HUMAN:HDAC3

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HDAC3
Protein Name(s)	Histone deacetylase 3 HD3 RPD3-2 SMAP45
External Links
UniProt	O15379
EMBL	U66914 U75697 U75696 AF005482 AF039703 AF059650 CH471062 CH471062 BC000614 AF053138 AF053137 AF053139
CCDS	CCDS4264.1
PIR	JC5834
RefSeq	NP_003874.2
UniGene	Hs.519632
PDB	4A69
PDBsum	4A69
ProteinModelPortal	O15379
SMR	O15379
BioGrid	114368
DIP	DIP-24253N
IntAct	O15379
MINT	MINT-196172
STRING	9606.ENSP00000302967
BindingDB	O15379
ChEMBL	CHEMBL3038484
DrugBank	DB02546
GuidetoPHARMACOLOGY	2617
PhosphoSite	O15379
MaxQB	O15379
PaxDb	O15379
PRIDE	O15379
DNASU	8841
Ensembl	ENST00000305264
GeneID	8841
KEGG	hsa:8841
UCSC	uc003lle.1
CTD	8841
GeneCards	GC05M140980
HGNC	HGNC:4854
HPA	CAB005583
MIM	605166
neXtProt	NX_O15379
PharmGKB	PA29228
eggNOG	COG0123
GeneTree	ENSGT00530000062889
HOGENOM	HOG000225180
HOVERGEN	HBG057112
InParanoid	O15379
KO	K11404
OMA	LFDFCSM
OrthoDB	EOG7DNNTW
PhylomeDB	O15379
TreeFam	TF352182
Reactome	REACT_111118 REACT_116145 REACT_118659 REACT_118780 REACT_118789 REACT_13695 REACT_160243 REACT_160254 REACT_19241 REACT_200608 REACT_228222 REACT_24941 REACT_27161
SABIO-RK	O15379
SignaLink	O15379
ChiTaRS	HDAC3
GeneWiki	HDAC3
GenomeRNAi	8841
NextBio	33190
PMAP-CutDB	O15379
PRO	PR:O15379
Proteomes	UP000005640
Bgee	O15379
CleanEx	HS_HDAC3
ExpressionAtlas	O15379
Genevestigator	O15379
GO	GO:0005737 GO:0000118 GO:0005654 GO:0005634 GO:0005876 GO:0017053 GO:0003682 GO:0031490 GO:0030332 GO:0019899 GO:0004407 GO:0042826 GO:0032041 GO:0097372 GO:0046969 GO:0046970 GO:0033558 GO:0003714 GO:0008134 GO:0044255 GO:0016568 GO:0032922 GO:0043066 GO:0045786 GO:0046329 GO:0000122 GO:0045892 GO:0048011 GO:0007219 GO:0006476 GO:0007346 GO:0040014 GO:0044281 GO:0051225 GO:0006351
Gene3D	3.40.800.20
InterPro	IPR000286 IPR003084 IPR023801
PANTHER	PTHR10625
Pfam	PF00850
PIRSF	PIRSF037913
PRINTS	PR01270 PR01271

