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Histone deacetylase 3 (HD3) (EC 3.5.1.98) (RPD3-2) (SMAP45)

 HDAC3_HUMAN             Reviewed;         428 AA.
O15379; D3DQE1; O43268; Q9UEI5; Q9UEV0;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
23-MAY-2018, entry version 196.
RecName: Full=Histone deacetylase 3;
Short=HD3;
EC=3.5.1.98;
AltName: Full=RPD3-2;
AltName: Full=SMAP45;
Name=HDAC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Spleen, and T-cell;
PubMed=9464271; DOI=10.1006/bbrc.1997.8033;
Dangond F., Hafler D.A., Tong J.K., Randall J., Kojima R., Utku N.,
Gullans S.R.;
"Differential display cloning of a novel human histone deacetylase
(HDAC3) cDNA from PHA-activated immune cells.";
Biochem. Biophys. Res. Commun. 242:648-652(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Fibroblast;
PubMed=9346952; DOI=10.1074/jbc.272.44.28001;
Yang W.-M., Yao Y.-L., Sun J.-M., Davie J.R., Seto E.;
"Isolation and characterization of cDNAs corresponding to an
additional member of the human histone deacetylase gene family.";
J. Biol. Chem. 272:28001-28007(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9501169; DOI=10.1073/pnas.95.6.2795;
Emiliani S., Fischle W., van Lint C., Al-Abed Y., Verdin E.;
"Characterization of a human RPD3 ortholog, HDAC3.";
Proc. Natl. Acad. Sci. U.S.A. 95:2795-2800(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=10051405; DOI=10.1006/geno.1998.5645;
Mahlknecht U., Emiliani S., Najfeld V., Young S., Verdin E.;
"Genomic organization and chromosomal localization of the human
histone deacetylase 3 gene.";
Genomics 56:197-202(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-353 AND 407-428.
Lynch E.D., Lee M.K., King M.-C.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH NRIP1.
PubMed=11006275; DOI=10.1074/jbc.M004821200;
Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.;
"Receptor-interacting protein 140 directly recruits histone
deacetylases for gene silencing.";
J. Biol. Chem. 275:40782-40787(2000).
[9]
INTERACTION WITH DAXX.
PubMed=10669754; DOI=10.1128/MCB.20.5.1784-1796.2000;
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.;
"Sequestration and inhibition of Daxx-mediated transcriptional
repression by PML.";
Mol. Cell. Biol. 20:1784-1796(2000).
[10]
INTERACTION WITH HDAC9.
PubMed=10655483; DOI=10.1073/pnas.97.3.1056;
Zhou X., Richon V.M., Rifkind R.A., Marks P.A.;
"Identification of a transcriptional repressor related to the
noncatalytic domain of histone deacetylases 4 and 5.";
Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000).
[11]
IDENTIFICATION IN A COMPLEX WITH NCOR1 AND NCOR2.
PubMed=10860984; DOI=10.1073/pnas.97.13.7202;
Wen Y.-D., Perissi V., Staszewski L.M., Yang W.-M., Krones A.,
Glass C.K., Rosenfeld M.G., Seto E.;
"The histone deacetylase-3 complex contains nuclear receptor
corepressors.";
Proc. Natl. Acad. Sci. U.S.A. 97:7202-7207(2000).
[12]
INTERACTION WITH HDAC7.
PubMed=11466315; DOI=10.1074/jbc.M104935200;
Fischle W., Dequiedt F., Fillion M., Hendzel M.J., Voelter W.,
Verdin E.;
"Human HDAC7 histone deacetylase activity is associated with HDAC3 in
vivo.";
J. Biol. Chem. 276:35826-35835(2001).
[13]
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).
[14]
INTERACTION WITH HDAC10.
PubMed=11861901; DOI=10.1093/nar/30.5.1114;
Tong J.J., Liu J., Bertos N.R., Yang X.-J.;
"Identification of HDAC10, a novel class II human histone deacetylase
containing a leucine-rich domain.";
Nucleic Acids Res. 30:1114-1123(2002).
[15]
SUMOYLATION.
PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
deacetylase.";
EMBO J. 21:2682-2691(2002).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF THE N-COR
COMPLEX WITH NCOR2 AND TBL1X.
PubMed=10809664;
Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A.,
Shiekhattar R.;
"A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-
repeat protein linked to deafness.";
Genes Dev. 14:1048-1057(2000).
