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Q9UQL6

- HDAC5_HUMAN

UniProt

Q9UQL6 - HDAC5_HUMAN

Protein

Histone deacetylase 5

Gene

HDAC5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      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 by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.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
    Metal bindingi696 – 6961ZincBy similarity
    Metal bindingi698 – 6981ZincBy similarity
    Metal bindingi704 – 7041ZincBy similarity
    Metal bindingi781 – 7811ZincBy similarity
    Active sitei833 – 8331By similarity

    GO - Molecular functioni

    1. histone deacetylase activity Source: BHF-UCL
    2. metal ion binding Source: UniProtKB-KW
    3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    5. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    7. protein binding Source: UniProtKB
    8. protein kinase C binding Source: UniProtKB
    9. repressing transcription factor binding Source: BHF-UCL
    10. transcription corepressor activity Source: Ensembl
    11. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. B cell activation Source: UniProtKB
    2. B cell differentiation Source: UniProtKB
    3. cellular response to insulin stimulus Source: BHF-UCL
    4. chromatin modification Source: UniProtKB
    5. chromatin organization Source: UniProtKB
    6. chromatin remodeling Source: ProtInc
    7. chromatin silencing Source: ProtInc
    8. heart development Source: Ensembl
    9. histone deacetylation Source: BHF-UCL
    10. inflammatory response Source: UniProtKB
    11. multicellular organismal response to stress Source: Ensembl
    12. negative regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
    13. negative regulation of myotube differentiation Source: BHF-UCL
    14. negative regulation of osteoblast differentiation Source: Ensembl
    15. negative regulation of transcription, DNA-templated Source: UniProtKB
    16. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    17. Notch signaling pathway Source: Reactome
    18. osteoblast development Source: Ensembl
    19. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    20. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    21. regulation of myotube differentiation Source: UniProtKB
    22. regulation of protein binding Source: BHF-UCL
    23. regulation of skeletal muscle fiber development Source: Ensembl
    24. response to cocaine Source: Ensembl
    25. response to drug Source: Ensembl
    26. 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

    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 5 (EC:3.5.1.98)
    Short name:
    HD5
    Alternative name(s):
    Antigen NY-CO-9
    Gene namesi
    Name:HDAC5
    Synonyms:KIAA0600
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:14068. HDAC5.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-259 and Ser-498 by AMPK, CaMK1 and SIK1.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Ensembl
    3. Golgi apparatus Source: HPA
    4. histone deacetylase complex Source: UniProtKB
    5. nuclear body Source: Ensembl
    6. nucleoplasm Source: Reactome
    7. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi259 – 2591S → A: Reduces AMPK- and caMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-498. Does not affect phosphorylation by PKN1 and PKN2. 3 Publications
    Mutagenesisi279 – 2791S → A: No effect. 1 Publication
    Mutagenesisi291 – 2911S → A: Does not affect phosphorylation by PKC. 1 Publication
    Mutagenesisi292 – 2921T → A: Abolishes phosphorylation by PKC. 1 Publication
    Mutagenesisi498 – 4981S → A: Reduces AMPK- and CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259. 2 Publications
    Mutagenesisi661 – 6611S → A: No effect. 1 Publication
    Mutagenesisi713 – 7131S → A: No effect. 1 Publication
    Mutagenesisi1086 – 10861V → A: Reduces CaMK-dependent nuclear export. 1 Publication
    Mutagenesisi1092 – 10921L → A: Reduces CaMK-dependent nuclear export. 1 Publication

    Organism-specific databases

    PharmGKBiPA29230.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11221122Histone deacetylase 5PRO_0000114701Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei259 – 2591Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD14 Publications
    Modified residuei292 – 2921Phosphothreonine; by PKC2 Publications
    Modified residuei498 – 4981Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD14 Publications
    Modified residuei533 – 5331N6-acetyllysine1 Publication
    Modified residuei661 – 6611Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and Ser-498. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription By similarity.By similarity
    Ubiquitinated. Polyubiquitination however does not lead to its degradation.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UQL6.
    PaxDbiQ9UQL6.
    PRIDEiQ9UQL6.

    PTM databases

    PhosphoSiteiQ9UQL6.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9UQL6.
    BgeeiQ9UQL6.
    CleanExiHS_HDAC5.
    GenevestigatoriQ9UQL6.

    Organism-specific databases

    HPAiCAB019400.
    HPA030991.

    Interactioni

    Subunit structurei

    Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts with EP300 in the presence of TFAP2C.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRMS1Q9HCU92EBI-715576,EBI-714781
    ICP0P083933EBI-715576,EBI-6148881From a different organism.
    RUNX3Q137615EBI-715576,EBI-925990
    SFNP319473EBI-715576,EBI-476295
    YWHAZP631042EBI-715576,EBI-347088

    Protein-protein interaction databases

    BioGridi115331. 332 interactions.
    DIPiDIP-38260N.
    IntActiQ9UQL6. 28 interactions.
    MINTiMINT-1407477.
    STRINGi9606.ENSP00000225983.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UQL6.
    SMRiQ9UQL6. Positions 96-133, 681-1061.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni684 – 1028345Histone deacetylaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1081 – 112242Nuclear export signalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi47 – 526Poly-Gly
    Compositional biasi85 – 928Poly-Gln
    Compositional biasi596 – 5994Poly-Glu
    Compositional biasi1099 – 11046Poly-Ala

