ID HDAC2_MOUSE Reviewed; 488 AA.
AC P70288; B2RRP3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 220.
DE RecName: Full=Histone deacetylase 2 {ECO:0000305};
DE Short=HD2;
DE EC=3.5.1.98 {ECO:0000269|PubMed:18754010, ECO:0000305|PubMed:30279482};
DE AltName: Full=Protein deacylase HDAC2 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000269|PubMed:30279482};
DE AltName: Full=YY1 transcription factor-binding protein;
GN Name=Hdac2 {ECO:0000312|MGI:MGI:1097691}; Synonyms=Yy1bp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP INTERACTION WITH SAP30.
RX PubMed=9702189; DOI=10.1016/s1097-2765(00)80111-2;
RA Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G.,
RA Ayer D.E., Eisenman R.N.;
RT "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-
RT mediated repression by specific transcription factors.";
RL Mol. Cell 2:33-42(1998).
RN [5]
RP INTERACTION WITH HDAC7.
RX PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT "Identification of a nuclear domain with deacetylase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN [6]
RP INTERACTION WITH 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 [7]
RP INTERACTION WITH SUV39H1.
RX PubMed=11788710; DOI=10.1093/nar/30.2.475;
RA Vaute O., Nicolas E., Vandel L., Trouche D.;
RT "Functional and physical interaction between the histone methyl transferase
RT Suv39H1 and histone deacetylases.";
RL Nucleic Acids Res. 30:475-481(2002).
RN [8]
RP INTERACTION WITH SETDB1.
RX PubMed=12398767; DOI=10.1042/bj20020854;
RA Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
RA Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
RT "An ERG (ets-related gene)-associated histone methyltransferase interacts
RT with histone deacetylases 1/2 and transcription co-repressors mSin3A/B.";
RL Biochem. J. 369:651-657(2003).
RN [9]
RP FUNCTION IN CIRCADIAN CLOCK, AND INTERACTION WITH CRY1.
RX PubMed=15226430; DOI=10.1128/mcb.24.14.6278-6287.2004;
RA Naruse Y., Oh-hashi K., Iijima N., Naruse M., Yoshioka H., Tanaka M.;
RT "Circadian and light-induced transcription of clock gene Per1 depends on
RT histone acetylation and deacetylation.";
RL Mol. Cell. Biol. 24:6278-6287(2004).
RN [10]
RP INTERACTION WITH MACROH2A1.
RX PubMed=16107708; DOI=10.1128/mcb.25.17.7616-7624.2005;
RA Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R.,
RA Khochbin S., Luger K.;
RT "Structural characterization of the histone variant macroH2A.";
RL Mol. Cell. Biol. 25:7616-7624(2005).
RN [11]
RP INTERACTION WITH PRDM6.
RX PubMed=16537907; DOI=10.1128/mcb.26.7.2626-2636.2006;
RA Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G.,
RA Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.;
RT "PRISM/PRDM6, a transcriptional repressor that promotes the proliferative
RT gene program in smooth muscle cells.";
RL Mol. Cell. Biol. 26:2626-2636(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY AS A COMPONENT OF A GFI-RCOR-KDM1A-HDAC
RP COMPLEX, INTERACTION WITH GFI1 AND GFI1B, AND FUNCTION.
RX PubMed=17707228; DOI=10.1016/j.molcel.2007.06.039;
RA Saleque S., Kim J., Rooke H.M., Orkin S.H.;
RT "Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b
RT is mediated by the cofactors CoREST and LSD1.";
RL Mol. Cell 27:562-572(2007).
RN [13]
RP INTERACTION WITH SIX3.
RX PubMed=17666527; DOI=10.1073/pnas.0705878104;
RA Manavathi B., Peng S., Rayala S.K., Talukder A.H., Wang M.H., Wang R.A.,
RA Balasenthil S., Agarwal N., Frishman L.J., Kumar R.;
RT "Repression of Six3 by a corepressor regulates rhodopsin expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13128-13133(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [15]
RP S-NITROSYLATION AT CYS-262 AND CYS-274, FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF CYS-152; CYS-262 AND CYS-274.