[17]
COMPONENT OF THE N-COR COMPLEX WITH NCOR2 AND HDAC3.
PubMed=10944117; DOI=10.1093/emboj/19.16.4342;
Li J., Wang J., Wang J., Nawaz Z., Liu J.M., Qin J., Wong J.;
"Both corepressor proteins SMRT and N-CoR exist in large protein
complexes containing HDAC3.";
EMBO J. 19:4342-4350(2000).
[18]
INTERACTION WITH BCOR.
PubMed=10898795;
Huynh K.D., Fischle W., Verdin E., Bardwell V.J.;
"BCoR, a novel corepressor involved in BCL-6 repression.";
Genes Dev. 14:1810-1823(2000).
[19]
COMPONENT OF THE N-COR COMPLEX WITH NCOR1; NCOR2; GPS2; TBL1R AND
TBL1X.
PubMed=11931768; DOI=10.1016/S1097-2765(02)00468-9;
Zhang J., Kalkum M., Chait B.T., Roeder R.G.;
"The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK
pathway through the integral subunit GPS2.";
Mol. Cell 9:611-623(2002).
[20]
COMPONENT OF THE N-COR COMPLEX WITH TBL1R; TBL1X AND CORO2A.
PubMed=12628926; DOI=10.1093/emboj/cdg120;
Yoon H.-G., Chan D.W., Huang Z.-Q., Li J., Fondell J.D., Qin J.,
Wong J.;
"Purification and functional characterization of the human N-CoR
complex: the roles of HDAC3, TBL1 and TBLR1.";
EMBO J. 22:1336-1346(2003).
[21]
INTERACTION WITH APEX1.
PubMed=14633989; DOI=10.1093/emboj/cdg595;
Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.;
"Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation
of the parathyroid hormone gene.";
EMBO J. 22:6299-6309(2003).
[22]
INTERACTION WITH DACH1.
PubMed=14525983; DOI=10.1074/jbc.M310021200;
Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K.,
Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.;
"DACH1 inhibits transforming growth factor-beta signaling through
binding Smad4.";
J. Biol. Chem. 278:51673-51684(2003).
[23]
INTERACTION WITH SRY.
PubMed=15297880; DOI=10.1038/sj.emboj.7600352;
Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N.,
Aldrian-Herrada G., Poulat F., Berta P., Benkirane M.,
Boizet-Bonhoure B.;
"Regulation of human SRY subcellular distribution by its
acetylation/deacetylation.";
EMBO J. 23:3336-3345(2004).
[24]
INTERACTION WITH JMJD2A.
PubMed=15927959; DOI=10.1074/jbc.M413687200;
Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S.,
Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
"Functional characterization of JMJD2A, a histone deacetylase- and
retinoblastoma-binding protein.";
J. Biol. Chem. 280:28507-28518(2005).
[25]
INTERACTION WITH INSM1.
PubMed=16569215; DOI=10.1042/BJ20051669;
Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.;
"INSM1 functions as a transcriptional repressor of the neuroD/beta2
gene through the recruitment of cyclin D1 and histone deacetylases.";
Biochem. J. 397:169-177(2006).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[27]
INTERACTION WITH INSM1.
PubMed=18417529; DOI=10.1677/JOE-08-0001;
Wang H.W., Muguira M., Liu W.D., Zhang T., Chen C., Aucoin R.,
Breslin M.B., Lan M.S.;
"Identification of an INSM1-binding site in the insulin promoter:
negative regulation of the insulin gene transcription.";
J. Endocrinol. 198:29-39(2008).
[28]
INTERACTION WITH NKAP.
PubMed=19409814; DOI=10.1016/j.immuni.2009.02.011;
Pajerowski A.G., Nguyen C., Aghajanian H., Shapiro M.J., Shapiro V.S.;
"NKAP is a transcriptional repressor of notch signaling and is
required for T cell development.";
Immunity 30:696-707(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
INTERACTION WITH CCAR2 AND MEF2D, AND SUBCELLULAR LOCATION.
PubMed=21030595; DOI=10.1074/jbc.M110.153270;
Chini C.C., Escande C., Nin V., Chini E.N.;
"HDAC3 is negatively regulated by the nuclear protein DBC1.";
J. Biol. Chem. 285:40830-40837(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
INTERACTION WITH BEND3.
