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P56524

- HDAC4_HUMAN

UniProt

P56524 - HDAC4_HUMAN

Protein

Histone deacetylase 4

Gene

HDAC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (22 Sep 2009)
      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). 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. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.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
    Metal bindingi667 – 6671ZincBy similarity
    Metal bindingi669 – 6691ZincBy similarity
    Metal bindingi675 – 6751ZincBy similarity
    Metal bindingi751 – 7511ZincBy similarity
    Active sitei803 – 8031By similarity

    GO - Molecular functioni

    1. activating transcription factor binding Source: BHF-UCL
    2. core promoter binding Source: Ensembl
    3. histone deacetylase activity Source: BHF-UCL
    4. histone deacetylase binding Source: BHF-UCL
    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. potassium ion binding Source: BHF-UCL
    10. protein binding Source: UniProtKB
    11. protein deacetylase activity Source: BHF-UCL
    12. repressing transcription factor binding Source: BHF-UCL
    13. transcription corepressor activity Source: Ensembl
    14. transcription factor binding Source: BHF-UCL
    15. zinc ion binding Source: BHF-UCL

    GO - Biological processi

    1. B cell activation Source: UniProtKB
    2. B cell differentiation Source: UniProtKB
    3. cardiac muscle hypertrophy in response to stress Source: BHF-UCL
    4. chromatin remodeling Source: BHF-UCL
    5. histone deacetylation Source: BHF-UCL
    6. histone H3 deacetylation Source: BHF-UCL
    7. histone H4 deacetylation Source: BHF-UCL
    8. inflammatory response Source: UniProtKB
    9. negative regulation of cell proliferation Source: Ensembl
    10. negative regulation of glycolytic process Source: BHF-UCL
    11. negative regulation of myotube differentiation Source: BHF-UCL
    12. negative regulation of osteoblast differentiation Source: Ensembl
    13. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    14. negative regulation of transcription, DNA-templated Source: BHF-UCL
    15. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    16. nervous system development Source: UniProtKB
    17. osteoblast development Source: Ensembl
    18. peptidyl-lysine deacetylation Source: BHF-UCL
    19. positive regulation of cell proliferation Source: BHF-UCL
    20. positive regulation of protein sumoylation Source: UniProtKB
    21. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    22. positive regulation of transcription, DNA-templated Source: BHF-UCL
    23. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    24. regulation of cardiac muscle contraction by calcium ion signaling Source: Ensembl
    25. regulation of protein binding Source: BHF-UCL
    26. regulation of skeletal muscle fiber development Source: Ensembl
    27. response to denervation involved in regulation of muscle adaptation Source: BHF-UCL
    28. response to drug Source: Ensembl
    29. response to interleukin-1 Source: BHF-UCL
    30. skeletal system development Source: Ensembl
    31. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.5.1.98. 2681.
    ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 4 (EC:3.5.1.98)
    Short name:
    HD4
    Gene namesi
    Name:HDAC4
    Synonyms:KIAA0288
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:14063. HDAC4.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-246, Ser-467 and Ser-632 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation.

    GO - Cellular componenti

    1. A band Source: Ensembl
    2. actomyosin Source: Ensembl
    3. cytoplasm Source: BHF-UCL
    4. cytosol Source: Ensembl
    5. histone deacetylase complex Source: BHF-UCL
    6. neuromuscular junction Source: Ensembl
    7. nucleus Source: BHF-UCL
    8. transcriptional repressor complex Source: BHF-UCL
    9. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Brachydactyly-mental retardation syndrome (BDMR) [MIM:600430]: A syndrome resembling the physical anomalies found in Albright hereditary osteodystrophy. Common features are mild facial dysmorphism, congenital heart defects, distinct brachydactyly type E, mental retardation, developmental delay, seizures, autism spectrum disorder, and stocky build. Soft tissue ossification is absent, and there are no abnormalities in parathyroid hormone or calcium metabolism.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi246 – 2461S → A: Reduces phosphorylation and its subsequent nuclear export. 1 Publication
    Mutagenesisi467 – 4671S → A: Reduces phosphorylation and its subsequent nuclear export. 2 Publications
    Mutagenesisi559 – 5591K → R: Abolishes sumoylation and reduces the histone deacetylase activity. 1 Publication
    Mutagenesisi632 – 6321S → A: Reduces phosphorylation and its subsequent nuclear export. 2 Publications
    Mutagenesisi803 – 8031H → L: Abolishes histone deacetylase activity. 1 Publication
    Mutagenesisi1056 – 10561V → A: Reduces CaMK-dependent nuclear export. 1 Publication
    Mutagenesisi1062 – 10621L → A: Reduces CaMK-dependent nuclear export. 1 Publication

