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O15379 (HDAC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 3

Short name=HD3
EC=3.5.1.98
Alternative name(s):
RPD3-2
SMAP45
Gene names
Name:HDAC3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. Ref.32 Ref.33

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. 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. Interact with SMRT/NCOR2 and BCL6 on DNA enhancer elements. Interacts with INSM1. 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.25 Ref.27 Ref.29 Ref.33

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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

chromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

circadian regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

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 direct assay Ref.25Ref.27. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16924111. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

protein deacetylation

Inferred from direct assay PubMed 17172643. Source: UniProtKB

regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

spindle assembly

Inferred from mutant phenotype PubMed 18326024. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Traceable author statement PubMed 12711221. Source: UniProtKB

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 18326024. Source: UniProtKB

spindle microtubule

Inferred from direct assay PubMed 18326024. Source: UniProtKB

transcriptional repressor complex

Inferred from direct assay Ref.20Ref.25Ref.27. Source: UniProtKB

   Molecular_functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

chromatin DNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay Ref.25Ref.27. Source: UniProtKB

cyclin binding

Inferred from physical interaction Ref.27. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 11641274. Source: UniProtKB

histone deacetylase activity

Inferred from mutant phenotype PubMed 16924111PubMed 18326024. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction PubMed 10869435PubMed 12590135. Source: BHF-UCL

protein deacetylase activity

Inferred from direct assay PubMed 17172643. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.25Ref.27. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.25. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Histone deacetylase 3
PRO_0000114696

Regions

Region3 – 316314Histone deacetylase

Sites

Active site1351 By similarity

Amino acid modifications

Modified residue4241Phosphoserine Ref.30
Cross-link44Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.28

Natural variations

Alternative sequence1 – 1515MAKTV…PDVGN → MIVFKPYQASQHDMCR in isoform 2.
VSP_002079
Natural variant4111N → S.
Corresponds to variant rs34901743 [ dbSNP | Ensembl ].
VAR_033988

Experimental info

Sequence conflict3591R → L in AAC52038. Ref.1

Secondary structure

.............................................................. 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RPD3-2B) [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 94485C1EBDCF5AD0

FASTA42848,848
        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 

« Hide

Isoform 2 (RPD3-2A) [UniParc].

Checksum: 0B654598513D284B
Show »

FASTA42949,111

References

« Hide '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. expand/collapse author list , 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]"INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene through the recruitment of cyclin D1 and histone deacetylases."
Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.
Biochem. J. 397:169-177(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSM1.
[26]"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.
[27]"Identification of an INSM1-binding site in the insulin promoter: negative regulation of the insulin gene transcription."
Wang H.W., Muguira M., Liu W.D., Zhang T., Chen C., Aucoin R., Breslin M.B., Lan M.S.
J. Endocrinol. 198:29-39(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSM1.
[28]"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.
Tissue: Cervix carcinoma.
[29]"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.
[30]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[31]"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].
[32]"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.
[33]"A hybrid mechanism of action for BCL6 in B cells defined by formation of functionally distinct complexes at enhancers and promoters."
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.
Cell Rep. 4:578-588(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEACETYLATION OF H3K27, IDENTIFICATION IN A COMPLEX WITH BCL6 AND NCOR2.
+Additional computationally mapped references.

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.
PIRJC5834.
RefSeqNP_003874.2. NM_003883.3.
UniGeneHs.519632.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4A69X-ray2.06A/B1-376[»]
ProteinModelPortalO15379.
SMRO15379. Positions 2-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114368. 250 interactions.
DIPDIP-24253N.
IntActO15379. 62 interactions.
MINTMINT-196172.
STRING9606.ENSP00000302967.

Chemistry

BindingDBO15379.
ChEMBLCHEMBL2111363.
DrugBankDB02546. Vorinostat.
GuidetoPHARMACOLOGY2617.

PTM databases

PhosphoSiteO15379.

Proteomic databases

PaxDbO15379.
PRIDEO15379.

Protocols and materials databases

DNASU8841.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305264; ENSP00000302967; ENSG00000171720. [O15379-1]
GeneID8841.
KEGGhsa:8841.
UCSCuc003lle.1. human. [O15379-1]

Organism-specific databases

CTD8841.
GeneCardsGC05M140980.
HGNCHGNC:4854. HDAC3.
HPACAB005583.
MIM605166. gene.
neXtProtNX_O15379.
PharmGKBPA29228.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000225180.
HOVERGENHBG057112.
InParanoidO15379.
KOK11404.
OMADESYIAL.
OrthoDBEOG7DNNTW.
PhylomeDBO15379.
TreeFamTF352182.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_24941. Circadian Clock.
SABIO-RKO15379.
SignaLinkO15379.

Gene expression databases

ArrayExpressO15379.
BgeeO15379.
CleanExHS_HDAC3.
GenevestigatorO15379.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Other

ChiTaRSHDAC3. human.
GeneWikiHDAC3.
GenomeRNAi8841.
NextBio33190.
PMAP-CutDBO15379.
PROO15379.
SOURCESearch...

Entry information

Entry nameHDAC3_HUMAN
AccessionPrimary (citable) accession number: O15379
Secondary accession number(s): D3DQE1 expand/collapse secondary AC list , O43268, Q9UEI5, Q9UEV0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM