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O88895

- HDAC3_MOUSE

UniProt

O88895 - HDAC3_MOUSE

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Protein

Histone deacetylase 3

Gene
Hdac3
Organism
Mus musculus (Mouse)
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.1 Publication

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 – 1351 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. chromatin modification Source: UniProtKB
  2. circadian regulation of gene expression Source: MGI
  3. histone deacetylation Source: MGI
  4. negative regulation of JNK cascade Source: Ensembl
  5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  6. regulation of mitotic cell cycle Source: MGI
  7. regulation of multicellular organism growth Source: MGI
  8. spindle assembly Source: Ensembl
  9. 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_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_202086. p75NTR negatively regulates cell cycle via SC1.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 3 (EC:3.5.1.98)
Short name:
HD3
Gene namesi
Name:Hdac3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1343091. Hdac3.

Subcellular locationi

Nucleus By similarity 1 Publication

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: Ensembl
  6. transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Histone deacetylase 3PRO_0000114697Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Sumoylated in vitro.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO88895.
PaxDbiO88895.
PRIDEiO88895.

PTM databases

PhosphoSiteiO88895.

Expressioni

Gene expression databases

ArrayExpressiO88895.
BgeeiO88895.
CleanExiMM_HDAC3.
GenevestigatoriO88895.

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 INSM1.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NfkbiaQ9Z1E32EBI-302263,EBI-644427

Protein-protein interaction databases

DIPiDIP-32547N.
IntActiO88895. 8 interactions.
MINTiMINT-4302141.

Structurei

3D structure databases

ProteinModelPortaliO88895.
SMRiO88895. Positions 2-370.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
HOGENOMiHOG000185805.
HOVERGENiHBG057112.
InParanoidiO88895.

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 Long (identifier: O88895-1) [UniParc]FASTAAdd to Basket

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

MAKTVAYFYD PDVGNFHYGA GHPMKPHRLA LTHSLVLHYG LYKKMIVFKP    50
YQASQHDMCR FHSEDYIDFL QRVSPTNMQG FTKSLNAFNV GDDCPVFPGL 100
FEFCSRYTGA SLQGATQLNN KICDIAINWA GGLHHAKKFE ASGFCYVNDI 150
VIGILELLKY HPRVLYIDID IHHGDGVQEA FYLTDRVMTV SFHKYGNYFF 200
PGTGDMYEVG AESGRYYCLN VPLRDGIDDQ SYKHLFQPVI SQVVDFYQPT 250
CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV 300
RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN 350
SRQYLDQIRQ TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP 400
EENYSRPEAP NEFYDGDHDN DKES 424
Length:424
Mass (Da):48,364
Last modified:November 1, 1998 - v1
Checksum:iB0C3BB2C5CD95E0E
GO
Isoform Short (identifier: O88895-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-259: Missing.

Show »
Length:233
Mass (Da):26,906
Checksum:i4052A9AF341E3A66
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei69 – 259191Missing in isoform Short. VSP_002080Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF074881 mRNA. Translation: AAC36305.1.
AF074882 mRNA. Translation: AAC36306.1.
AF079310, AF079309 Genomic DNA. Translation: AAC67258.1.
PIRiJC7102.
UniGeneiMm.20521.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF074881 mRNA. Translation: AAC36305.1 .
AF074882 mRNA. Translation: AAC36306.1 .
AF079310 , AF079309 Genomic DNA. Translation: AAC67258.1 .
PIRi JC7102.
UniGenei Mm.20521.

3D structure databases

ProteinModelPortali O88895.
SMRi O88895. Positions 2-370.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-32547N.
IntActi O88895. 8 interactions.
MINTi MINT-4302141.

Chemistry

BindingDBi O88895.

PTM databases

PhosphoSitei O88895.

Proteomic databases

MaxQBi O88895.
PaxDbi O88895.
PRIDEi O88895.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:1343091. Hdac3.

Phylogenomic databases

eggNOGi COG0123.
HOGENOMi HOG000185805.
HOVERGENi HBG057112.
InParanoidi O88895.

Enzyme and pathway databases

Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_202086. p75NTR negatively regulates cell cycle via SC1.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSi HDAC3. mouse.
PROi O88895.
SOURCEi Search...

Gene expression databases

ArrayExpressi O88895.
Bgeei O88895.
CleanExi MM_HDAC3.
Genevestigatori O88895.

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

  1. "Cloning and characterization of the murine histone deacetylase (HDAC3)."
    Mahlknecht U., Hoelzer D., Bucala R., Verdin E.
    Biochem. Biophys. Res. Commun. 263:482-490(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    Strain: C3H and C57BL/6J.
  2. Cited for: INTERACTION WITH HDAC7.
  3. "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor."
    Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.
    J. Biol. Chem. 276:35-39(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC9.
  4. "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.
  5. "Tissue-specific regulation of retinal and pituitary precursor cell proliferation."
    Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.
    Science 297:1180-1183(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DACH1.
  6. "Histone deacetylase 9 couples neuronal activity to muscle chromatin acetylation and gene expression."
    Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N., Schaeffer L.
    Nat. Neurosci. 8:313-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC9.
  7. "Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses transcription through interaction with C-terminal binding protein 1 (CtBP1)."
    Kim S.-C., Kim Y.-S., Jetten A.M.
    Nucleic Acids Res. 33:6805-6815(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLIS2.
  8. "PRISM/PRDM6, a transcriptional repressor that promotes the proliferative gene program in smooth muscle cells."
    Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G., Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.
    Mol. Cell. Biol. 26:2626-2636(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRDM6.
  9. "HDAC3 as a molecular chaperone for shuttling phosphorylated TR2 to PML: a novel deacetylase activity-independent function of HDAC3."
    Gupta P., Ho P.C., Ha S.G., Lin Y.W., Wei L.N.
    PLoS ONE 4:E4363-E4363(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, INTERACTION WITH HDAC3, SUBCELLULAR LOCATION.
  10. "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor essential for spermiogenesis and male fertility."
    Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A., Saunders L., Verdin E., Charo I.F.
    J. Biol. Chem. 285:31418-31426(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZMYND15.
  11. Cited for: FUNCTION IN DEACETYLATION OF H3K27.

Entry informationi

Entry nameiHDAC3_MOUSE
AccessioniPrimary (citable) accession number: O88895
Secondary accession number(s): O88896
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi