HUMAN:HDAC3

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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
IPI	IPI00006187 IPI00217965
PIR	JC5834
RefSeq	NP_003874.2
UniGene	Hs.519632
ProteinModelPortal	O15379
SMR	O15379
DIP	DIP-24253N
IntAct	O15379
MINT	MINT-196172
STRING	O15379
PhosphoSite	O15379
PRIDE	O15379
Ensembl	ENST00000305264
GeneID	8841
KEGG	hsa:8841
UCSC	uc003llf.2
CTD	8841
GeneCards	GC05M136145
H-InvDB	HIX0200752
HGNC	HGNC:4854
HPA	CAB005583
MIM	605166
neXtProt	NX_O15379
PharmGKB	PA29228
eggNOG	prNOG11179
HOGENOM	HBG396919
HOVERGEN	HBG057112
InParanoid	O15379
OMA	NLKMCQH
OrthoDB	EOG4MGS79
PhylomeDB	O15379
Pathway_Interaction_DB	retinoic_acid_pathway hdac_classi_pathway hdac_classii_pathway
Reactome	REACT_111045 REACT_111102 REACT_22258
BindingDB	O15379
DrugBank	DB02546
NextBio	33190
PMAP-CutDB	O15379
ArrayExpress	O15379
Bgee	O15379
CleanEx	HS_HDAC3
Genevestigator	O15379
GermOnline	ENSG00000171720
GO	GO:0005737 GO:0000118 GO:0005876 GO:0017053 GO:0034739 GO:0042826 GO:0032041 GO:0046969 GO:0046970 GO:0003714 GO:0008134 GO:0006916 GO:0044255 GO:0045786 GO:0046329 GO:0000122 GO:0048011 GO:0051225 GO:0006351
InterPro	IPR000286 IPR003084 IPR023801
Gene3D	G3DSA:3.40.800.20
KO	K11404
PANTHER	PTHR10625
Pfam	PF00850
PIRSF	PIRSF037913
PRINTS	PR01270 PR01271