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:21075309^[1]	ECO:0000315			P	Figure 1, F	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O88895	P	Seeded From UniProt	complete
involved_in	GO:0031398	positive regulation of protein ubiquitination	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O88895	P	Seeded From UniProt	complete
involved_in	GO:0042752	regulation of circadian rhythm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O88895	P	Seeded From UniProt	complete
involved_in	GO:0120162	positive regulation of cold-induced thermogenesis	PMID:28614293^[2]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O88895	P	Seeded From UniProt	complete
part_of	GO:0000118	histone deacetylase complex	PMID:18326024^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006476	protein deacetylation	PMID:21030595^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21030595^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21030595^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0051059	NF-kappaB binding	PMID:17785205^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q04206	F	Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:23867755^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UQL6	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:25190803^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0032008	positive regulation of TOR signaling	PMID:25190803^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:25190803^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042307	positive regulation of protein import into nucleus	PMID:25190803^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031647	regulation of protein stability	PMID:25190803^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:25190803^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0071498	cellular response to fluid shear stress	PMID:25190803^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:12590135^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UKV0	F	Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:10869435^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P56524	F	Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:10869435^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UQL6	F	Seeded From UniProt	complete
part_of	GO:0017053	transcriptional repressor complex	PMID:11804585^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
NOT\|involved_in	GO:0010832	negative regulation of myotube differentiation	PMID:10983972^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:18347167^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:18854353^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051225	spindle assembly	PMID:18326024^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046329	negative regulation of JNK cascade	PMID:11931768^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:16924111^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0033558	protein deacetylase activity	PMID:17172643^[16]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0030332	cyclin binding	PMID:18417529^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P24385	F	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:11641274^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9NWT6	F	Seeded From UniProt	complete
part_of	GO:0017053	transcriptional repressor complex	PMID:18417529^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0017053	transcriptional repressor complex	PMID:16569215^[19]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0017053	transcriptional repressor complex	PMID:12628926^[20]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:16569215^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q01101	F	Seeded From UniProt	complete
involved_in	GO:0006476	protein deacetylation	PMID:17172643^[16]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0072686	mitotic spindle	PMID:18326024^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:18326024^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004407	histone deacetylase activity	PMID:16924111^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004407	histone deacetylase activity	PMID:18326024^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:12628926^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:18417529^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:16569215^[19]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:18417529^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:16569215^[19]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:12628926^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:18417529^[17]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:16569215^[19]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0070933	histone H4 deacetylation	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:108086 MGI:MGI:1097691 MGI:MGI:1343091 PANTHER:PTN002578320 PomBase:SPAC3G9.07c SGD:S000005274 SGD:S000006272 UniProtKB:G5EB64 UniProtKB:Q13547	P	Seeded From UniProt	complete
involved_in	GO:0070932	histone H3 deacetylation	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:108086 MGI:MGI:1097691 PANTHER:PTN002578320 RGD:1309799 RGD:619976 RGD:619977 SGD:S000005274 TAIR:locus:2098115 UniProtKB:G5EB64 UniProtKB:Q13547	P	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002578320 PomBase:SPBC36.05c SGD:S000005274 SGD:S000006272 UniProtKB:O15379 UniProtKB:Q13547 UniProtKB:Q92769 WB:WBGene00001834	P	Seeded From UniProt	complete
enables	GO:0004407	histone deacetylase activity	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015805 FB:FBgn0025825 MGI:MGI:108086 MGI:MGI:1097691 PANTHER:PTN002578320 PomBase:SPAC3G9.07c PomBase:SPBC36.05c RGD:1309799 SGD:S000003162 SGD:S000005274 TAIR:locus:2162017 UniProtKB:G5EB64 UniProtKB:O15379 UniProtKB:Q13547 UniProtKB:Q7K6A1 UniProtKB:Q92769 WB:WBGene00001834 dictyBase:DDB_G0270338	F	Seeded From UniProt	complete