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi600430. phenotype.
    Orphaneti1001. 2q37 microdeletion syndrome.
    PharmGKBiPA29229.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10841084Histone deacetylase 4PRO_0000114699Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461Phosphoserine; by CaMK4 and SIK11 Publication
    Modified residuei350 – 3501Phosphoserine2 Publications
    Modified residuei467 – 4671Phosphoserine; by CaMK4 and SIK11 Publication
    Cross-linki559 – 559Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei565 – 5651Phosphoserine
    Modified residuei632 – 6321Phosphoserine; by CaMK42 Publications
    Modified residuei633 – 6331Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-350 impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3.4 Publications
    Sumoylation on Lys-559 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP56524.
    PaxDbiP56524.
    PRIDEiP56524.

    PTM databases

    PhosphoSiteiP56524.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP56524.
    BgeeiP56524.
    CleanExiHS_HDAC4.
    GenevestigatoriP56524.

    Organism-specific databases

    HPAiCAB004431.

    Interactioni

    Subunit structurei

    Interacts with HDAC7 By similarity. Homodimer. Homodimerization via its N-terminal domain. Interacts with MEF2C, AHRR, and NR2C1. Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner. Interacts with BTBD14B By similarity. Interacts with KDM5B. Interacts with MYOCD By similarity. Interacts with MORC2. Interacts with ANKRA2. Interacts with EP300 in the presence of TFAP2C.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102754EBI-308629,EBI-608057
    ATF2P153362EBI-308629,EBI-1170906
    BCL6P411823EBI-308629,EBI-765407
    BRMS1Q9HCU92EBI-308629,EBI-714781
    ICP0P083933EBI-308629,EBI-6148881From a different organism.
    MIF4GDA9UHW64EBI-308629,EBI-373498
    RUNX3Q137619EBI-308629,EBI-925990
    SFNP319474EBI-308629,EBI-476295
    UBE2IP632793EBI-308629,EBI-80168
    YWHABP319463EBI-308629,EBI-359815
    YWHAEP622584EBI-308629,EBI-356498
    YWHAGP619813EBI-308629,EBI-359832
    YWHAHQ049173EBI-308629,EBI-306940
    YWHAZP631045EBI-308629,EBI-347088

    Protein-protein interaction databases

    BioGridi115106. 189 interactions.
    DIPiDIP-34565N.
    IntActiP56524. 30 interactions.
    MINTiMINT-104901.
    STRINGi9606.ENSP00000264606.

    Structurei

    Secondary structure

    1
    1084
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 11249
    Helixi115 – 1217
    Turni122 – 1254
    Helixi126 – 1283
    Turni354 – 3574
    Beta strandi652 – 6576
    Helixi660 – 6623
    Beta strandi673 – 6753
    Helixi681 – 69111
    Helixi694 – 6974
    Beta strandi698 – 7014
    Helixi708 – 7114
    Turni712 – 7143
    Helixi717 – 7248
    Helixi727 – 7304
    Helixi737 – 7459
    Beta strandi746 – 7483
    Beta strandi754 – 7563
    Helixi762 – 78625
    Beta strandi789 – 7957
    Beta strandi813 – 8153
    Helixi817 – 82812
    Beta strandi834 – 8385
    Beta strandi840 – 8423
    Helixi845 – 8517
    Beta strandi857 – 8648
    Helixi866 – 8683
    Beta strandi870 – 8723
    Helixi883 – 8853
    Beta strandi889 – 8946
    Beta strandi898 – 9003
    Helixi904 – 91310
    Helixi915 – 9228
    Beta strandi925 – 9317
    Beta strandi936 – 9383
    Turni940 – 9434
    Helixi950 – 96112
    Helixi964 – 9663
    Beta strandi968 – 9725
    Helixi978 – 99215
    Helixi1002 – 10065
    Helixi1011 – 102515
    Helixi1029 – 10313
    Helixi1042 – 10476

