O15379 (HDAC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase 3
Short name=HD3
EC=3.5.1.98

Alternative name(s):
RPD3-2
SMAP45

Gene names

Name:

HDAC3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. 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 By similarity. Ref.30
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	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 By similarity. 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 By similarity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 Ref.21 Ref.22 Ref.23 Ref.24 Ref.27
Subcellular location	Nucleus.
Tissue specificity	Widely expressed.
Post-translational modification	Sumoylated in vitro. Ref.15
Sequence similarities	Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement. Source: Reactome cellular lipid metabolic process Traceable author statement. Source: Reactome circadian regulation of gene expression Inferred from electronic annotation. Source: Compara histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC negative regulation of JNK cascade Inferred from mutant phenotype Ref.19. Source: UniProtKB negative regulation of apoptotic process Traceable author statement PubMed 10777477. Source: ProtInc negative regulation of cell cycle Traceable author statement. Source: Reactome negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.20. Source: UniProtKB neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome spindle assembly Inferred from mutant phenotype PubMed 18326024. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Traceable author statement PubMed 12711221. Source: UniProtKB histone deacetylase complex Traceable author statement PubMed 12711221. Source: UniProtKB spindle microtubule Inferred from direct assay PubMed 18326024. Source: UniProtKB transcriptional repressor complex Inferred from direct assay Ref.20. Source: UniProtKB
Molecular_function	NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC chromatin DNA binding Inferred from electronic annotation. Source: Compara histone deacetylase activity Inferred from mutant phenotype PubMed 16924111PubMed 18326024. Source: UniProtKB transcription corepressor activity Inferred from mutant phenotype Ref.20. Source: UniProtKB transcription factor binding Traceable author statement PubMed 12711221. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAGEA2	P43356	4	EBI-607682,EBI-5650739
MBD1	Q9UIS9	3	EBI-607682,EBI-867196
MYC	P01106	6	EBI-607682,EBI-447544
NCOR1	O75376	2	EBI-607682,EBI-347233
Nrip1	Q8CBD1	2	EBI-607682,EBI-1771626	From a different organism.
SUZ12	Q15022	7	EBI-607682,EBI-1264675
vif	P12504	2	EBI-607682,EBI-779991	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15379-1)

Also known as: RPD3-2B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O15379-2)

Also known as: RPD3-2A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MAKTVAYFYDPDVGN → MIVFKPYQASQHDMCR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 428

428

Histone deacetylase 3

PRO_0000114696

Regions

Region

3 – 316

314

Histone deacetylase

Sites

Active site

135

1

By similarity

Amino acid modifications

Modified residue

424

1

Phosphoserine Ref.28

Cross-link

44

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.26

Natural variations

Alternative sequence

1 – 15

15

MAKTV…PDVGN → MIVFKPYQASQHDMCR in isoform 2.

VSP_002079

Natural variant

411

1

N → S.
Corresponds to variant rs34901743 [ dbSNP | Ensembl ].