part_of	GO:0000118	histone deacetylase complex	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015805 MGI:MGI:108086 PANTHER:PTN002578320 PomBase:SPAC3G9.07c PomBase:SPBC36.05c SGD:S000003162 SGD:S000005274 SGD:S000006272 UniProtKB:Q13547 UniProtKB:Q92769 WB:WBGene00001834	C	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004407	histone deacetylase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003084	F	Seeded From UniProt	complete
involved_in	GO:0016575	histone deacetylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003084	P	Seeded From UniProt	complete
enables	GO:0004407	histone deacetylase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.5.1.98	F	Seeded From UniProt	complete
enables	GO:0032041	NAD-dependent histone deacetylase activity (H3-K14 specific)	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.5.1.98	F	Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P56520	F	Seeded From UniProt	complete
involved_in	GO:1903507	negative regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003714	P	Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:10777477^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9501169^[23] PMID:12711221^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004407	histone deacetylase activity	PMID:10777477^[22] PMID:12711221^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006325	chromatin organization	PMID:12711221^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:12711221^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12711221^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0000118	histone deacetylase complex	PMID:12711221^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0019216	regulation of lipid metabolic process	Reactome:R-HSA-400206	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007623	circadian rhythm	Reactome:R-HSA-400253	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-5663271 Reactome:R-HSA-5663265 Reactome:R-HSA-5663258 Reactome:R-HSA-5663245 Reactome:R-HSA-400183 Reactome:R-HSA-400143 Reactome:R-HSA-3777129 Reactome:R-HSA-2220982 Reactome:R-HSA-1368069	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
involved_in	GO:0006325	chromatin organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0156	P	Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0091	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Bhaskara, S et al. (2010) Hdac3 is essential for the maintenance of chromatin structure and genome stability. Cancer Cell 18 436-47 PubMed GONUTS page
↑ Emmett, MJ et al. (2017) Histone deacetylase 3 prepares brown adipose tissue for acute thermogenic challenge. Nature 546 544-548 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Ishii, S et al. (2008) Histone deacetylase 3 localizes to the mitotic spindle and is required for kinetochore-microtubule attachment. Proc. Natl. Acad. Sci. U.S.A. 105 4179-84 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Chini, CC et al. (2010) HDAC3 is negatively regulated by the nuclear protein DBC1. J. Biol. Chem. 285 40830-7 PubMed GONUTS page
↑ Wang, J et al. (2007) LZAP, a putative tumor suppressor, selectively inhibits NF-kappaB. Cancer Cell 12 239-51 PubMed GONUTS page
↑ Chang, CW et al. (2013) Involvement of Epac1/Rap1/CaMKI/HDAC5 signaling cascade in the regulation of placental cell fusion. Mol. Hum. Reprod. 19 745-55 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Martin, D et al. (2014) Unspliced X-box-binding protein 1 (XBP1) protects endothelial cells from oxidative stress through interaction with histone deacetylase 3. J. Biol. Chem. 289 30625-34 PubMed GONUTS page
↑ Petrie, K et al. (2003) The histone deacetylase 9 gene encodes multiple protein isoforms. J. Biol. Chem. 278 16059-72 PubMed GONUTS page
↑ ^9.0 ^9.1 Grozinger, CM & Schreiber, SL (2000) Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. U.S.A. 97 7835-40 PubMed GONUTS page
↑ Fischle, W et al. (2002) Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR. Mol. Cell 9 45-57 PubMed GONUTS page
↑ Lu, J et al. (2000) Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II histone deacetylases. Mol. Cell 6 233-44 PubMed GONUTS page
↑ Weichert, W et al. (2008) Class I histone deacetylase expression has independent prognostic impact in human colorectal cancer: specific role of class I histone deacetylases in vitro and in vivo. Clin. Cancer Res. 14 1669-77 PubMed GONUTS page
↑ Jahnke, P et al. (2008) The Cohesin loading factor NIPBL recruits histone deacetylases to mediate local chromatin modifications. Nucleic Acids Res. 36 6450-8 PubMed GONUTS page
↑ Zhang, J et al. (2002) The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2. Mol. Cell 9 611-23 PubMed GONUTS page
↑ ^15.0 ^15.1 Kim, MY et al. (2006) A repressor complex, AP4 transcription factor and geminin, negatively regulates expression of target genes in nonneuronal cells. Proc. Natl. Acad. Sci. U.S.A. 103 13074-9 PubMed GONUTS page
↑ ^16.0 ^16.1 Shimazu, T et al. (2007) Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing. J. Biol. Chem. 282 4470-8 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 Wang, HW et al. (2008) Identification of an INSM1-binding site in the insulin promoter: negative regulation of the insulin gene transcription. J. Endocrinol. 198 29-39 PubMed GONUTS page
↑ Mahon, PC et al. (2001) FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15 2675-86 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 ^19.4 Liu, WD et al. (2006) INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene through the recruitment of cyclin D1 and histone deacetylases. Biochem. J. 397 169-77 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 Yoon, HG et al. (2003) Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1. EMBO J. 22 1336-46 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 ^21.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^22.0 ^22.1 Juan, LJ et al. (2000) Histone deacetylases specifically down-regulate p53-dependent gene activation. J. Biol. Chem. 275 20436-43 PubMed GONUTS page
↑ Emiliani, S et al. (1998) Characterization of a human RPD3 ortholog, HDAC3. Proc. Natl. Acad. Sci. U.S.A. 95 2795-800 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 ^24.3 ^24.4 ^24.5 Verdin, E et al. (2003) Class II histone deacetylases: versatile regulators. Trends Genet. 19 286-93 PubMed GONUTS page