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H8NX-ray2.60A/B/C/D62-153[»]
    2O94X-ray3.00A/B/C/D62-153[»]
    2VQJX-ray2.10A648-1057[»]
    2VQMX-ray1.80A648-1057[»]
    2VQOX-ray2.15A/B648-1057[»]
    2VQQX-ray1.90A/B648-1057[»]
    2VQVX-ray3.30A/B648-1057[»]
    2VQWX-ray3.00G648-1057[»]
    3UXGX-ray1.85B343-359[»]
    3UZDX-ray1.86B343-359[»]
    3V31X-ray1.57B343-359[»]
    4CBTX-ray3.03A/B/C648-1033[»]
    4CBYX-ray2.72A/B/C/D648-1033[»]
    ProteinModelPortaliP56524.
    SMRiP56524. Positions 62-129, 650-1051.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56524.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni118 – 313196Interaction with MEF2AAdd
    BLAST
    Regioni655 – 1084430Histone deacetylaseAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili67 – 177111Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1051 – 108434Nuclear export signalBy similarityAdd
    BLAST

    Domaini

    The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000232065.
    HOVERGENiHBG057100.
    InParanoidiP56524.
    KOiK11406.
    OMAiVSFGGHR.
    OrthoDBiEOG7RFTH5.
    PhylomeDBiP56524.
    TreeFamiTF106174.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR019154. Arb2_domain.
    IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF09757. Arb2. 1 hit.
    PF12203. HDAC4_Gln. 1 hit.
    PF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSiPR01270. HDASUPER.

    Sequencei

    Sequence statusi: Complete.

    P56524-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPSAVPMD     50
    LRLDHQFSLP VAEPALREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL 100
    SRQHEAQLHE HIKQQQEMLA MKHQQELLEH QRKLERHRQE QELEKQHREQ 150
    KLQQLKNKEK GKESAVASTE VKMKLQEFVL NKKKALAHRN LNHCISSDPR 200
    YWYGKTQHSS LDQSSPPQSG VSTSYNHPVL GMYDAKDDFP LRKTASEPNL 250
    KLRSRLKQKV AERRSSPLLR RKDGPVVTAL KKRPLDVTDS ACSSAPGSGP 300
    SSPNNSSGSV SAENGIAPAV PSIPAETSLA HRLVAREGSA APLPLYTSPS 350
    LPNITLGLPA TGPSAGTAGQ QDAERLTLPA LQQRLSLFPG THLTPYLSTS 400
    PLERDGGAAH SPLLQHMVLL EQPPAQAPLV TGLGALPLHA QSLVGADRVS 450
    PSIHKLRQHR PLGRTQSAPL PQNAQALQHL VIQQQHQQFL EKHKQQFQQQ 500
    QLQMNKIIPK PSEPARQPES HPEETEEELR EHQALLDEPY LDRLPGQKEA 550
    HAQAGVQVKQ EPIESDEEEA EPPREVEPGQ RQPSEQELLF RQQALLLEQQ 600
    RIHQLRNYQA SMEAAGIPVS FGGHRPLSRA QSSPASATFP VSVQEPPTKP 650
    RFTTGLVYDT LMLKHQCTCG SSSSHPEHAG RIQSIWSRLQ ETGLRGKCEC 700
    IRGRKATLEE LQTVHSEAHT LLYGTNPLNR QKLDSKKLLG SLASVFVRLP 750
    CGGVGVDSDT IWNEVHSAGA ARLAVGCVVE LVFKVATGEL KNGFAVVRPP 800
    GHHAEESTPM GFCYFNSVAV AAKLLQQRLS VSKILIVDWD VHHGNGTQQA 850
    FYSDPSVLYM SLHRYDDGNF FPGSGAPDEV GTGPGVGFNV NMAFTGGLDP 900
    PMGDAEYLAA FRTVVMPIAS EFAPDVVLVS SGFDAVEGHP TPLGGYNLSA 950
    RCFGYLTKQL MGLAGGRIVL ALEGGHDLTA ICDASEACVS ALLGNELDPL 1000
    PEKVLQQRPN ANAVRSMEKV MEIHSKYWRC LQRTTSTAGR SLIEAQTCEN 1050
    EEAETVTAMA SLSVGVKPAE KRPDEEPMEE EPPL 1084
    Length:1,084
    Mass (Da):119,040
    Last modified:September 22, 2009 - v3
    Checksum:iBB7FD37652D12398
    GO

