, EBI-447544;
CC Q92769; P06748: NPM1; NbExp=2; IntAct=EBI-301821, EBI-78579;
CC Q92769; P48382: RFX5; NbExp=4; IntAct=EBI-301821, EBI-923266;
CC Q92769; Q96ST3: SIN3A; NbExp=6; IntAct=EBI-301821, EBI-347218;
CC Q92769; O95863: SNAI1; NbExp=2; IntAct=EBI-301821, EBI-1045459;
CC Q92769; Q9HD15: SRA1; NbExp=2; IntAct=EBI-301821, EBI-727136;
CC Q92769; O43463: SUV39H1; NbExp=3; IntAct=EBI-301821, EBI-349968;
CC Q92769; Q92618: ZNF516; NbExp=6; IntAct=EBI-301821, EBI-2799490;
CC Q92769; Q17R98: ZNF827; NbExp=2; IntAct=EBI-301821, EBI-5564776;
CC Q92769; Q2HR82: K8; Xeno; NbExp=7; IntAct=EBI-301821, EBI-9006943;
CC Q92769; PRO_0000449623 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-301821, EBI-25475864;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24970816}. Cytoplasm
CC {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 -!- TISSUE SPECIFICITY: Widely expressed; lower levels in brain and lung.
CC -!- PTM: S-nitrosylated by GAPDH. In neurons, S-nitrosylation at Cys-262
CC and Cys-274 does not affect enzyme activity, but induces HDAC2 release
CC from chromatin. This in turn increases acetylation of histones
CC surrounding neurotrophin-dependent gene promoters and promotes their
CC transcription. In embryonic cortical neurons, S-Nitrosylation regulates
CC dendritic 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=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG59420.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HDAC2ID40803ch6q22.html";
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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 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 PDB; 6WBW; X-ray; 1.46 A; A/B/C=1-376.
DR PDB; 6WBZ; X-ray; 1.32 A; A/B/C=1-376.
DR PDB; 6WHN; X-ray; 1.54 A; A/B/C=2-385.
DR PDB; 6WHO; X-ray; 2.20 A; A/B/C=2-385.
DR PDB; 6WHQ; X-ray; 2.35 A; A/B/C=2-385.
DR PDB; 6WHZ; X-ray; 2.90 A; A/B/C=2-385.
DR PDB; 6WI3; X-ray; 2.35 A; A/B/C=2-385.
DR PDB; 6XDM; X-ray; 1.56 A; A/B/C=1-376.
DR PDB; 6XEB; X-ray; 1.50 A; A/B/C=1-376.
DR PDB; 6XEC; X-ray; 1.70 A; A/B/C=1-376.
DR PDB; 7JS8; X-ray; 1.63 A; A/B/C=1-376.
DR PDB; 7KBG; X-ray; 1.26 A; A/B/C=1-376.
DR PDB; 7KBH; X-ray; 2.68 A; A/B/C=1-376.
DR PDB; 7LTG; X-ray; 1.80 A; A/B/C=1-376.
DR PDB; 7LTK; X-ray; 1.59 A; A/B/C=1-376.
DR PDB; 7LTL; X-ray; 1.49 A; A/B/C=1-376.
DR PDB; 7MOS; X-ray; 1.70 A; A/B/C=1-376.
DR PDB; 7MOT; X-ray; 1.54 A; A/B/C=1-376.
DR PDB; 7MOX; X-ray; 1.69 A; A/B/C=1-376.
DR PDB; 7MOY; X-ray; 1.78 A; A/B/C=1-376.
DR PDB; 7MOZ; X-ray; 1.54 A; A/B/C=1-376.
DR PDBsum; 3MAX; -.
DR PDBsum; 4LXZ; -.
DR PDBsum; 4LY1; -.
DR PDBsum; 5IWG; -.
DR PDBsum; 5IX0; -.
DR PDBsum; 6G3O; -.
DR PDBsum; 6WBW; -.
DR PDBsum; 6WBZ; -.
DR PDBsum; 6WHN; -.
DR PDBsum; 6WHO; -.
DR PDBsum; 6WHQ; -.
DR PDBsum; 6WHZ; -.
DR PDBsum; 6WI3; -.
DR PDBsum; 6XDM; -.
DR PDBsum; 6XEB; -.
DR PDBsum; 6XEC; -.
DR PDBsum; 7JS8; -.
DR PDBsum; 7KBG; -.
DR PDBsum; 7KBH; -.
DR PDBsum; 7LTG; -.
DR PDBsum; 7LTK; -.
DR PDBsum; 7LTL; -.
DR PDBsum; 7MOS; -.
DR PDBsum; 7MOT; -.
DR PDBsum; 7MOX; -.
DR PDBsum; 7MOY; -.
DR PDBsum; 7MOZ; -.
DR AlphaFoldDB; Q92769; -.
DR SMR; Q92769; -.
DR BioGRID; 109316; 712.
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; 220.
DR MINT; Q92769; -.
DR STRING; 9606.ENSP00000430432; -.
DR BindingDB; Q92769; -.
DR ChEMBL; CHEMBL1937; -.
DR DrugBank; DB01223; Aminophylline.
DR DrugBank; DB01076; Atorvastatin.
DR DrugBank; DB05015; Belinostat.
DR DrugBank; DB01095; Fluvastatin.
DR DrugBank; DB00227; Lovastatin.
DR DrugBank; DB11830; Mocetinostat.
DR DrugBank; DB01303; Oxtriphylline.