PubMed=21914818; DOI=10.1242/jcs.086603;
Sathyan K.M., Shen Z., Tripathi V., Prasanth K.V., Prasanth S.G.;
"A BEN-domain-containing protein associates with heterochromatin and
represses transcription.";
J. Cell Sci. 124:3149-3163(2011).
[33]
FUNCTION IN DEACETYLATION OF MAPK14.
PubMed=21444723; DOI=10.1128/MCB.01205-10;
Pillai V.B., Sundaresan N.R., Samant S.A., Wolfgeher D., Trivedi C.M.,
Gupta M.P.;
"Acetylation of a conserved lysine residue in the ATP binding pocket
of p38 augments its kinase activity during hypertrophy of
cardiomyocytes.";
Mol. Cell. Biol. 31:2349-2363(2011).
[34]
FUNCTION IN DEACETYLATION OF H3K27, AND IDENTIFICATION IN A COMPLEX
WITH BCL6 AND NCOR2.
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).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
FUNCTION, INTERACTION WITH XBP1, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=25190803; DOI=10.1074/jbc.M114.571984;
Martin D., Li Y., Yang J., Wang G., Margariti A., Jiang Z., Yu H.,
Zampetaki A., Hu Y., Xu Q., Zeng L.;
"Unspliced X-box-binding protein 1 (XBP1) protects endothelial cells
from oxidative stress through interaction with histone deacetylase
3.";
J. Biol. Chem. 289:30625-30634(2014).
-!- 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:21444723, 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 (PubMed:25190803). {ECO:0000269|PubMed:21444723,
ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:25190803}.
-!- 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:10655483, PubMed:10669754, PubMed:10860984,
PubMed:10898795, PubMed:11006275, PubMed:11466315,
PubMed:11533236, PubMed:11861901, PubMed:14525983,
PubMed:14633989, PubMed:15297880, PubMed:15927959,
PubMed:16569215, PubMed:18417529, PubMed:19409814,
PubMed:23911289). Interacts with XBP1 isoform 1; the interaction
occurs in endothelial cell (EC) under disturbed flow
(PubMed:25190803). Interacts (via C-terminus) with CCAR2 (via N-
terminus). Interacts with and deacetylates MEF2D. Interacts with
BEND3. Interacts with NKAPL (By similarity).
{ECO:0000250|UniProtKB:O88895, ECO:0000269|PubMed:10655483,
ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:10860984,
ECO:0000269|PubMed:10898795, ECO:0000269|PubMed:11006275,
ECO:0000269|PubMed:11466315, ECO:0000269|PubMed:11533236,
ECO:0000269|PubMed:11861901, ECO:0000269|PubMed:14525983,
ECO:0000269|PubMed:14633989, ECO:0000269|PubMed:15297880,
ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16569215,
ECO:0000269|PubMed:18417529, ECO:0000269|PubMed:19409814,
ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:21914818,
ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:25190803}.
-!- INTERACTION:
O43823:AKAP8; NbExp=10; IntAct=EBI-607682, EBI-1237481;
Q9ULX6:AKAP8L; NbExp=5; IntAct=EBI-607682, EBI-357530;
Q9UKG1:APPL1; NbExp=2; IntAct=EBI-607682, EBI-741243;
P24385:CCND1; NbExp=3; IntAct=EBI-607682, EBI-375001;
P23771:GATA3; NbExp=7; IntAct=EBI-607682, EBI-6664760;
Q13227:GPS2; NbExp=6; IntAct=EBI-607682, EBI-713355;
P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-607682, EBI-6148881;
O60341:KDM1A; NbExp=4; IntAct=EBI-607682, EBI-710124;
Q969R5:L3MBTL2; NbExp=6; IntAct=EBI-607682, EBI-739909;
P43356:MAGEA2B; NbExp=4; IntAct=EBI-607682, EBI-5650739;
Q9UIS9:MBD1; NbExp=3; IntAct=EBI-607682, EBI-867196;
P01106:MYC; NbExp=6; IntAct=EBI-607682, EBI-447544;
O75376:NCOR1; NbExp=5; IntAct=EBI-607682, EBI-347233;
Q60974:Ncor1 (xeno); NbExp=2; IntAct=EBI-607682, EBI-349004;
Q9Y618:NCOR2; NbExp=13; IntAct=EBI-607682, EBI-80830;
Q15466:NR0B2; NbExp=2; IntAct=EBI-607682, EBI-3910729;
P48552:NRIP1; NbExp=2; IntAct=EBI-607682, EBI-746484;
Q8CBD1:Nrip1 (xeno); NbExp=2; IntAct=EBI-607682, EBI-1771626;
P00558:PGK1; NbExp=2; IntAct=EBI-607682, EBI-709599;
P00558-1:PGK1; NbExp=3; IntAct=EBI-607682, EBI-16177310;
P60510:PPP4C; NbExp=4; IntAct=EBI-607682, EBI-1046072;
Q15022:SUZ12; NbExp=7; IntAct=EBI-607682, EBI-1264675;
P12504:vif (xeno); NbExp=2; IntAct=EBI-607682, EBI-779991;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21030595}.