VAR_033988

Experimental info

Sequence conflict

359

1

R → L in AAC52038. Ref.1

Secondary structure

1

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428

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Turn

11 – 14

4

Helix

27 – 38

12

Helix

41 – 44

4

Beta strand

45 – 48

4

Helix

55 – 58

4

Turn

59 – 61

3

Helix

64 – 72

9

Turn

75 – 77

3

Helix

78 – 81

4

Helix

82 – 88

7

Beta strand

91 – 94

4

Helix

100 – 119

20

Beta strand

124 – 128

5

Beta strand

145 – 147

3

Helix

149 – 157

9

Turn

158 – 160

3

Beta strand

164 – 168

5

Beta strand

170 – 172

3

Helix

175 – 180

6

Turn

181 – 183

3

Beta strand

185 – 194

10

Helix

212 – 214

3

Beta strand

217 – 223

7

Helix

229 – 247

19

Beta strand

250 – 255

6

Helix

258 – 260

3

Helix

273 – 284

12

Beta strand

290 – 293

4

Helix

300 – 314

15

Helix

329 – 332

4

Turn

333 – 335

3

Beta strand

337 – 339

3

Helix

352 – 367

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (RPD3-2B) [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 94485C1EBDCF5AD0	FASTA	428	48,848
	10 20 30 40 50 60 MAKTVAYFYD PDVGNFHYGA GHPMKPHRLA LTHSLVLHYG LYKKMIVFKP YQASQHDMCR 70 80 90 100 110 120 FHSEDYIDFL QRVSPTNMQG FTKSLNAFNV GDDCPVFPGL FEFCSRYTGA SLQGATQLNN 130 140 150 160 170 180 KICDIAINWA GGLHHAKKFE ASGFCYVNDI VIGILELLKY HPRVLYIDID IHHGDGVQEA 190 200 210 220 230 240 FYLTDRVMTV SFHKYGNYFF PGTGDMYEVG AESGRYYCLN VPLRDGIDDQ SYKHLFQPVI 250 260 270 280 290 300 NQVVDFYQPT CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV 310 320 330 340 350 360 RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN SRQYLDQIRQ 370 380 390 400 410 420 TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP EENYSRPEAP NEFYDGDHDN DKESDVEI
	Isoform 2 (RPD3-2A) [UniParc]. Checksum: 0B654598513D284B	FASTA	429	49,111
	10 20 30 40 50 60 MIVFKPYQAS QHDMCRFHYG AGHPMKPHRL ALTHSLVLHY GLYKKMIVFK PYQASQHDMC 70 80 90 100 110 120 RFHSEDYIDF LQRVSPTNMQ GFTKSLNAFN VGDDCPVFPG LFEFCSRYTG ASLQGATQLN 130 140 150 160 170 180 NKICDIAINW AGGLHHAKKF EASGFCYVND IVIGILELLK YHPRVLYIDI DIHHGDGVQE 190 200 210 220 230 240 AFYLTDRVMT VSFHKYGNYF FPGTGDMYEV GAESGRYYCL NVPLRDGIDD QSYKHLFQPV 250 260 270 280 290 300 INQVVDFYQP TCIVLQCGAD SLGCDRLGCF NLSIRGHGEC VEYVKSFNIP LLVLGGGGYT 310 320 330 340 350 360 VRNVARCWTY ETSLLVEEAI SEELPYSEYF EYFAPDFTLH PDVSTRIENQ NSRQYLDQIR 370 380 390 400 410 420 QTIFENLKML NHAPSVQIHD VPADLLTYDR TDEADAEERG PEENYSRPEA PNEFYDGDHD NDKESDVEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential display cloning of a novel human histone deacetylase (HDAC3) cDNA from PHA-activated immune cells." Dangond F., Hafler D.A., Tong J.K., Randall J., Kojima R., Utku N., Gullans S.R. Biochem. Biophys. Res. Commun. 242:648-652(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). Tissue: Spleen and T-cell.
[2]	"Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family." Yang W.-M., Yao Y.-L., Sun J.-M., Davie J.R., Seto E. J. Biol. Chem. 272:28001-28007(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Fibroblast.
[3]	"Characterization of a human RPD3 ortholog, HDAC3." Emiliani S., Fischle W., van Lint C., Al-Abed Y., Verdin E. Proc. Natl. Acad. Sci. U.S.A. 95:2795-2800(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Genomic organization and chromosomal localization of the human histone deacetylase 3 gene." Mahlknecht U., Emiliani S., Najfeld V., Young S., Verdin E. Genomics 56:197-202(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[7]	Lynch E.D., Lee M.K., King M.-C. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-353 AND 407-428.
[8]	"Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing." Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M. J. Biol. Chem. 275:40782-40787(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NRIP1.
[9]	"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML." Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D. Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAXX.
[10]	"Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5." Zhou X., Richon V.M., Rifkind R.A., Marks P.A. Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC9.
[11]	"The histone deacetylase-3 complex contains nuclear receptor corepressors." Wen Y.-D., Perissi V., Staszewski L.M., Yang W.-M., Krones A., Glass C.K., Rosenfeld M.G., Seto E. Proc. Natl. Acad. Sci. U.S.A. 97:7202-7207(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH NCOR1 AND NCOR2.
[12]	"Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo." Fischle W., Dequiedt F., Fillion M., Hendzel M.J., Voelter W., Verdin E. J. Biol. Chem. 276:35826-35835(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC7.
[13]	"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain." Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W. Mol. Cell. Biol. 21:6470-6483(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBFA2T3.
[14]	"Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain." Tong J.J., Liu J., Bertos N.R., Yang X.-J. Nucleic Acids Res. 30:1114-1123(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC10.
[15]	"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase." Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A. EMBO J. 21:2682-2691(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION.
[16]	"A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness." Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A., Shiekhattar R. Genes Dev. 14:1048-1057(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE N-COR COMPLEX WITH NCOR2 AND TBL1X.
[17]	"Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3." Li J., Wang J., Wang J., Nawaz Z., Liu J.M., Qin J., Wong J. EMBO J. 19:4342-4350(2000) [PubMed] [Europe PMC] [Abstract] Cited for: COMPONENT OF THE N-COR COMPLEX WITH NCOR2 AND HDAC3.
[18]	"BCoR, a novel corepressor involved in BCL-6 repression." Huynh K.D., Fischle W., Verdin E., Bardwell V.J. Genes Dev. 14:1810-1823(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BCOR.
[19]	"The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2." Zhang J., Kalkum M., Chait B.T., Roeder R.G. Mol. Cell 9:611-623(2002) [PubMed] [Europe PMC] [Abstract] Cited for: COMPONENT OF THE N-COR COMPLEX WITH NCOR1; NCOR2; GPS2; TBL1R AND TBL1X.
[20]	"Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1." Yoon H.-G., Chan D.W., Huang Z.-Q., Li J., Fondell J.D., Qin J., Wong J. EMBO J. 22:1336-1346(2003) [PubMed] [Europe PMC] [Abstract] Cited for: COMPONENT OF THE N-COR COMPLEX WITH TBL1R; TBL1X AND CORO2A.
[21]	"Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene." Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S. EMBO J. 22:6299-6309(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APEX1.
[22]	"DACH1 inhibits transforming growth factor-beta signaling through binding Smad4." 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. J. Biol. Chem. 278:51673-51684(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DACH1.
[23]	"Regulation of human SRY subcellular distribution by its acetylation/deacetylation." Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B. EMBO J. 23:3336-3345(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRY.
[24]	"Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein." 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. J. Biol. Chem. 280:28507-28518(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH JMJD2A.
[25]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[26]	"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells." Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X. Proteomics 8:2885-2896(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-44, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"NKAP is a transcriptional repressor of notch signaling and is required for T cell development." Pajerowski A.G., Nguyen C., Aghajanian H., Shapiro M.J., Shapiro V.S. Immunity 30:696-707(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NKAP.
[28]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[29]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]	"Acetylation of a conserved lysine residue in the ATP binding pocket of p38 augments its kinase activity during hypertrophy of cardiomyocytes." Pillai V.B., Sundaresan N.R., Samant S.A., Wolfgeher D., Trivedi C.M., Gupta M.P. Mol. Cell. Biol. 31:2349-2363(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DEACETYLATION OF MAPK14.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U66914 mRNA. Translation: AAC52038.1.
U75697 mRNA. Translation: AAB88241.1.
U75696 mRNA. Translation: AAB88240.1.
AF005482 mRNA. Translation: AAB87752.1.
AF039703 mRNA. Translation: AAC98927.1.
AF059650 Genomic DNA. Translation: AAC26509.1.
CH471062 Genomic DNA. Translation: EAW61915.1.
CH471062 Genomic DNA. Translation: EAW61916.1.
BC000614 mRNA. Translation: AAH00614.1.
AF053138, AF053137 Genomic DNA. Translation: AAC08351.1.
AF053139 Genomic DNA. Translation: AAC08352.1.

