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Histone deacetylase 3 (HD3) (EC 3.5.1.98)

 HDAC3_MOUSE             Reviewed;         424 AA.
O88895; O88896;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
27-SEP-2017, entry version 148.
RecName: Full=Histone deacetylase 3;
Short=HD3;
EC=3.5.1.98;
Name=Hdac3;
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] (ISOFORMS LONG AND SHORT).
STRAIN=C3H/HeJ, and C57BL/6J;
PubMed=10491319; DOI=10.1006/bbrc.1999.1389;
Mahlknecht U., Hoelzer D., Bucala R., Verdin E.;
"Cloning and characterization of the murine histone deacetylase
(HDAC3).";
Biochem. Biophys. Res. Commun. 263:482-490(1999).
[2]
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).
[3]
INTERACTION WITH HDAC9.
PubMed=11022042; DOI=10.1074/jbc.M007364200;
Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.;
"Association of COOH-terminal-binding protein (CtBP) and MEF2-
interacting transcription repressor (MITR) contributes to
transcriptional repression of the MEF2 transcription factor.";
J. Biol. Chem. 276:35-39(2001).
[4]
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).
[5]
INTERACTION WITH DACH1.
PubMed=12130660; DOI=10.1126/science.1073263;
Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.;
"Tissue-specific regulation of retinal and pituitary precursor cell
proliferation.";
Science 297:1180-1183(2002).
[6]
INTERACTION WITH HDAC9.
PubMed=15711539; DOI=10.1038/nn1408;
Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N.,
Schaeffer L.;
"Histone deacetylase 9 couples neuronal activity to muscle chromatin
acetylation and gene expression.";
Nat. Neurosci. 8:313-321(2005).
[7]
INTERACTION WITH GLIS2.
PubMed=16326862; DOI=10.1093/nar/gki985;
Kim S.-C., Kim Y.-S., Jetten A.M.;
"Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses
transcription through interaction with C-terminal binding protein 1
(CtBP1).";
Nucleic Acids Res. 33:6805-6815(2005).
[8]
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).
[9]
SUMOYLATION, INTERACTION WITH HDAC3, AND SUBCELLULAR LOCATION.
PubMed=19204783; DOI=10.1371/journal.pone.0004363;
Gupta P., Ho P.C., Ha S.G., Lin Y.W., Wei L.N.;
"HDAC3 as a molecular chaperone for shuttling phosphorylated TR2 to
PML: a novel deacetylase activity-independent function of HDAC3.";
PLoS ONE 4:E4363-E4363(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
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).
[11]
INTERACTION WITH ZMYND15.
PubMed=20675388; DOI=10.1074/jbc.M110.116418;
Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
Saunders L., Verdin E., Charo I.F.;
"Zmynd15 encodes a histone deacetylase-dependent transcriptional
repressor essential for spermiogenesis and male fertility.";
J. Biol. Chem. 285:31418-31426(2010).
[12]
FUNCTION IN DEACETYLATION OF H3K27.
PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016;
Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D.,
Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M.,
Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W.,
Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.;
"A hybrid mechanism of action for BCL6 in B cells defined by formation
of functionally distinct complexes at enhancers and promoters.";
Cell Rep. 4:578-588(2013).
[13]
INTERACTION WITH NKAPL.
PubMed=25875095; DOI=10.1371/journal.pone.0124293;
Okuda H., Kiuchi H., Takao T., Miyagawa Y., Tsujimura A., Nonomura N.,
Miyata H., Okabe M., Ikawa M., Kawakami Y., Goshima N., Wada M.,
Tanaka H.;
"A novel transcriptional factor Nkapl is a germ cell-specific
suppressor of Notch signaling and is indispensable for
spermatogenesis.";
PLoS ONE 10:E0124293-E0124293(2015).
-!- FUNCTION: Responsible for the deacetylation of lysine residues on
the N-terminal part of the core histones (H2A, H2B, H3 and H4),
and some other non-histone substrates. 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. Participates in the BCL6
transcriptional repressor activity by deacetylating the H3 'Lys-
27' (H3K27) on enhancer elements, antagonizing EP300
acetyltransferase activity and repressing proximal gene
expression. Probably participates in the regulation of
transcription through its binding to the zinc-finger transcription
factor YY1; increases YY1 repression activity. Required to repress
transcription of the POU1F1 transcription factor. Acts as a
molecular chaperone for shuttling phosphorylated NR2C1 to PML
bodies for sumoylation (PubMed:23911289). Contributes, together
with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1
transcription factor gene expression in a PI(3)K/mTORC2/Akt-
dependent signaling pathway leading to endothelial cell (EC)
survival under disturbed flow/oxidative stress (By similarity).
{ECO:0000250|UniProtKB:O15379, ECO:0000269|PubMed:23911289}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Interacts with HDAC7 and HDAC9. Forms a heterologous
complex at least with YY1. Interacts with DAXX, HDAC10 and DACH1.
Found in a complex with NCOR1 and NCOR2. Component of the N-Cor
repressor complex, at least composed of NCOR1, NCOR2, HDAC3,
TBL1X, TBL1R, CORO2A and GPS2. Interacts with BCOR, MJD2A/JHDM3A,
NRIP1, PRDM6 and SRY. Interacts with BTBD14B. Interacts with
GLIS2. Interacts (via the DNA-binding domain) with NR2C1; the
interaction recruits phosphorylated NR2C1 to PML bodies for
sumoylation. Component of the Notch corepressor complex. Interacts
with CBFA2T3 and NKAP. Interacts with APEX1; the interaction is
not dependent on the acetylated status of APEX1. Interacts with
and deacetylates MAPK14. Interacts with ZMYND15. Interacts with
SMRT/NCOR2 and BCL6 on DNA enhancer elements. Interacts with INSM1
(PubMed:10984530, PubMed:11022042, PubMed:11533236,
PubMed:12130660, PubMed:15711539, PubMed:16326862,
PubMed:16537907, PubMed:19204783, PubMed:20675388). Interacts with
XBP1 isoform 1; the interaction occurs in endothelial cell (EC)
under disturbed flow. Interacts (via C-terminus) with CCAR2 (via
N-terminus). Interacts with and deacetylates MEF2D (By
similarity). Interacts with BEND3 (By similarity). Interacts with
NKAPL (PubMed:25875095). {ECO:0000250|UniProtKB:O15379,
ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11022042,
ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:12130660,
ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16326862,
ECO:0000269|PubMed:16537907, ECO:0000269|PubMed:19204783,
ECO:0000269|PubMed:20675388, ECO:0000269|PubMed:25875095}.
-!- INTERACTION:
Q9Z1E3:Nfkbia; NbExp=2; IntAct=EBI-302263, EBI-644427;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15379}.
Cytoplasm {ECO:0000250|UniProtKB:O15379}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:O15379}. Note=Colocalizes with XBP1 and
AKT1 in the cytoplasm. Predominantly expressed in the nucleus in
the presence of CCAR2 (By similarity).
{ECO:0000250|UniProtKB:O15379}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=O88895-1; Sequence=Displayed;
Name=Short;
IsoId=O88895-2; Sequence=VSP_002080;
-!- PTM: Sumoylated in vitro. {ECO:0000269|PubMed:19204783}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF074881; AAC36305.1; -; mRNA.
EMBL; AF074882; AAC36306.1; -; mRNA.
EMBL; AF079310; AAC67258.1; -; Genomic_DNA.
EMBL; AF079309; AAC67258.1; JOINED; Genomic_DNA.
PIR; JC7102; JC7102.
UniGene; Mm.20521; -.
ProteinModelPortal; O88895; -.
SMR; O88895; -.
CORUM; O88895; -.
DIP; DIP-32547N; -.
IntAct; O88895; 11.
MINT; MINT-4302141; -.
STRING; 10090.ENSMUSP00000037981; -.
ChEMBL; CHEMBL3832944; -.
iPTMnet; O88895; -.
PhosphoSitePlus; O88895; -.
EPD; O88895; -.
MaxQB; O88895; -.
PaxDb; O88895; -.
PeptideAtlas; O88895; -.
PRIDE; O88895; -.
MGI; MGI:1343091; Hdac3.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
HOGENOM; HOG000185805; -.
HOVERGEN; HBG057112; -.
InParanoid; O88895; -.
Reactome; R-MMU-1368071; NR1D1 (REV-ERBA) represses gene expression.
Reactome; R-MMU-1368082; RORA activates gene expression.
Reactome; R-MMU-1368092; Rora activates gene expression.
Reactome; R-MMU-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-MMU-1368110; Bmal1:Clock,Npas2 activates circadian gene expression.
Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-MMU-400253; Circadian Clock.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
Reactome; R-MMU-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-MMU-5667092; Nr1d1 (Rev-erba) represses gene expression.
ChiTaRS; Hdac3; mouse.
PRO; PR:O88895; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_HDAC3; -.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005876; C:spindle microtubule; ISO:MGI.
GO; GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0030332; F:cyclin binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0004407; F:histone deacetylase activity; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
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:MGI.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:MGI.
GO; GO:0071498; P:cellular response to fluid shear stress; ISS:UniProtKB.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; IGI:MGI.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0016575; P:histone deacetylation; IMP:MGI.
GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IMP:MGI.
GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006476; P:protein deacetylation; ISO:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IGI:MGI.
GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
GO; GO:0051225; P:spindle assembly; ISO: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.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Complete proteome;
Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 424 Histone deacetylase 3.
/FTId=PRO_0000114697.
REGION 3 316 Histone deacetylase.
ACT_SITE 135 135 {ECO:0000250}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000250|UniProtKB:O15379}.
VAR_SEQ 69 259 Missing (in isoform Short).
{ECO:0000303|PubMed:10491319}.
/FTId=VSP_002080.
SEQUENCE 424 AA; 48364 MW; B0C3BB2C5CD95E0E CRC64;
MAKTVAYFYD PDVGNFHYGA GHPMKPHRLA LTHSLVLHYG LYKKMIVFKP YQASQHDMCR
FHSEDYIDFL QRVSPTNMQG FTKSLNAFNV GDDCPVFPGL FEFCSRYTGA SLQGATQLNN
KICDIAINWA GGLHHAKKFE ASGFCYVNDI VIGILELLKY HPRVLYIDID IHHGDGVQEA
FYLTDRVMTV SFHKYGNYFF PGTGDMYEVG AESGRYYCLN VPLRDGIDDQ SYKHLFQPVI
SQVVDFYQPT CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV
RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN SRQYLDQIRQ
TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP EENYSRPEAP NEFYDGDHDN
DKES


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