    Sequence cautioni

    The sequence BAA22957.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti373 – 3731A → T in AAD29046. (PubMed:10220385)Curated
    Sequence conflicti373 – 3731A → T in BAA22957. (PubMed:9179496)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti727 – 7271P → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036042

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132607 mRNA. Translation: AAD29046.1.
    AB006626 mRNA. Translation: BAA22957.2. Different initiation.
    AC017028 Genomic DNA. No translation available.
    CCDSiCCDS2529.1.
    RefSeqiNP_006028.2. NM_006037.3.
    UniGeneiHs.20516.

    Genome annotation databases

    EnsembliENST00000345617; ENSP00000264606; ENSG00000068024.
    GeneIDi9759.
    KEGGihsa:9759.
    UCSCiuc002vyk.4. human.

    Polymorphism databases

    DMDMi259016348.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132607 mRNA. Translation: AAD29046.1 .
    AB006626 mRNA. Translation: BAA22957.2 . Different initiation.
    AC017028 Genomic DNA. No translation available.
    CCDSi CCDS2529.1.
    RefSeqi NP_006028.2. NM_006037.3.
    UniGenei Hs.20516.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H8N X-ray 2.60 A/B/C/D 62-153 [» ]
    2O94 X-ray 3.00 A/B/C/D 62-153 [» ]
    2VQJ X-ray 2.10 A 648-1057 [» ]
    2VQM X-ray 1.80 A 648-1057 [» ]
    2VQO X-ray 2.15 A/B 648-1057 [» ]
    2VQQ X-ray 1.90 A/B 648-1057 [» ]
    2VQV X-ray 3.30 A/B 648-1057 [» ]
    2VQW X-ray 3.00 G 648-1057 [» ]
    3UXG X-ray 1.85 B 343-359 [» ]
    3UZD X-ray 1.86 B 343-359 [» ]
    3V31 X-ray 1.57 B 343-359 [» ]
    4CBT X-ray 3.03 A/B/C 648-1033 [» ]
    4CBY X-ray 2.72 A/B/C/D 648-1033 [» ]
    ProteinModelPortali P56524.
    SMRi P56524. Positions 62-129, 650-1051.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115106. 189 interactions.
    DIPi DIP-34565N.
    IntActi P56524. 30 interactions.
    MINTi MINT-104901.
    STRINGi 9606.ENSP00000264606.

    Chemistry

    BindingDBi P56524.
    ChEMBLi CHEMBL3524.
    GuidetoPHARMACOLOGYi 2659.

    PTM databases

    PhosphoSitei P56524.

    Polymorphism databases

    DMDMi 259016348.

    Proteomic databases

    MaxQBi P56524.
    PaxDbi P56524.
    PRIDEi P56524.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345617 ; ENSP00000264606 ; ENSG00000068024 .
    GeneIDi 9759.
    KEGGi hsa:9759.
    UCSCi uc002vyk.4. human.

    Organism-specific databases

    CTDi 9759.
    GeneCardsi GC02M239969.
    GeneReviewsi HDAC4.
    HGNCi HGNC:14063. HDAC4.
    HPAi CAB004431.
    MIMi 600430. phenotype.
    605314. gene.
    neXtProti NX_P56524.
    Orphaneti 1001. 2q37 microdeletion syndrome.
    PharmGKBi PA29229.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000232065.
    HOVERGENi HBG057100.
    InParanoidi P56524.
    KOi K11406.
    OMAi VSFGGHR.
    OrthoDBi EOG7RFTH5.
    PhylomeDBi P56524.
    TreeFami TF106174.

