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Histone deacetylase 2 (HD2) (EC 3.5.1.98) (YY1 transcription factor-binding protein)

 HDAC2_MOUSE             Reviewed;         488 AA.
P70288; B2RRP3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 176.
RecName: Full=Histone deacetylase 2;
Short=HD2;
EC=3.5.1.98;
AltName: Full=YY1 transcription factor-binding protein;
Name=Hdac2; Synonyms=Yy1bp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphoma;
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 GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
INTERACTION WITH SAP30.
PubMed=9702189; DOI=10.1016/S1097-2765(00)80111-2;
Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K.,
Rosenfeld M.G., Ayer D.E., Eisenman R.N.;
"SAP30, a component of the mSin3 corepressor complex involved in N-
CoR-mediated repression by specific transcription factors.";
Mol. Cell 2:33-42(1998).
[5]
INTERACTION WITH HDAC7.
PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
"Identification of a nuclear domain with deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
[6]
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).
[7]
INTERACTION WITH SUV39H1.
PubMed=11788710; DOI=10.1093/nar/30.2.475;
Vaute O., Nicolas E., Vandel L., Trouche D.;
"Functional and physical interaction between the histone methyl
transferase Suv39H1 and histone deacetylases.";
Nucleic Acids Res. 30:475-481(2002).
[8]
INTERACTION WITH SETDB1.
PubMed=12398767; DOI=10.1042/BJ20020854;
Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
"An ERG (ets-related gene)-associated histone methyltransferase
interacts with histone deacetylases 1/2 and transcription co-
repressors mSin3A/B.";
Biochem. J. 369:651-657(2003).
[9]
FUNCTION IN CIRCADIAN CLOCK, AND INTERACTION WITH CRY1.
PubMed=15226430; DOI=10.1128/MCB.24.14.6278-6287.2004;
Naruse Y., Oh-hashi K., Iijima N., Naruse M., Yoshioka H., Tanaka M.;
"Circadian and light-induced transcription of clock gene Per1 depends
on histone acetylation and deacetylation.";
Mol. Cell. Biol. 24:6278-6287(2004).
[10]
INTERACTION WITH H2AFY.
PubMed=16107708; DOI=10.1128/MCB.25.17.7616-7624.2005;
Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y.,
Pehrson J.R., Khochbin S., Luger K.;
"Structural characterization of the histone variant macroH2A.";
Mol. Cell. Biol. 25:7616-7624(2005).
[11]
INTERACTION WITH PRDM6.
PubMed=16537907; DOI=10.1128/MCB.26.7.2626-2636.2006;
Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G.,
Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.;
"PRISM/PRDM6, a transcriptional repressor that promotes the
proliferative gene program in smooth muscle cells.";
Mol. Cell. Biol. 26:2626-2636(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY AS A COMPONENT OF A
GFI-RCOR-KDM1A-HDAC COMPLEX, INTERACTION WITH GFI1 AND GFI1B, AND
FUNCTION.
PubMed=17707228; DOI=10.1016/j.molcel.2007.06.039;
Saleque S., Kim J., Rooke H.M., Orkin S.H.;
"Epigenetic regulation of hematopoietic differentiation by Gfi-1 and
Gfi-1b is mediated by the cofactors CoREST and LSD1.";
Mol. Cell 27:562-572(2007).
[13]
INTERACTION WITH SIX3.
PubMed=17666527; DOI=10.1073/pnas.0705878104;
Manavathi B., Peng S., Rayala S.K., Talukder A.H., Wang M.H.,
Wang R.A., Balasenthil S., Agarwal N., Frishman L.J., Kumar R.;
"Repression of Six3 by a corepressor regulates rhodopsin expression.";
Proc. Natl. Acad. Sci. U.S.A. 104:13128-13133(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-422, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[15]
S-NITROSYLATION AT CYS-262 AND CYS-274, AND MUTAGENESIS OF CYS-152;
CYS-262 AND CYS-274.
PubMed=18754010; DOI=10.1038/nature07238;
Nott A., Watson P.M., Robinson J.D., Crepaldi L., Riccio A.;
"S-Nitrosylation of histone deacetylase 2 induces chromatin
remodelling in neurons.";
Nature 455:411-415(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-422, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
FUNCTION.
PubMed=20071335; DOI=10.1074/jbc.M109.079095;
Li D.Q., Pakala S.B., Reddy S.D., Ohshiro K., Peng S.H., Lian Y.,
Fu S.W., Kumar R.;
"Revelation of p53-independent function of MTA1 in DNA damage response
via modulation of the p21 WAF1-proliferating cell nuclear antigen
pathway.";
J. Biol. Chem. 285:10044-10052(2010).
[20]
CAUTION.
PubMed=20519513; DOI=10.1074/jbc.M110.139469;
Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S.,
Rayala S.K., Behringer R.R., Kumar R.;
"Regulation of NF-kappaB circuitry by a component of the nucleosome
remodeling and deacetylase complex controls inflammatory response
homeostasis.";
J. Biol. Chem. 285:23590-23597(2010).
[21]
CAUTION, AND RETRACTION.