[PMID:21075309-1] Bhaskara, S et al. (2010) Hdac3 is essential for the maintenance of chromatin structure and genome stability. Cancer Cell 18 436-47 PubMed GONUTS page

[PMID:28614293-2] Emmett, MJ et al. (2017) Histone deacetylase 3 prepares brown adipose tissue for acute thermogenic challenge. Nature 546 544-548 PubMed GONUTS page

[PMID:18326024-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Ishii, S et al. (2008) Histone deacetylase 3 localizes to the mitotic spindle and is required for kinetochore-microtubule attachment. Proc. Natl. Acad. Sci. U.S.A. 105 4179-84 PubMed GONUTS page

[PMID:21030595-4] 4.0 ^4.1 ^4.2 Chini, CC et al. (2010) HDAC3 is negatively regulated by the nuclear protein DBC1. J. Biol. Chem. 285 40830-7 PubMed GONUTS page

[PMID:17785205-5] Wang, J et al. (2007) LZAP, a putative tumor suppressor, selectively inhibits NF-kappaB. Cancer Cell 12 239-51 PubMed GONUTS page

[PMID:23867755-6] Chang, CW et al. (2013) Involvement of Epac1/Rap1/CaMKI/HDAC5 signaling cascade in the regulation of placental cell fusion. Mol. Hum. Reprod. 19 745-55 PubMed GONUTS page

[PMID:25190803-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Martin, D et al. (2014) Unspliced X-box-binding protein 1 (XBP1) protects endothelial cells from oxidative stress through interaction with histone deacetylase 3. J. Biol. Chem. 289 30625-34 PubMed GONUTS page

[PMID:12590135-8] Petrie, K et al. (2003) The histone deacetylase 9 gene encodes multiple protein isoforms. J. Biol. Chem. 278 16059-72 PubMed GONUTS page

[PMID:10869435-9] 9.0 ^9.1 Grozinger, CM & Schreiber, SL (2000) Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. U.S.A. 97 7835-40 PubMed GONUTS page

[PMID:11804585-10] Fischle, W et al. (2002) Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR. Mol. Cell 9 45-57 PubMed GONUTS page

[PMID:10983972-11] Lu, J et al. (2000) Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II histone deacetylases. Mol. Cell 6 233-44 PubMed GONUTS page

[PMID:18347167-12] Weichert, W et al. (2008) Class I histone deacetylase expression has independent prognostic impact in human colorectal cancer: specific role of class I histone deacetylases in vitro and in vivo. Clin. Cancer Res. 14 1669-77 PubMed GONUTS page

[PMID:18854353-13] Jahnke, P et al. (2008) The Cohesin loading factor NIPBL recruits histone deacetylases to mediate local chromatin modifications. Nucleic Acids Res. 36 6450-8 PubMed GONUTS page

[PMID:11931768-14] Zhang, J et al. (2002) The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2. Mol. Cell 9 611-23 PubMed GONUTS page

[PMID:16924111-15] 15.0 ^15.1 Kim, MY et al. (2006) A repressor complex, AP4 transcription factor and geminin, negatively regulates expression of target genes in nonneuronal cells. Proc. Natl. Acad. Sci. U.S.A. 103 13074-9 PubMed GONUTS page

[PMID:17172643-16] 16.0 ^16.1 Shimazu, T et al. (2007) Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing. J. Biol. Chem. 282 4470-8 PubMed GONUTS page

[PMID:18417529-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 Wang, HW et al. (2008) Identification of an INSM1-binding site in the insulin promoter: negative regulation of the insulin gene transcription. J. Endocrinol. 198 29-39 PubMed GONUTS page

[PMID:11641274-18] Mahon, PC et al. (2001) FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15 2675-86 PubMed GONUTS page

[PMID:16569215-19] 19.0 ^19.1 ^19.2 ^19.3 ^19.4 Liu, WD et al. (2006) INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene through the recruitment of cyclin D1 and histone deacetylases. Biochem. J. 397 169-77 PubMed GONUTS page

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