RX PubMed=18754010; DOI=10.1038/nature07238;
RA Nott A., Watson P.M., Robinson J.D., Crepaldi L., Riccio A.;
RT "S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in
RT neurons.";
RL Nature 455:411-415(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [19]
RP FUNCTION.
RX PubMed=20071335; DOI=10.1074/jbc.m109.079095;
RA Li D.Q., Pakala S.B., Reddy S.D., Ohshiro K., Peng S.H., Lian Y., Fu S.W.,
RA Kumar R.;
RT "Revelation of p53-independent function of MTA1 in DNA damage response via
RT modulation of the p21 WAF1-proliferating cell nuclear antigen pathway.";
RL J. Biol. Chem. 285:10044-10052(2010).
RN [20]
RP RETRACTED PAPER.
RX PubMed=20519513; DOI=10.1074/jbc.m110.139469;
RA Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S., Rayala S.K.,
RA Behringer R.R., Kumar R.;
RT "Regulation of NF-kappaB circuitry by a component of the nucleosome
RT remodeling and deacetylase complex controls inflammatory response
RT homeostasis.";
RL J. Biol. Chem. 285:23590-23597(2010).
RN [21]
RP CAUTION, AND RETRACTION NOTICE OF PUBMED:20519513.
RX PubMed=28314777; DOI=10.1074/jbc.a117.139469;
RA Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S., Rayala S.K.,
RA Behringer R.R., Kumar R.;
RL J. Biol. Chem. 292:4764-4764(2017).
RN [22]
RP S-NITROSYLATION BY GAPDH.
RX PubMed=20972425; DOI=10.1038/ncb2114;
RA Kornberg M.D., Sen N., Hara M.R., Juluri K.R., Nguyen J.V., Snowman A.M.,
RA Law L., Hester L.D., Snyder S.H.;
RT "GAPDH mediates nitrosylation of nuclear proteins.";
RL Nat. Cell Biol. 12:1094-1100(2010).
RN [23]
RP INTERACTION WITH ZNF431.
RX PubMed=21177534; DOI=10.1074/jbc.m110.178780;
RA He Z., Cai J., Lim J.W., Kroll K., Ma L.;
RT "A novel KRAB domain-containing zinc finger transcription factor ZNF431
RT directly represses Patched1 transcription.";
RL J. Biol. Chem. 286:7279-7289(2011).
RN [24]
RP INTERACTION WITH ZNF431.
RX PubMed=22391310; DOI=10.1016/b978-0-12-394622-5.00014-6;
RA Huang G.J., He Z., Ma L.;
RT "ZFP932 suppresses cellular Hedgehog response and Patched1 transcription.";
RL Vitam. Horm. 88:309-332(2012).
RN [25]
RP INTERACTION WITH INSM1.
RX PubMed=24227653; DOI=10.1242/dev.097642;
RA Welcker J.E., Hernandez-Miranda L.R., Paul F.E., Jia S., Ivanov A.,
RA Selbach M., Birchmeier C.;
RT "Insm1 controls development of pituitary endocrine cells and requires a
RT SNAG domain for function and for recruitment of histone-modifying
RT factors.";
RL Development 140:4947-4958(2013).
RN [26]
RP IDENTIFICATION IN THE NURD COMPLEX, INTERACTION WITH CHD4 AND CHD5, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27806305; DOI=10.1016/j.celrep.2016.10.022;
RA Nitarska J., Smith J.G., Sherlock W.T., Hillege M.M., Nott A.,
RA Barshop W.D., Vashisht A.A., Wohlschlegel J.A., Mitter R., Riccio A.;
RT "A Functional Switch of NuRD Chromatin Remodeling Complex Subunits
RT Regulates Mouse Cortical Development.";
RL Cell Rep. 17:1683-1698(2016).
RN [27]
RP INTERACTION WITH PWWP2B.
RX PubMed=34180153; DOI=10.1002/advs.202102060;
RA Yan L., Jin W., Zhao Q., Cui X., Shi T., Xu Y., Li F., Jin W., Zhang Z.,
RA Zhang Z., Tang Q.Q., Pan D.;
RT "PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD
RT Subcomplex.";
RL Adv. Sci. 8:e2102060-e2102060(2021).
