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O15379

- HDAC3_HUMAN

UniProt

O15379 - HDAC3_HUMAN

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Protein

Histone deacetylase 3

Gene

HDAC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei135 – 1351By similarity

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. chromatin DNA binding Source: Ensembl
  3. cyclin binding Source: UniProtKB
  4. enzyme binding Source: UniProtKB
  5. histone deacetylase activity Source: UniProtKB
  6. histone deacetylase binding Source: BHF-UCL
  7. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  8. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  9. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  10. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  11. protein deacetylase activity Source: UniProtKB
  12. transcription corepressor activity Source: UniProtKB
  13. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. chromatin modification Source: UniProtKB
  3. circadian regulation of gene expression Source: Ensembl
  4. negative regulation of apoptotic process Source: ProtInc
  5. negative regulation of cell cycle Source: Reactome
  6. negative regulation of JNK cascade Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: UniProtKB
  8. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  9. neurotrophin TRK receptor signaling pathway Source: Reactome
  10. Notch signaling pathway Source: Reactome
  11. protein deacetylation Source: UniProtKB
  12. regulation of mitotic cell cycle Source: Ensembl
  13. regulation of multicellular organism growth Source: Ensembl
  14. small molecule metabolic process Source: Reactome
  15. spindle assembly Source: UniProtKB
  16. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_13695. p75NTR negatively regulates cell cycle via SC1.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SABIO-RKO15379.
SignaLinkiO15379.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 3 (EC:3.5.1.98)
Short name:
HD3
Alternative name(s):
RPD3-2
SMAP45
Gene namesi
Name:HDAC3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4854. HDAC3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. histone deacetylase complex Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. spindle microtubule Source: UniProtKB
  6. transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Histone deacetylase 3PRO_0000114696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki44 – 44Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei424 – 4241Phosphoserine1 Publication

Post-translational modificationi

Sumoylated in vitro.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15379.
PaxDbiO15379.
PRIDEiO15379.

PTM databases

PhosphoSiteiO15379.

Miscellaneous databases

PMAP-CutDBO15379.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiO15379.
CleanExiHS_HDAC3.
ExpressionAtlasiO15379. baseline and differential.
GenevestigatoriO15379.

Organism-specific databases

HPAiCAB005583.

Interactioni

Subunit structurei

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 INSM1.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPL1Q9UKG12EBI-607682,EBI-741243
DHX30Q7L2E33EBI-607682,EBI-1211456
ICP0P083933EBI-607682,EBI-6148881From a different organism.
KDM1AO603414EBI-607682,EBI-710124
L3MBTL2Q969R56EBI-607682,EBI-739909
MAGEA2BP433564EBI-607682,EBI-5650739
MBD1Q9UIS93EBI-607682,EBI-867196
MYCP011066EBI-607682,EBI-447544
NCOR1O753763EBI-607682,EBI-347233
NR2E3Q9Y5X42EBI-607682,EBI-7216962
NRIP1P485522EBI-607682,EBI-746484
Nrip1Q8CBD12EBI-607682,EBI-1771626From a different organism.
PPP4CP605104EBI-607682,EBI-1046072
SUZ12Q150227EBI-607682,EBI-1264675
vifP125042EBI-607682,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi114368. 256 interactions.
DIPiDIP-24253N.
IntActiO15379. 62 interactions.
MINTiMINT-196172.
STRINGi9606.ENSP00000302967.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Turni11 – 144Combined sources
Helixi27 – 3812Combined sources
Helixi41 – 444Combined sources
Beta strandi45 – 484Combined sources
Helixi55 – 584Combined sources
Turni59 – 613Combined sources
Helixi64 – 729Combined sources
Turni75 – 773Combined sources
Helixi78 – 814Combined sources
Helixi82 – 887Combined sources
Beta strandi91 – 944Combined sources
Helixi100 – 11920Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi145 – 1473Combined sources
Helixi149 – 1579Combined sources
Turni158 – 1603Combined sources
Beta strandi164 – 1685Combined sources
Beta strandi170 – 1723Combined sources
Helixi175 – 1806Combined sources
Turni181 – 1833Combined sources
Beta strandi185 – 19410Combined sources
Helixi212 – 2143Combined sources
Beta strandi217 – 2237Combined sources
Helixi229 – 24719Combined sources
Beta strandi250 – 2556Combined sources
Helixi258 – 2603Combined sources
Helixi273 – 28412Combined sources
Beta strandi290 – 2934Combined sources
Helixi300 – 31415Combined sources
Helixi329 – 3324Combined sources
Turni333 – 3353Combined sources
Beta strandi337 – 3393Combined sources
Helixi352 – 36716Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A69X-ray2.06A/B1-376[»]
ProteinModelPortaliO15379.
SMRiO15379. Positions 2-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 316314Histone deacetylaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiO15379.
KOiK11404.
OMAiNFHYGPG.
OrthoDBiEOG7DNNTW.
PhylomeDBiO15379.
TreeFamiTF352182.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15379-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAKTVAYFYD PDVGNFHYGA GHPMKPHRLA LTHSLVLHYG LYKKMIVFKP
60 70 80 90 100
YQASQHDMCR FHSEDYIDFL QRVSPTNMQG FTKSLNAFNV GDDCPVFPGL
110 120 130 140 150
FEFCSRYTGA SLQGATQLNN KICDIAINWA GGLHHAKKFE ASGFCYVNDI
160 170 180 190 200
VIGILELLKY HPRVLYIDID IHHGDGVQEA FYLTDRVMTV SFHKYGNYFF
210 220 230 240 250
PGTGDMYEVG AESGRYYCLN VPLRDGIDDQ SYKHLFQPVI NQVVDFYQPT
260 270 280 290 300
CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV
310 320 330 340 350
RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN
360 370 380 390 400
SRQYLDQIRQ TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP
410 420
EENYSRPEAP NEFYDGDHDN DKESDVEI
Length:428
Mass (Da):48,848
Last modified:July 15, 1998 - v2
Checksum:i94485C1EBDCF5AD0
GO
Isoform 2 (identifier: O15379-2) [UniParc]FASTAAdd to Basket