PubMed=28314777; DOI=10.1074/jbc.A117.139469;
Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S.,
Rayala S.K., Behringer R.R., Kumar R.;
"Regulation of NF-kappaB circuitry by a component of the nucleosome
remodeling and deacetylase complex controls inflammatory response
homeostasis.";
J. Biol. Chem. 292:4764-4764(2017).
[22]
S-NITROSYLATION BY GAPDH.
PubMed=20972425; DOI=10.1038/ncb2114;
Kornberg M.D., Sen N., Hara M.R., Juluri K.R., Nguyen J.V.,
Snowman A.M., Law L., Hester L.D., Snyder S.H.;
"GAPDH mediates nitrosylation of nuclear proteins.";
Nat. Cell Biol. 12:1094-1100(2010).
[23]
INTERACTION WITH ZNF431.
PubMed=21177534; DOI=10.1074/jbc.M110.178780;
He Z., Cai J., Lim J.W., Kroll K., Ma L.;
"A novel KRAB domain-containing zinc finger transcription factor
ZNF431 directly represses Patched1 transcription.";
J. Biol. Chem. 286:7279-7289(2011).
[24]
INTERACTION WITH ZNF431.
PubMed=22391310; DOI=10.1016/B978-0-12-394622-5.00014-6;
Huang G.J., He Z., Ma L.;
"ZFP932 suppresses cellular Hedgehog response and Patched1
transcription.";
Vitam. Horm. 88:309-332(2012).
[25]
INTERACTION WITH INSM1.
PubMed=24227653; DOI=10.1242/dev.097642;
Welcker J.E., Hernandez-Miranda L.R., Paul F.E., Jia S., Ivanov A.,
Selbach M., Birchmeier C.;
"Insm1 controls development of pituitary endocrine cells and requires
a SNAG domain for function and for recruitment of histone-modifying
factors.";
Development 140:4947-4958(2013).
-!- 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 (By similarity).
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:0000250, ECO:0000269|PubMed:15226430,
ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:20071335}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Interacts with SNW1, PELP1, ATR, DNMT1, MINT, HDAC10,
HCFC1, NRIP1, KDM4A, CHFR and SAP30L. 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. 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. 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.
Component of a mSin3A corepressor complex that contains SIN3A,
SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CBFA2T3,
HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY
(via the non-histone region). Component of a RCOR/GFI/KDM1A/HDAC
complex. Interacts directly with GFI1 and GFI1B. 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 (By similarity).
Interacts with MTA1, with a preference for sumoylated MTA1.
Interacts with SIX3. Interacts with BEND3 (By similarity).
Component of a histone deacetylase complex containing DNTTIP1,
ZNF541, HDAC1 and HDAC2 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q92769, ECO:0000269|PubMed:10984530,
ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11788710,
ECO:0000269|PubMed:12398767, ECO:0000269|PubMed:15226430,
ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16537907,
ECO:0000269|PubMed:17666527, ECO:0000269|PubMed:17707228,
ECO:0000269|PubMed:20519513, ECO:0000269|PubMed:21177534,
ECO:0000269|PubMed:22391310, ECO:0000269|PubMed:24227653,
ECO:0000269|PubMed:9702189}.
-!- INTERACTION:
Q6ZQ88:Kdm1a; NbExp=4; IntAct=EBI-302251, EBI-1216284;
Q9R190:Mta2; NbExp=7; IntAct=EBI-302251, EBI-904134;
P11103:Parp1; NbExp=3; IntAct=EBI-302251, EBI-642213;
Q8C796:Rcor2; NbExp=2; IntAct=EBI-302251, EBI-3043949;
Q60520:Sin3a; NbExp=7; IntAct=EBI-302251, EBI-349034;
Q62233:Six3; NbExp=2; IntAct=EBI-302251, EBI-2297327;
Q3TKT4:Smarca4; NbExp=4; IntAct=EBI-302251, EBI-1210244;
E9QAG8:Znf431; NbExp=3; IntAct=EBI-302251, EBI-9549639;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
-!- 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:0000269|PubMed:18754010,
ECO:0000269|PubMed:20519513, ECO:0000269|PubMed:20972425}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
-!- CAUTION: Was originally thought to be S-nitrosylated and to
interact with MTA1 (PubMed:20519513). However, this work was later
retracted (PubMed:28314777). Nevertheless, other publications
demonstrate that it is S-nitrosylated and there are several
publications in the human ortholog demonstrating its interaction
with MTA1 (PubMed:18754010, PubMed:20972425).
{ECO:0000269|PubMed:18754010, ECO:0000269|PubMed:20519513,
ECO:0000269|PubMed:20972425, ECO:0000305|PubMed:28314777}.
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EMBL; U31758; AAC52889.1; -; mRNA.
EMBL; CH466540; EDL04897.1; -; Genomic_DNA.
EMBL; BC138517; AAI38518.1; -; mRNA.
CCDS; CCDS23783.1; -.
RefSeq; NP_032255.2; NM_008229.2.
UniGene; Mm.19806; -.
ProteinModelPortal; P70288; -.
SMR; P70288; -.
BioGrid; 200260; 52.
CORUM; P70288; -.
DIP; DIP-32854N; -.
IntAct; P70288; 35.
MINT; MINT-146936; -.
STRING; 10090.ENSMUSP00000019911; -.
ChEMBL; CHEMBL3832944; -.
iPTMnet; P70288; -.
PhosphoSitePlus; P70288; -.
EPD; P70288; -.
MaxQB; P70288; -.
PaxDb; P70288; -.
PeptideAtlas; P70288; -.
PRIDE; P70288; -.
GeneID; 15182; -.
KEGG; mmu:15182; -.
UCSC; uc007evf.1; mouse.
CTD; 3066; -.
MGI; MGI:1097691; Hdac2.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
HOGENOM; HOG000225180; -.
HOVERGEN; HBG057112; -.
InParanoid; P70288; -.
KO; K06067; -.
PhylomeDB; P70288; -.
TreeFam; TF106171; -.
BRENDA; 3.5.1.98; 3474.
Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-573389; NoRC negatively regulates rRNA expression.
ChiTaRS; Hdac2; mouse.
PRO; PR:P70288; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_HDAC2; -.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016581; C:NuRD complex; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005657; C:replication fork; IDA:MGI.
GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
GO; GO:0016580; C:Sin3 complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IPI:MGI.
GO; GO:0017053; C:transcriptional repressor complex; IPI:MGI.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB.
GO; GO:0034739; F:histone deacetylase activity (H4-K16 specific); IMP:CACAO.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0035851; F:Krueppel-associated box domain 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; ISO:MGI.
GO; GO:0033558; F:protein deacetylase activity; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISO:MGI.
GO; GO:0001226; F:RNA polymerase II transcription corepressor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISO:MGI.
GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
GO; GO:0035984; P:cellular response to trichostatin A; IDA:MGI.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
GO; GO:0016358; P:dendrite development; IMP:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; IGI:BHF-UCL.
GO; GO:0009913; P:epidermal cell differentiation; IGI:BHF-UCL.
GO; GO:0061029; P:eyelid development in camera-type eye; IGI:BHF-UCL.
GO; GO:0061198; P:fungiform papilla formation; IGI:BHF-UCL.
GO; GO:0060789; P:hair follicle placode formation; IGI:BHF-UCL.
GO; GO:0021766; P:hippocampus development; IGI:MGI.
GO; GO:0016575; P:histone deacetylation; IGI:MGI.
GO; GO:0070932; P:histone H3 deacetylation; IDA:UniProtKB.
GO; GO:0070734; P:histone H3-K27 methylation; IMP:MGI.
GO; GO:0070933; P:histone H4 deacetylation; IDA:UniProtKB.
GO; GO:0006344; P:maintenance of chromatin silencing; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:BHF-UCL.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IGI:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:BHF-UCL.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0030182; P:neuron differentiation; IGI:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:BHF-UCL.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IGI:MGI.
GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; ISO:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0006476; P:protein deacetylation; IDA:BHF-UCL.
GO; GO:0090311; P:regulation of protein deacetylation; IGI:MGI.
GO; GO:0051896; P:regulation of protein kinase B signaling; IMP:MGI.
GO; GO:0060297; P:regulation of sarcomere organization; IMP:MGI.
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_domain.
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;
Acetylation; Biological rhythms; Chromatin regulator;
Complete proteome; Cytoplasm; Hydrolase; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repressor; S-nitrosylation;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 488 Histone deacetylase 2.
/FTId=PRO_0000114694.
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:0000269|PubMed:18754010}.
MOD_RES 274 274 S-nitrosocysteine.
{ECO:0000269|PubMed:18754010}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000250|UniProtKB:Q92769}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
CROSSLNK 75 75 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q92769}.
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:0000250|UniProtKB:Q92769}.
CROSSLNK 458 458 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 462 462 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 478 478 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92769}.
CROSSLNK 481 481 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13547}.
MUTAGEN 152 152 C->A: Does not affect S-nitrosylation.
{ECO:0000269|PubMed:18754010}.
MUTAGEN 262 262 C->A: Impairs S-nitrosylation. Abolishes
S-nitrosylation; when associated with A-
274. {ECO:0000269|PubMed:18754010}.
MUTAGEN 274 274 C->A: Impairs S-nitrosylation. Abolishes
S-nitrosylation; when associated with A-
262. {ECO:0000269|PubMed:18754010}.
CONFLICT 289 289 A -> V (in Ref. 2; EDL04897).
{ECO:0000305}.
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


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