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0000118	histone deacetylase complex	PMID:12711221^[1]	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0000122	negative regulation of transcription from RNA polymerase II promoter	PMID:12628926^[2]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0000122	negative regulation of transcription from RNA polymerase II promoter	PMID:18854353^[3]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0000785	chromatin	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000060357	C	Seeded From UniProt
	GO:0003677	DNA binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000037981	F	Seeded From UniProt
	GO:0003682	chromatin binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000037981	F	Seeded From UniProt
	GO:0003714	transcription corepressor activity	PMID:12628926^[2]	IMP: Inferred from Mutant Phenotype		F	Seeded From UniProt
	GO:0004407	histone deacetylase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003084	F	Seeded From UniProt
	GO:0004407	histone deacetylase activity	PMID:10777477^[4]	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004407	histone deacetylase activity	PMID:12711221^[1]	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004407	histone deacetylase activity	PMID:16924111^[5]	IMP: Inferred from Mutant Phenotype		F	Seeded From UniProt
	GO:0004407	histone deacetylase activity	PMID:18326024^[6]	IMP: Inferred from Mutant Phenotype		F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10898795^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q6W2J9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11006275^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q8CBD1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11006275^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q8CBD1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11259576^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P29590-5	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11861901^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q969S8	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15016912^[11]	IPI: Inferred from Physical Interaction	UniProtKB:P54253	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16432238^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UIS9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16924111^[5]	IPI: Inferred from Physical Interaction	UniProtKB:O75496	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16924111^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q01664	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16924111^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y618	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17172643^[13]	IPI: Inferred from Physical Interaction	UniProtKB:O43809	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18854353^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q6KC79	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19409814^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q8N5F7	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21258344^[15]	IPI: Inferred from Physical Interaction	UniProtKB:O75376	F	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000060357	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C	Seeded From UniProt
	GO:0005634	nucleus	PMID:12711221^[1]	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:18326024^[6]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:18347167^[16]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:9501169^[17]	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005654	nucleoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000060357	C	Seeded From UniProt
	GO:0005654	nucleoplasm	Reactome:REACT_19175	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005654	nucleoplasm	Reactome:REACT_19283	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000060357	C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:12711221^[1]	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005876	spindle microtubule	PMID:18326024^[6]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0006351	transcription, DNA-dependent	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0804	P	Seeded From UniProt
	GO:0006355	regulation of transcription, DNA-dependent	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0805	P	Seeded From UniProt
	GO:0006476	protein deacetylation	PMID:17172643^[13]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006916	anti-apoptosis	PMID:10777477^[4]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007346	regulation of mitotic cell cycle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000037981	P	Seeded From UniProt
	GO:0008134	transcription factor binding	PMID:12711221^[1]	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0016568	chromatin modification	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0156	P	Seeded From UniProt
	GO:0016568	chromatin modification	PMID:12711221^[1]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0016575	histone deacetylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003084	P	Seeded From UniProt
	GO:0016575	histone deacetylation	PMID:10777477^[4]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0016575	histone deacetylation	PMID:12711221^[1]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0016575	histone deacetylation	PMID:16924111^[5]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0016575	histone deacetylation	PMID:18326024^[6]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0016787	hydrolase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0378	F	Seeded From UniProt
	GO:0017053	transcriptional repressor complex	PMID:11804585^[18]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0017053	transcriptional repressor complex	PMID:12628926^[2]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0031078	histone deacetylase activity (H3-K14 specific)	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:3.5.1.98	F	Seeded From UniProt
	GO:0032041	NAD-dependent histone deacetylase activity (H3-K14 specific)	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:3.5.1.98	F	Seeded From UniProt
	GO:0032129	histone deacetylase activity (H3-K9 specific)	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:3.5.1.98	F	Seeded From UniProt
	GO:0032922	circadian regulation of gene expression	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000037981	P	Seeded From UniProt
	GO:0033558	protein deacetylase activity	PMID:17172643^[13]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0034739	histone deacetylase activity (H3-K16 specific)	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:3.5.1.98	F	Seeded From UniProt
	GO:0040014	regulation of multicellular organism growth	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000037981	P	Seeded From UniProt
	GO:0042493	response to drug	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000060357	P	Seeded From UniProt
	GO:0042826	histone deacetylase binding	PMID:10869435^[19]	IPI: Inferred from Physical Interaction	UniProtKB:P56524	F	Seeded From UniProt
	GO:0042826	histone deacetylase binding	PMID:10869435^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UQL6	F	Seeded From UniProt
	GO:0042826	histone deacetylase binding	PMID:12590135^[20]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UKV0	F	Seeded From UniProt
	GO:0044255	cellular lipid metabolic process	Reactome:REACT_22279	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0044281	small molecule metabolic process	Reactome:REACT_111217	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0045786	negative regulation of cell cycle	Reactome:REACT_13695	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0045892	negative regulation of transcription, DNA-dependent	PMID:16924111^[5]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0046329	negative regulation of JNK cascade	PMID:11931768^[21]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0046969	NAD-dependent histone deacetylase activity (H3-K9 specific)	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:3.5.1.98	F	Seeded From UniProt
	GO:0046970	NAD-dependent histone deacetylase activity (H4-K16 specific)	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:3.5.1.98	F	Seeded From UniProt
	GO:0048011	nerve growth factor receptor signaling pathway	Reactome:REACT_11061	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0048011	nerve growth factor receptor signaling pathway	Reactome:REACT_13776	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0051225	spindle assembly	PMID:18326024^[6]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0010832	negative regulation of myotube differentiation	PMID:10983972^[22]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:21075309^[23]	IMP: Inferred from Mutant Phenotype		P	Figure 1, F	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Verdin E et al. (2003) Class II histone deacetylases: versatile regulators. Trends Genet 19: 286-93 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 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
↑ ^3.0 ^3.1 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
↑ ^4.0 ^4.1 ^4.2 Juan LJ et al. (2000) Histone deacetylases specifically down-regulate p53-dependent gene activation. J Biol Chem 275: 20436-43 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 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
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 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
↑ Huynh KD et al. (2000) BCoR, a novel corepressor involved in BCL-6 repression. Genes Dev 14: 1810-23 PubMed GONUTS page
↑ ^8.0 ^8.1 Wei LN et al. (2000) Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing. J Biol Chem 275: 40782-7 PubMed GONUTS page
↑ Wu WS et al. (2001) The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol Cell Biol 21: 2259-68 PubMed GONUTS page
↑ Tong JJ et al. (2002) Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain. Nucleic Acids Res 30: 1114-23 PubMed GONUTS page
↑ Tsai CC et al. (2004) Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors. Proc Natl Acad Sci U S A 101: 4047-52 PubMed GONUTS page
↑ Villa R et al. (2006) The methyl-CpG binding protein MBD1 is required for PML-RARalpha function. Proc Natl Acad Sci U S A 103: 1400-5 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 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
↑ Pajerowski AG et al. (2009) NKAP is a transcriptional repressor of notch signaling and is required for T cell development. Immunity 30: 696-707 PubMed GONUTS page
↑ Bantscheff M et al. (2011) Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes. Nat Biotechnol 29: 255-65 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
↑ 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
↑ 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
↑ ^19.0 ^19.1 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
↑ Petrie K et al. (2003) The histone deacetylase 9 gene encodes multiple protein isoforms. J Biol Chem 278: 16059-72 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
↑ 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
↑ 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:12711221-0] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Verdin E et al. (2003) Class II histone deacetylases: versatile regulators. Trends Genet 19: 286-93 PubMed GONUTS page