Cytoplasm {ECO:0000269|PubMed:25190803}. Cytoplasm, cytosol
{ECO:0000269|PubMed:21030595}. Note=Colocalizes with XBP1 and AKT1
in the cytoplasm (PubMed:25190803). Predominantly expressed in the
nucleus in the presence of CCAR2. {ECO:0000269|PubMed:21030595,
ECO:0000269|PubMed:25190803}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=RPD3-2B;
IsoId=O15379-1; Sequence=Displayed;
Name=2; Synonyms=RPD3-2A;
IsoId=O15379-2; Sequence=VSP_002079;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- INDUCTION: Up-regulated by disturbed flow in umbilical vein
endothelial cells in vitro (PubMed:25190803).
-!- PTM: Sumoylated in vitro. {ECO:0000269|PubMed:12032081}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HDAC3ID40804ch5q31.html";
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EMBL; U66914; AAC52038.1; -; mRNA.
EMBL; U75697; AAB88241.1; -; mRNA.
EMBL; U75696; AAB88240.1; -; mRNA.
EMBL; AF005482; AAB87752.1; -; mRNA.
EMBL; AF039703; AAC98927.1; -; mRNA.
EMBL; AF059650; AAC26509.1; -; Genomic_DNA.
EMBL; CH471062; EAW61915.1; -; Genomic_DNA.
EMBL; CH471062; EAW61916.1; -; Genomic_DNA.
EMBL; BC000614; AAH00614.1; -; mRNA.
EMBL; AF053138; AAC08351.1; -; Genomic_DNA.
EMBL; AF053137; AAC08351.1; JOINED; Genomic_DNA.
EMBL; AF053139; AAC08352.1; -; Genomic_DNA.
CCDS; CCDS4264.1; -. [O15379-1]
PIR; JC5834; JC5834.
RefSeq; NP_003874.2; NM_003883.3. [O15379-1]
UniGene; Hs.519632; -.
PDB; 4A69; X-ray; 2.06 A; A/B=1-376.
PDBsum; 4A69; -.
ProteinModelPortal; O15379; -.
SMR; O15379; -.
BioGrid; 114368; 221.
CORUM; O15379; -.
DIP; DIP-24253N; -.
IntAct; O15379; 83.
MINT; O15379; -.
STRING; 9606.ENSP00000302967; -.
BindingDB; O15379; -.
ChEMBL; CHEMBL1829; -.
DrugBank; DB05015; Belinostat.
DrugBank; DB05651; MGCD-0103.
DrugBank; DB06603; Panobinostat.
DrugBank; DB05223; SB939.
DrugBank; DB02546; Vorinostat.
GuidetoPHARMACOLOGY; 2617; -.
iPTMnet; O15379; -.
PhosphoSitePlus; O15379; -.
BioMuta; HDAC3; -.
EPD; O15379; -.
MaxQB; O15379; -.
PaxDb; O15379; -.
PeptideAtlas; O15379; -.
PRIDE; O15379; -.
DNASU; 8841; -.
Ensembl; ENST00000305264; ENSP00000302967; ENSG00000171720. [O15379-1]
GeneID; 8841; -.
KEGG; hsa:8841; -.
UCSC; uc003llf.3; human. [O15379-1]
CTD; 8841; -.
DisGeNET; 8841; -.
EuPathDB; HostDB:ENSG00000171720.9; -.
GeneCards; HDAC3; -.
HGNC; HGNC:4854; HDAC3.
HPA; CAB005583; -.
HPA; HPA052052; -.
MIM; 605166; gene.
neXtProt; NX_O15379; -.
OpenTargets; ENSG00000171720; -.