    Enzyme and pathway databases

    BRENDAi 3.5.1.98. 2681.
    Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

    Miscellaneous databases

    EvolutionaryTracei P56524.
    GeneWikii HDAC4.
    GenomeRNAii 9759.
    NextBioi 36731.
    PROi P56524.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56524.
    Bgeei P56524.
    CleanExi HS_HDAC4.
    Genevestigatori P56524.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR019154. Arb2_domain.
    IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF09757. Arb2. 1 hit.
    PF12203. HDAC4_Gln. 1 hit.
    PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSi PR01270. HDASUPER.
    ProtoNeti Search...

    Publicationsi

    1. "Three proteins define a class of human histone deacetylases related to yeast Hda1p."
      Grozinger C.M., Hassig C.A., Schreiber S.L.
      Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leukemia.
    2. "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins."
      Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
      DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO N-TERMINUS.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "HDAC4 deacetylase associates with and represses the MEF2 transcription factor."
      Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T.
      EMBO J. 18:5099-5107(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MEF2A.
    6. "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor."
      Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., Th'ng J., Han J., Yang X.-J.
      Mol. Cell. Biol. 19:7816-7827(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MEF2C AND MEF2D, MUTAGENESIS OF HIS-803.
    7. Cited for: PHOSPHORYLATION AT SER-246; SER-467 AND SER-632, MUTAGENESIS OF SER-246; SER-467 AND SER-632.
    8. "The modular nature of histone deacetylase HDAC4 confers phosphorylation-dependent intracellular trafficking."
      Zhao X., Ito A., Kane C.D., Liao T.-S., Bolger T.A., Lemrow S.M., Means A.R., Yao T.-P.
      J. Biol. Chem. 276:35042-35048(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-467 AND SER-632.
    9. "Identification of a signal-responsive nuclear export sequence in class II histone deacetylases."
      McKinsey T.A., Zhang C.-L., Olson E.N.
      Mol. Cell. Biol. 21:6312-6321(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR EXPORT SIGNAL, MUTAGENESIS OF VAL-1056 AND LEU-1062.
    10. "The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases."
      Franco P.J., Farooqui M., Seto E., Wei L.-N.
      Mol. Endocrinol. 15:1318-1328(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C1.
    11. Cited for: HOMODIMERIZATION, SUMOYLATION AT LYS-559, MUTAGENESIS OF LYS-559.
    12. "Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases."
      Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.
      Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDM5B.
    13. "Nuclear calcium/calmodulin-dependent protein kinase IIdelta preferentially transmits signals to histone deacetylase 4 in cardiac cells."
      Little G.H., Bai Y., Williams T., Poizat C.
      J. Biol. Chem. 282:7219-7231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CAMK2D.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Haploinsufficiency of HDAC4 causes brachydactyly mental retardation syndrome, with brachydactyly type E, developmental delays, and behavioral problems."
      Williams S.R., Aldred M.A., Der Kaloustian V.M., Halal F., Gowans G., McLeod D.R., Zondag S., Toriello H.V., Magenis R.E., Elsea S.H.
      Am. J. Hum. Genet. 87:219-228(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN BDMR.
    17. "Involvement of histone deacetylation in MORC2-mediated down-regulation of carbonic anhydrase IX."
      Shao Y., Li Y., Zhang J., Liu D., Liu F., Zhao Y., Shen T., Li F.
      Nucleic Acids Res. 38:2813-2824(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MORC2.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Differential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1."
      Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y., Kim Y.N., Seong J.K., Lee M.O.
      Cancer Res. 74:1484-1494(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EP300.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 343-359 IN COMPLEX WITH ANKRA2, PHOSPHORYLATION AT SER-350.
    22. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-727.

    Entry informationi

    Entry nameiHDAC4_HUMAN
    AccessioniPrimary (citable) accession number: P56524
    Secondary accession number(s): Q9UND6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 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 2
      Human chromosome 2: 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