IPI

IPI00006187.
IPI00217965.

PIR

JC5834.

RefSeq

NP_003874.2. NM_003883.3.

UniGene

Hs.519632.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4A69	X-ray	2.06	A/B	1-376	[»]

ProteinModelPortal

O15379.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24253N.

IntAct

O15379. 30 interactions.

MINT

MINT-196172.

STRING

9606.ENSP00000302967.

PTM databases

PhosphoSite

O15379.

Proteomic databases

PaxDb

O15379.

PRIDE

O15379.

Protocols and materials databases

DNASU

8841.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305264; ENSP00000302967; ENSG00000171720.

GeneID

8841.

KEGG

hsa:8841.

UCSC

uc003lle.1. human.

Organism-specific databases

CTD

8841.

GeneCards

GC05M140980.

HGNC

HGNC:4854. HDAC3.

HPA

CAB005583.

MIM

605166. gene.

neXtProt

NX_O15379.

PharmGKB

PA29228.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0123.

HOGENOM

HOG000225180.

HOVERGEN

HBG057112.

InParanoid

O15379.

KO

K11404.

OMA

NFHYGPG.

OrthoDB

EOG4MGS79.

PhylomeDB

O15379.

Enzyme and pathway databases

Pathway_Interaction_DB

retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_24941. Circadian Clock.

SABIO-RK

O15379.

SignaLink

O15379.

Gene expression databases

ArrayExpress

O15379.

Bgee

O15379.

CleanEx

HS_HDAC3.

Genevestigator

O15379.

GermOnline

ENSG00000171720. Homo sapiens.

Family and domain databases

Gene3D

3.40.800.20. 1 hit.

InterPro

IPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]

PANTHER

PTHR10625. PTHR10625. 1 hit.

Pfam

PF00850. Hist_deacetyl. 1 hit.
[Graphical view]

PIRSF

PIRSF037913. His_deacetylse_1. 1 hit.

PRINTS

PR01270. HDASUPER.
PR01271. HISDACETLASE.

ProtoNet

Search...

Other

BindingDB

O15379.

ChEMBL

CHEMBL1829.

ChiTaRS

HDAC3. human.

DrugBank

DB02546. Vorinostat.

GenomeRNAi

8841.

NextBio

33190.

PMAP-CutDB

O15379.

SOURCE

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Entry information

Entry name

HDAC3_HUMAN

Accession

Primary (citable) accession number: O15379
Secondary accession number(s): D3DQE1 , O43268, Q9UEI5, Q9UEV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	May 29, 2013
This is version 144 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.