DR DrugBank; DB06603; Panobinostat.
DR DrugBank; DB05223; Pracinostat.
DR DrugBank; DB00175; Pravastatin.
DR DrugBank; DB06176; Romidepsin.
DR DrugBank; DB00641; Simvastatin.
DR DrugBank; DB00277; Theophylline.
DR DrugBank; DB09091; Tixocortol.
DR DrugBank; DB00313; Valproic acid.
DR DrugBank; DB02546; Vorinostat.
DR DrugCentral; Q92769; -.
DR GuidetoPHARMACOLOGY; 2616; -.
DR GlyGen; Q92769; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92769; -.
DR MetOSite; Q92769; -.
DR PhosphoSitePlus; Q92769; -.
DR SwissPalm; Q92769; -.
DR BioMuta; HDAC2; -.
DR DMDM; 68068066; -.
DR EPD; Q92769; -.
DR jPOST; Q92769; -.
DR MassIVE; Q92769; -.
DR MaxQB; Q92769; -.
DR PaxDb; Q92769; -.
DR PeptideAtlas; Q92769; -.
DR PRIDE; Q92769; -.
DR ProteomicsDB; 3614; -.
DR ProteomicsDB; 75454; -. [Q92769-1]
DR Antibodypedia; 1842; 1028 antibodies from 48 providers.
DR DNASU; 3066; -.
DR Ensembl; ENST00000368632.6; ENSP00000357621.2; ENSG00000196591.12. [Q92769-3]
DR Ensembl; ENST00000519065.6; ENSP00000430432.1; ENSG00000196591.12. [Q92769-1]
DR Ensembl; ENST00000519108.5; ENSP00000430008.1; ENSG00000196591.12. [Q92769-3]
DR GeneID; 3066; -.
DR KEGG; hsa:3066; -.
DR MANE-Select; ENST00000519065.6; ENSP00000430432.1; NM_001527.4; NP_001518.3.
DR UCSC; uc003pwc.3; human. [Q92769-1]
DR CTD; 3066; -.
DR DisGeNET; 3066; -.
DR GeneCards; HDAC2; -.
DR HGNC; HGNC:4853; HDAC2.
DR HPA; ENSG00000196591; Low tissue specificity.
DR MIM; 605164; gene.
DR neXtProt; NX_Q92769; -.
DR OpenTargets; ENSG00000196591; -.
DR PharmGKB; PA29227; -.
DR VEuPathDB; HostDB:ENSG00000196591; -.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000155725; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; Q92769; -.
DR OMA; EIPMNEY; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; Q92769; -.
DR TreeFam; TF106171; -.
DR BRENDA; 3.5.1.98; 2681.
DR PathwayCommons; Q92769; -.
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-350054; Notch-HLH transcription pathway.
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-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SABIO-RK; Q92769; -.
DR SignaLink; Q92769; -.
DR SIGNOR; Q92769; -.
DR BioGRID-ORCS; 3066; 40 hits in 1107 CRISPR screens.
DR ChiTaRS; HDAC2; human.
DR EvolutionaryTrace; Q92769; -.
DR GeneWiki; Histone_deacetylase_2; -.
DR GenomeRNAi; 3066; -.
DR Pharos; Q92769; Tclin.
DR PRO; PR:Q92769; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q92769; protein.
DR Bgee; ENSG00000196591; Expressed in ganglionic eminence and 205 other tissues.
DR ExpressionAtlas; Q92769; baseline and differential.
DR Genevisible; Q92769; HS.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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: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:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0160009; F:histone decrotonylase activity; IDA:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0160010; F:protein de-2-hydroxyisobutyrylase activity; IDA:UniProtKB.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IMP:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
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; IDA:ComplexPortal.
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:0070828; P:heterochromatin organization; IMP:BHF-UCL.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
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:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
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:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population 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:1902437; P:positive regulation of male mating behavior; 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:2000273; P:positive regulation of signaling receptor activity; IMP:BHF-UCL.
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; 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:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.40.800.20; -; 1.
DR IDEAL; IID00488; -.
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 3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW Chromatin regulator; Cytoplasm; Hydrolase; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; S-nitrosylation;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..488
FT /note="Histone deacetylase 2"
FT /id="PRO_0000114693"
FT REGION 9..322
FT /note="Histone deacetylase"
FT REGION 389..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT MOD_RES 75
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT MOD_RES 262
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P70288"
FT MOD_RES 274
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P70288"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056175"
FT VARIANT 230
FT /note="R -> C (in dbSNP:rs1042903)"
FT /evidence="ECO:0000269|PubMed:8917507"
FT /id="VAR_025311"
FT VARIANT 315
FT /note="Y -> H (in dbSNP:rs17852888)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025312"
FT CONFLICT 93..94
FT /note="QR -> HI (in Ref. 1; AAC50814)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="V -> A (in Ref. 1; AAC50814)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="S -> Y (in Ref. 1; AAC50814)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="K -> M (in Ref. 2; BAG59420)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="G -> D (in Ref. 2; BAG59420)"
FT /evidence="ECO:0000305"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:7KBG"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:7KBG"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 107..126
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6WHQ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6WBZ"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:7KBG"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:7KBG"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 192..201
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 235..253
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 306..321
FT /evidence="ECO:0007829|PDB:7KBG"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:7KBG"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:7KBG"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6WBW"
FT HELIX 357..371
FT /evidence="ECO:0007829|PDB:7KBG"
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