[PMID:12628926-1] 2.0 ^2.1 ^2.2 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

[PMID:18854353-2] 3.0 ^3.1 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:10777477-3] 4.0 ^4.1 ^4.2 Juan LJ et al. (2000) Histone deacetylases specifically down-regulate p53-dependent gene activation. J Biol Chem 275: 20436-43 PubMed GONUTS page

[PMID:16924111-4] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 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:18326024-5] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 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:10898795-6] Huynh KD et al. (2000) BCoR, a novel corepressor involved in BCL-6 repression. Genes Dev 14: 1810-23 PubMed GONUTS page

[PMID:11006275-7] 8.0 ^8.1 Wei LN et al. (2000) Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing. J Biol Chem 275: 40782-7 PubMed GONUTS page

[PMID:11259576-8] Wu WS et al. (2001) The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol Cell Biol 21: 2259-68 PubMed GONUTS page

[PMID:11861901-9] Tong JJ et al. (2002) Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain. Nucleic Acids Res 30: 1114-23 PubMed GONUTS page

[PMID:15016912-10] Tsai CC et al. (2004) Ataxin 1, a SCA1 neurodegenerative disorder protein, is functionally linked to the silencing mediator of retinoid and thyroid hormone receptors. Proc Natl Acad Sci U S A 101: 4047-52 PubMed GONUTS page

[PMID:16432238-11] Villa R et al. (2006) The methyl-CpG binding protein MBD1 is required for PML-RARalpha function. Proc Natl Acad Sci U S A 103: 1400-5 PubMed GONUTS page

[PMID:17172643-12] 13.0 ^13.1 ^13.2 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:19409814-13] Pajerowski AG et al. (2009) NKAP is a transcriptional repressor of notch signaling and is required for T cell development. Immunity 30: 696-707 PubMed GONUTS page

[PMID:21258344-14] Bantscheff M et al. (2011) Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes. Nat Biotechnol 29: 255-65 PubMed GONUTS page

[PMID:18347167-15] 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:9501169-16] 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

[PMID:11804585-17] 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:10869435-18] 19.0 ^19.1 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:12590135-19] Petrie K et al. (2003) The histone deacetylase 9 gene encodes multiple protein isoforms. J Biol Chem 278: 16059-72 PubMed GONUTS page

[PMID:11931768-20] 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:10983972-21] 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:21075309-22] 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

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HUMAN:HDAC3

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