Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O88895

- HDAC3_MOUSE

UniProt

O88895 - HDAC3_MOUSE

Protein

Histone deacetylase 3

Gene

Hdac3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 1351By 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

    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

    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

    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 – 4241PhosphoserineBy 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. 10 interactions.
    MINTiMINT-4302141.

    Structurei

    3D structure databases

    ProteinModelPortaliO88895.
    SMRiO88895. Positions 2-370.
    ModBaseiSearch...
    MobiDBiSearch...

    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. 1 PublicationVSP_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. 10 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: October 1, 2014
    This is version 125 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