PharmGKB; PA29228; -.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00910000144047; -.
HOGENOM; HOG000225180; -.
HOVERGEN; HBG057112; -.
InParanoid; O15379; -.
KO; K11404; -.
OMA; PRAWTHL; -.
OrthoDB; EOG091G067J; -.
PhylomeDB; O15379; -.
TreeFam; TF352182; -.
Reactome; R-HSA-1368071; NR1D1 (REV-ERBA) represses gene expression.
Reactome; R-HSA-193670; p75NTR negatively regulates cell cycle via SC1.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SABIO-RK; O15379; -.
SignaLink; O15379; -.
SIGNOR; O15379; -.
ChiTaRS; HDAC3; human.
GeneWiki; HDAC3; -.
GenomeRNAi; 8841; -.
PMAP-CutDB; O15379; -.
PRO; PR:O15379; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000171720; -.
CleanEx; HS_HDAC3; -.
ExpressionAtlas; O15379; baseline and differential.
Genevisible; O15379; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; IMP:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0033558; F:protein deacetylase activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0071498; P:cellular response to fluid shear stress; IDA:UniProtKB.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 428 Histone deacetylase 3.
/FTId=PRO_0000114696.
REGION 3 316 Histone deacetylase.
ACT_SITE 135 135 {ECO:0000250}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 15 MAKTVAYFYDPDVGN -> MIVFKPYQASQHDMCR (in
isoform 2). {ECO:0000303|PubMed:9346952}.
/FTId=VSP_002079.
VARIANT 411 411 N -> S (in dbSNP:rs34901743).
/FTId=VAR_033988.
CONFLICT 359 359 R -> L (in Ref. 1; AAC52038).
{ECO:0000305}.
STRAND 5 8 {ECO:0000244|PDB:4A69}.
TURN 11 14 {ECO:0000244|PDB:4A69}.
HELIX 27 38 {ECO:0000244|PDB:4A69}.
HELIX 41 44 {ECO:0000244|PDB:4A69}.
STRAND 45 48 {ECO:0000244|PDB:4A69}.
HELIX 55 58 {ECO:0000244|PDB:4A69}.
TURN 59 61 {ECO:0000244|PDB:4A69}.
HELIX 64 72 {ECO:0000244|PDB:4A69}.
TURN 75 77 {ECO:0000244|PDB:4A69}.
HELIX 78 81 {ECO:0000244|PDB:4A69}.
HELIX 82 88 {ECO:0000244|PDB:4A69}.
STRAND 91 94 {ECO:0000244|PDB:4A69}.
HELIX 100 119 {ECO:0000244|PDB:4A69}.
STRAND 124 128 {ECO:0000244|PDB:4A69}.
STRAND 145 147 {ECO:0000244|PDB:4A69}.
HELIX 149 157 {ECO:0000244|PDB:4A69}.
TURN 158 160 {ECO:0000244|PDB:4A69}.
STRAND 164 168 {ECO:0000244|PDB:4A69}.
STRAND 170 172 {ECO:0000244|PDB:4A69}.
HELIX 175 180 {ECO:0000244|PDB:4A69}.
TURN 181 183 {ECO:0000244|PDB:4A69}.
STRAND 185 194 {ECO:0000244|PDB:4A69}.
HELIX 212 214 {ECO:0000244|PDB:4A69}.
STRAND 217 223 {ECO:0000244|PDB:4A69}.
HELIX 229 247 {ECO:0000244|PDB:4A69}.
STRAND 250 255 {ECO:0000244|PDB:4A69}.
HELIX 258 260 {ECO:0000244|PDB:4A69}.
HELIX 273 284 {ECO:0000244|PDB:4A69}.
STRAND 290 293 {ECO:0000244|PDB:4A69}.
HELIX 300 314 {ECO:0000244|PDB:4A69}.
HELIX 329 332 {ECO:0000244|PDB:4A69}.
TURN 333 335 {ECO:0000244|PDB:4A69}.
STRAND 337 339 {ECO:0000244|PDB:4A69}.
HELIX 352 367 {ECO:0000244|PDB:4A69}.
SEQUENCE 428 AA; 48848 MW; 94485C1EBDCF5AD0 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
NQVVDFYQPT CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV
RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN SRQYLDQIRQ
TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP EENYSRPEAP NEFYDGDHDN
DKESDVEI


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