RN [28]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30279482; DOI=10.1038/s41598-018-32927-9;
RA Kelly R.D.W., Chandru A., Watson P.J., Song Y., Blades M., Robertson N.S.,
RA Jamieson A.G., Schwabe J.W.R., Cowley S.M.;
RT "Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone
RT acetylation and crotonylation in vivo.";
RL Sci. Rep. 8:14690-14690(2018).
RN [29]
RP IDENTIFICATION IN A COMPLEX WITH HDAC1; KCTD19; DNTTIP1 AND ZNF541.
RX PubMed=34075040; DOI=10.1038/s41467-021-23378-4;
RA Horisawa-Takada Y., Kodera C., Takemoto K., Sakashita A., Horisawa K.,
RA Maeda R., Shimada R., Usuki S., Fujimura S., Tani N., Matsuura K.,
RA Akiyama T., Suzuki A., Niwa H., Tachibana M., Ohba T., Katabuchi H.,
RA Namekawa S.H., Araki K., Ishiguro K.I.;
RT "Meiosis-specific ZFP541 repressor complex promotes developmental
RT progression of meiotic prophase towards completion during mouse
RT spermatogenesis.";
RL Nat. Commun. 12:3184-3184(2021).
RN [30]
RP IDENTIFICATION IN A COMPLEX WITH HDAC1; KCTD19; DNTTIP1 AND ZNF541.
RX PubMed=35341968; DOI=10.1016/j.jgg.2022.03.005;
RA Li Y., Meng R., Li S., Gu B., Xu X., Zhang H., Tan X., Shao T., Wang J.,
RA Xu D., Wang F.;
RT "The ZFP541-KCTD19 complex is essential for pachytene progression by
RT activating meiotic genes during mouse spermatogenesis.";
RL J. Genet. Genomics 49:1029-1041(2022).
CC -!- FUNCTION: Histone deacetylase that catalyzes the deacetylation of
CC lysine residues on the N-terminal part of the core histones (H2A, H2B,
CC H3 and H4) (PubMed:18754010). Histone deacetylation gives a tag for
CC epigenetic repression and plays an important role in transcriptional
CC regulation, cell cycle progression and developmental events
CC (PubMed:18754010). Histone deacetylases act via the formation of large
CC multiprotein complexes (PubMed:18754010). Forms transcriptional
CC repressor complexes by associating with MAD, SIN3, YY1 and N-COR (By
CC similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that
CC suppresses, via histone deacetylase (HDAC) recruitment, a number of
CC genes implicated in multilineage blood cell development
CC (PubMed:17707228). Acts as a component of the histone deacetylase NuRD
CC complex which participates in the remodeling of chromatin (By
CC similarity). Component of the SIN3B complex that represses
CC transcription and counteracts the histone acetyltransferase activity of
CC EP300 through the recognition H3K27ac marks by PHF12 and the activity
CC of the histone deacetylase HDAC2 (By similarity). Also deacetylates
CC non-histone targets: deacetylates TSHZ3, thereby regulating its
CC transcriptional repressor activity (By similarity). May be involved in
CC the transcriptional repression of circadian target genes, such as PER1,
CC mediated by CRY1 through histone deacetylation (PubMed:15226430).
CC Involved in MTA1-mediated transcriptional corepression of TFF1 and
CC CDKN1A (PubMed:20071335). In addition to protein deacetylase activity,
CC also acts as a protein-lysine deacylase by recognizing other acyl
CC groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2-
CC hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine
CC residues, leading to protein decrotonylation and de-2-
CC hydroxyisobutyrylation, respectively (PubMed:30279482).
CC {ECO:0000250|UniProtKB:Q92769, ECO:0000269|PubMed:15226430,
CC ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:18754010,
CC ECO:0000269|PubMed:20071335, ECO:0000269|PubMed:30279482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000269|PubMed:18754010, ECO:0000305|PubMed:30279482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000269|PubMed:18754010, ECO:0000305|PubMed:30279482};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q92769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000250|UniProtKB:Q92769};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate
CC + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC Evidence={ECO:0000269|PubMed:30279482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000269|PubMed:30279482};
CC -!- 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:0000250|UniProtKB:Q92769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69177;
CC Evidence={ECO:0000250|UniProtKB:Q92769};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q92769};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q92769};
CC Note=Binds 2 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:Q92769};
CC -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex composed
CC of HDAC1, HDAC2, RBBP4 and RBBP7, the core complex associates with
CC SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex (By similarity).
CC Component of the nucleosome remodeling and deacetylase (NuRD) repressor
CC complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4, RBBP7,
CC HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins CDK2AP1,
CC CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5 (PubMed:27806305). The
CC exact stoichiometry of the NuRD complex is unknown, and some subunits
CC such as MBD2 and MBD3, GATAD2A and GATAD2B, and CHD3, CHD4 and CHD5
CC define mutually exclusive NuRD complexes (PubMed:27806305). Component
CC of a RCOR/GFI/KDM1A/HDAC complex (PubMed:17707228). Component of a BHC
CC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A,
CC RCOR1 and PHF21A (By similarity). The BHC complex may also contain
CC ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I (By similarity). Part of a complex
CC containing the core histones H2A, H2B, H3 and H4, DEK and
CC unphosphorylated DAXX (By similarity). Part of a complex containing ATR
CC and CHD4 (By similarity). Forms a heterologous complex at least with
CC YY1 (By similarity). Interacts in the late S-phase of DNA-replication
CC with DNMT1 in the other transcriptional repressor complex composed of
CC DNMT1, DMAP1, PCNA, CAF1 (By similarity). Component of a mSin3A
CC corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1
CC and HDAC2 (By similarity). Part of a complex composed of TRIM28, HDAC1,
CC HDAC2 and EHMT2 (By similarity). Part of a complex containing at least
CC CDYL, MIER1, MIER2, HDAC1 and HDAC2 (By similarity). Component of a
CC histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2
CC (By similarity). Forms a complex comprising APPL1, RUVBL2, APPL2,
CC CTNNB1 and HDAC1 (By similarity). Interacts directly with GFI1 (By
CC similarity). Interacts directly with GFI1B (By similarity). Interacts
CC with APEX1; the interaction is not dependent on the acetylated status
CC of APEX1 (By similarity). Interacts with ATR (By similarity). Interacts
CC with BCL6 (non-acetylated form) (By similarity). Interacts with BEND3
CC (By similarity). Interacts with CBFA2T3 (PubMed:11533236). Interacts
CC with CDK2AP1 (By similarity). Interacts with CHD4 (PubMed:27806305).
CC Interacts with CHD5 (PubMed:27806305). Interacts with CHFR (By
CC similarity). Interacts with CRY1 (PubMed:15226430). Interacts with
CC DNMT1 (By similarity). Interacts with GATAD2A (By similarity).
CC Interacts with HCFC1 (By similarity). Interacts with HDAC7
CC (PubMed:10984530). Interacts with HDAC10 (By similarity). Interacts
CC with INSM1 (PubMed:24227653). Interacts with KDM4A (By similarity).
CC Interacts with MACROH2A1 (via the non-histone region)
CC (PubMed:16107708). Interacts with MBD3L2 (By similarity). Interacts
CC with MTA1, with a preference for sumoylated MTA1 (By similarity).
CC Interacts with NACC2 (By similarity). Interacts with NRIP1 (By
CC similarity). Interacts with PELP1 (By similarity). Interacts with
CC PIMREG (By similarity). Interacts with PRDM6 (PubMed:16537907).
CC Interacts with PWWP2B (PubMed:34180153) Interacts with SAP30
CC (PubMed:9702189). Interacts with SAP30L (By similarity). Interacts with
CC SETDB1 (PubMed:12398767). Interacts with SIX3 (PubMed:17666527).