Also known as: RPD3-2A

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

Show »
Length:429
Mass (Da):49,111
Checksum:i0B654598513D284B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti359 – 3591R → L in AAC52038. (PubMed:9464271)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti411 – 4111N → S.
Corresponds to variant rs34901743 [ dbSNP | Ensembl ].
VAR_033988

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MAKTV…PDVGN → MIVFKPYQASQHDMCR in isoform 2. 1 PublicationVSP_002079Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4264.1. [O15379-1]
PIRiJC5834.
RefSeqiNP_003874.2. NM_003883.3. [O15379-1]
UniGeneiHs.519632.

Genome annotation databases

EnsembliENST00000305264; ENSP00000302967; ENSG00000171720. [O15379-1]
GeneIDi8841.
KEGGihsa:8841.
UCSCiuc003lle.1. human. [O15379-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4264.1. [O15379-1 ]
PIRi JC5834.
RefSeqi NP_003874.2. NM_003883.3. [O15379-1 ]
UniGenei Hs.519632.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4A69 X-ray 2.06 A/B 1-376 [» ]
ProteinModelPortali O15379.
SMRi O15379. Positions 2-370.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114368. 256 interactions.
DIPi DIP-24253N.
IntActi O15379. 62 interactions.
MINTi MINT-196172.
STRINGi 9606.ENSP00000302967.

Chemistry

BindingDBi O15379.
ChEMBLi CHEMBL3038484.
DrugBanki DB02546. Vorinostat.
GuidetoPHARMACOLOGYi 2617.

PTM databases

PhosphoSitei O15379.

Proteomic databases

MaxQBi O15379.
PaxDbi O15379.
PRIDEi O15379.

Protocols and materials databases

DNASUi 8841.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305264 ; ENSP00000302967 ; ENSG00000171720 . [O15379-1 ]
GeneIDi 8841.
KEGGi hsa:8841.
UCSCi uc003lle.1. human. [O15379-1 ]

Organism-specific databases

CTDi 8841.
GeneCardsi GC05M140980.
HGNCi HGNC:4854. HDAC3.
HPAi CAB005583.
MIMi 605166. gene.
neXtProti NX_O15379.
PharmGKBi PA29228.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0123.
GeneTreei ENSGT00530000062889.
HOGENOMi HOG000225180.
HOVERGENi HBG057112.
InParanoidi O15379.
KOi K11404.
OMAi NFHYGPG.
OrthoDBi EOG7DNNTW.
PhylomeDBi O15379.
TreeFami TF352182.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118789. REV-ERBA represses gene expression.
REACT_13695. p75NTR negatively regulates cell cycle via SC1.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SABIO-RK O15379.
SignaLinki O15379.

Miscellaneous databases

ChiTaRSi HDAC3. human.
GeneWikii HDAC3.
GenomeRNAii 8841.
NextBioi 33190.
PMAP-CutDB O15379.
PROi O15379.
SOURCEi Search...

Gene expression databases

Bgeei O15379.
CleanExi HS_HDAC3.
ExpressionAtlasi O15379. baseline and differential.
Genevestigatori O15379.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037913. His_deacetylse_1. 1 hit.
PRINTSi PR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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. 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. Cited for: FUNCTION IN DEACETYLATION OF H3K27, IDENTIFICATION IN A COMPLEX WITH BCL6 AND NCOR2.

Entry informationi

Entry nameiHDAC3_HUMAN
AccessioniPrimary (citable) accession number: O15379
Secondary accession number(s): D3DQE1
, O43268, Q9UEI5, Q9UEV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: October 29, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3