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O15379

- HDAC3_HUMAN

UniProt

O15379 - HDAC3_HUMAN

Protein

Histone deacetylase 3

Gene

HDAC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    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 binding Source: UniProtKB
    12. protein deacetylase activity Source: UniProtKB
    13. transcription corepressor activity Source: UniProtKB
    14. 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

    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

    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

    ArrayExpressiO15379.
    BgeeiO15379.
    CleanExiHS_HDAC3.
    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. 251 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 – 84
    Turni11 – 144
    Helixi27 – 3812
    Helixi41 – 444
    Beta strandi45 – 484
    Helixi55 – 584
    Turni59 – 613
    Helixi64 – 729
    Turni75 – 773
    Helixi78 – 814
    Helixi82 – 887
    Beta strandi91 – 944
    Helixi100 – 11920
    Beta strandi124 – 1285
    Beta strandi145 – 1473
    Helixi149 – 1579
    Turni158 – 1603
    Beta strandi164 – 1685
    Beta strandi170 – 1723
    Helixi175 – 1806
    Turni181 – 1833
    Beta strandi185 – 19410
    Helixi212 – 2143
    Beta strandi217 – 2237
    Helixi229 – 24719
    Beta strandi250 – 2556
    Helixi258 – 2603
    Helixi273 – 28412
    Beta strandi290 – 2934
    Helixi300 – 31415
    Helixi329 – 3324
    Turni333 – 3353
    Beta strandi337 – 3393
    Helixi352 – 36716

    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.
    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

    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 NQVVDFYQPT 250
    CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV 300
    RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN 350
    SRQYLDQIRQ TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP 400
    EENYSRPEAP NEFYDGDHDN DKESDVEI 428
    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. 251 interactions.
    DIPi DIP-24253N.
    IntActi O15379. 62 interactions.
    MINTi MINT-196172.
    STRINGi 9606.ENSP00000302967.

    Chemistry

    BindingDBi O15379.
    ChEMBLi CHEMBL2093865.
    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.
    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

    ArrayExpressi O15379.
    Bgeei O15379.
    CleanExi HS_HDAC3.
    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

    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 1, 2014
    This is version 159 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