CC Interacts with SMARCAD1 (By similarity). Interacts with SNW1 (By
CC similarity). Interacts with SPHK2 (By similarity). Interacts with
CC SPEN/MINT (By similarity). Interacts (CK2 phosphorylated form) with SP3
CC (By similarity). Interacts with SUV39H1 (PubMed:11788710). Interacts
CC with TSHZ3 (via its N-terminus) (By similarity). Interacts with ZMYND8
CC (By similarity). Interacts with ZNF431 (PubMed:21177534,
CC PubMed:22391310). Interacts with ZNF263; recruited to the SIX3 promoter
CC along with other proteins involved in chromatin modification and
CC transcriptional corepression where it contributes to transcriptional
CC repression (By similarity). Identified in a complex with HDAC1, KCTD19,
CC DNTTIP1 and ZNF541 (PubMed:34075040, PubMed:35341968). Component of the
CC SIN3B complex, which includes SIN3B, HDAC2, PHF12 and MORF4L1;
CC interacts directly with all subunits (By similarity).
CC {ECO:0000250|UniProtKB:Q92769, ECO:0000269|PubMed:10984530,
CC ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11788710,
CC ECO:0000269|PubMed:12398767, ECO:0000269|PubMed:15226430,
CC ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16537907,
CC ECO:0000269|PubMed:17666527, ECO:0000269|PubMed:17707228,
CC ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310,
CC ECO:0000269|PubMed:24227653, ECO:0000269|PubMed:27806305,
CC ECO:0000269|PubMed:34075040, ECO:0000269|PubMed:34180153,
CC ECO:0000269|PubMed:35341968, ECO:0000269|PubMed:9702189}.
CC -!- INTERACTION:
CC P70288; Q6ZQ88: Kdm1a; NbExp=4; IntAct=EBI-302251, EBI-1216284;
CC P70288; Q9R190: Mta2; NbExp=7; IntAct=EBI-302251, EBI-904134;
CC P70288; P11103: Parp1; NbExp=3; IntAct=EBI-302251, EBI-642213;
CC P70288; Q8C796: Rcor2; NbExp=2; IntAct=EBI-302251, EBI-3043949;
CC P70288; Q60520: Sin3a; NbExp=7; IntAct=EBI-302251, EBI-349034;
CC P70288; Q62233: Six3; NbExp=2; IntAct=EBI-302251, EBI-2297327;
CC P70288; Q3TKT4: Smarca4; NbExp=4; IntAct=EBI-302251, EBI-1210244;
CC P70288; E9QAG8: Znf431; NbExp=3; IntAct=EBI-302251, EBI-9549639;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92769}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q92769}.
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:0000269|PubMed:18754010,
CC ECO:0000269|PubMed:20519513, ECO:0000269|PubMed:20972425}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be S-nitrosylated and to interact
CC with MTA1 (PubMed:20519513). However, this work was later retracted
CC (PubMed:28314777). Nevertheless, other publications demonstrate that it
CC is S-nitrosylated and there are several publications in the human
CC ortholog demonstrating its interaction with MTA1 (PubMed:18754010,
CC PubMed:20972425). {ECO:0000269|PubMed:18754010,
CC ECO:0000269|PubMed:20519513, ECO:0000269|PubMed:20972425,
CC ECO:0000305|PubMed:28314777}.
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DR EMBL; U31758; AAC52889.1; -; mRNA.
DR EMBL; CH466540; EDL04897.1; -; Genomic_DNA.
DR EMBL; BC138517; AAI38518.1; -; mRNA.
DR CCDS; CCDS23783.1; -.
DR RefSeq; NP_032255.2; NM_008229.2.
DR AlphaFoldDB; P70288; -.
DR SMR; P70288; -.
DR BioGRID; 200260; 68.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; P70288; -.
DR DIP; DIP-32854N; -.
DR IntAct; P70288; 41.
DR MINT; P70288; -.
DR STRING; 10090.ENSMUSP00000019911; -.
DR BindingDB; P70288; -.
DR ChEMBL; CHEMBL3832944; -.
DR ChEMBL; CHEMBL3883302; -.
DR ChEMBL; CHEMBL4523989; -.
DR GlyGen; P70288; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P70288; -.
DR PhosphoSitePlus; P70288; -.
DR EPD; P70288; -.
DR jPOST; P70288; -.
DR MaxQB; P70288; -.
DR PaxDb; 10090-ENSMUSP00000019911; -.
DR PeptideAtlas; P70288; -.
DR ProteomicsDB; 269728; -.
DR Pumba; P70288; -.
DR DNASU; 15182; -.
DR GeneID; 15182; -.
DR KEGG; mmu:15182; -.
DR UCSC; uc007evf.1; mouse.
DR AGR; MGI:1097691; -.
DR CTD; 3066; -.
DR MGI; MGI:1097691; Hdac2.
DR eggNOG; KOG1342; Eukaryota.
DR InParanoid; P70288; -.
DR OrthoDB; 1327607at2759; -.
DR PhylomeDB; P70288; -.
DR TreeFam; TF106171; -.
DR BRENDA; 3.5.1.98; 3474.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-MMU-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 15182; 5 hits in 85 CRISPR screens.
DR ChiTaRS; Hdac2; mouse.
DR PRO; PR:P70288; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70288; Protein.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005657; C:replication fork; IDA:MGI.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
DR GO; GO:0070822; C:Sin3-type complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IPI:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0019213; F:deacetylase activity; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0160009; F:histone decrotonylase activity; IDA:UniProtKB.
DR GO; GO:0034739; F:histone H4K16 deacetylase activity; IMP:CACAO.
DR GO; GO:0035851; F:Krueppel-associated box domain binding; IPI:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
DR GO; GO:0160010; F:protein de-2-hydroxyisobutyrylase activity; ISS:UniProtKB.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IDA:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:BHF-UCL.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0035984; P:cellular response to trichostatin A; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IMP:UniProtKB.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IGI:BHF-UCL.
DR GO; GO:0009913; P:epidermal cell differentiation; IGI:BHF-UCL.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IGI:BHF-UCL.
DR GO; GO:0061198; P:fungiform papilla formation; IGI:BHF-UCL.
DR GO; GO:0060789; P:hair follicle placode formation; IGI:BHF-UCL.
DR GO; GO:0031507; P:heterochromatin formation; ISO:MGI.
DR GO; GO:0021766; P:hippocampus development; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:BHF-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IGI:MGI.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:BHF-UCL.
DR GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; ISO:MGI.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; NAS:ComplexPortal.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; NAS:ComplexPortal.
DR GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:BHF-UCL.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0032732; P:positive regulation of interleukin-1 production; ISO:MGI.
DR GO; GO:1902437; P:positive regulation of male mating behavior; ISO:MGI.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IGI:MGI.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0006476; P:protein deacetylation; IDA:BHF-UCL.
DR GO; GO:0036211; P:protein modification process; ISO:MGI.
DR GO; GO:0042659; P:regulation of cell fate specification; NAS:ComplexPortal.
DR GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:MGI.
DR GO; GO:0090311; P:regulation of protein deacetylation; IGI:MGI.
DR GO; GO:0060297; P:regulation of sarcomere organization; IMP:MGI.
DR GO; GO:2000736; P:regulation of stem cell differentiation; NAS:ComplexPortal.
DR CDD; cd10011; HDAC2; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF2; HISTONE DEACETYLASE 2; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 1: Evidence at protein level;
KW Acetylation; Biological rhythms; Calcium; Chromatin regulator; Cytoplasm;
KW Hydrolase; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; S-nitrosylation; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..488
FT /note="Histone deacetylase 2"
FT /id="PRO_0000114694"
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 BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
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:0000269|PubMed:18754010"
FT MOD_RES 274
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:18754010"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
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:0000250|UniProtKB:Q92769"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT MUTAGEN 152
FT /note="C->A: Does not affect S-nitrosylation."
FT /evidence="ECO:0000269|PubMed:18754010"
FT MUTAGEN 262
FT /note="C->A: Impairs S-nitrosylation. Abolishes S-
FT nitrosylation; when associated with A-274."
FT /evidence="ECO:0000269|PubMed:18754010"
FT MUTAGEN 274
FT /note="C->A: Impairs S-nitrosylation. Abolishes S-
FT nitrosylation; when associated with A-262."
FT /evidence="ECO:0000269|PubMed:18754010"
FT CONFLICT 289
FT /note="A -> V (in Ref. 2; EDL04897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 55302 MW; B9843D24A775157C 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 GHAKCVEVAK TFNLPLLMLG
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE
FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKTD VKEEDKSKDN SGEKTDPKGA
KSEQLSNP
//