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000232065.
    HOVERGENiHBG057100.
    InParanoidiQ9UQL6.
    KOiK11406.
    OMAiLGPYDSR.
    OrthoDBiEOG7RFTH5.
    PhylomeDBiQ9UQL6.
    TreeFamiTF106174.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF12203. HDAC4_Gln. 1 hit.
    PF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSiPR01270. HDASUPER.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UQL6-1) [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

    MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG     50
    GGSPSPVELR GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK 100
    QHDHLTRQHE VQLQKHLKQQ QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ 150
    RQEELEKQRL EQQLLILRNK EKSKESAIAS TEVKLRLQEF LLSKSKEPTP 200
    GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL PLPGPYDSRD 250
    DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI 300
    TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR 350
    ALPLDSSPNQ FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE 400
    RQALQSLRQG GTLTGKFMST SSIPGCLLGV ALEGDGSPHG HASLLQHVLL 450
    LEQARQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH RPLSRTQSSP 500
    LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE LPRQPTTHPE 550
    ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED 600
    CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT 650
    VPHQALGRTQ SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN 700
    THVHPEHAGR IQSIWSRLQE TGLLSKCERI RGRKATLDEI QTVHSEYHTL 750
    LYGTSPLNRQ KLDSKKLLGP ISQKMYAVLP CGGIGVDSDT VWNEMHSSSA 800
    VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM GFCFFNSVAI 850
    TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF 900
    FPGSGAPEEV GGGPGVGYNV NVAWTGGVDP PIGDVEYLTA FRTVVMPIAH 950
    EFSPDVVLVS AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL 1000
    ALEGGHDLTA ICDASEACVS ALLSVELQPL DEAVLQQKPN INAVATLEKV 1050
    IEIQSKHWSC VQKFAAGLGR SLREAQAGET EEAETVSAMA LLSVGAEQAQ 1100
    AAAAREHSPR PAEEPMEQEP AL 1122
    Length:1,122
    Mass (Da):121,978
    Last modified:May 18, 2010 - v2
    Checksum:iCF4BE774E3588FEC
    GO
    Isoform 2 (identifier: Q9UQL6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         684-768: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,037
    Mass (Da):112,191
    Checksum:iD4F09B907D2C1457
    GO
    Isoform 3 (identifier: Q9UQL6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         7-7: S → SA

    Show »
    Length:1,123
    Mass (Da):122,049
    Checksum:i909ED5CCFEE3FB4F
    GO

    Sequence cautioni

    The sequence AAC18040.1 differs from that shown. Reason: Frameshift at position 1085.
    The sequence BAA25526.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371V → L in BX458255. 1 PublicationCurated
    Sequence conflicti139 – 1391Q → R in BX458255. 1 PublicationCurated
    Sequence conflicti147 – 1471R → G in BX458255. 1 PublicationCurated
    Sequence conflicti593 – 5931D → E in AAD29047. (PubMed:10220385)Curated
    Sequence conflicti593 – 5931D → E in AAH51824. (PubMed:15489334)Curated
    Sequence conflicti593 – 5931D → E in AAC18040. (PubMed:9610721)Curated
    Sequence conflicti671 – 6711S → N in AAC18040. (PubMed:9610721)Curated
    Sequence conflicti684 – 6841G → S in AAC18040. (PubMed:9610721)Curated
    Sequence conflicti1026 – 10261E → K in AAC18040. (PubMed:9610721)Curated
    Sequence conflicti1074 – 10741E → G in AAC18040. (PubMed:9610721)Curated
    Sequence conflicti1093 – 10931S → L in AAC18040. (PubMed:9610721)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371R → Q.
    Corresponds to variant rs438096 [ dbSNP | Ensembl ].
    VAR_055903
    Natural varianti565 – 5651G → A.
    Corresponds to variant rs33916560 [ dbSNP | Ensembl ].
    VAR_055904

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei7 – 71S → SA in isoform 3. 1 PublicationVSP_039180
    Alternative sequencei684 – 76885Missing in isoform 2. 1 PublicationVSP_002081Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132608 mRNA. Translation: AAD29047.1.
    AB011172 mRNA. Translation: BAA25526.2. Different initiation.
    AC023855 Genomic DNA. No translation available.
    BC013140 mRNA. Translation: AAH13140.1. Different termination.
    BC051824 mRNA. Translation: AAH51824.1.
    BX458255 mRNA. No translation available.
    AF039691 mRNA. Translation: AAC18040.1. Frameshift.
    BK000028 Genomic DNA. Translation: DAA00017.1.
    CCDSiCCDS32663.1. [Q9UQL6-3]
    CCDS45696.1. [Q9UQL6-1]
    RefSeqiNP_001015053.1. NM_001015053.1. [Q9UQL6-3]
    NP_005465.2. NM_005474.4. [Q9UQL6-1]
    XP_005256961.1. XM_005256904.2. [Q9UQL6-3]
    XP_005256963.1. XM_005256906.2. [Q9UQL6-1]
    UniGeneiHs.438782.

    Genome annotation databases

    EnsembliENST00000225983; ENSP00000225983; ENSG00000108840. [Q9UQL6-3]
    ENST00000336057; ENSP00000337290; ENSG00000108840. [Q9UQL6-2]
    ENST00000586802; ENSP00000468004; ENSG00000108840. [Q9UQL6-1]
    GeneIDi10014.
    KEGGihsa:10014.
    UCSCiuc002ifd.1. human. [Q9UQL6-1]
    uc002iff.1. human. [Q9UQL6-3]
    uc010czp.1. human. [Q9UQL6-2]

    Polymorphism databases

    DMDMi296434519.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132608 mRNA. Translation: AAD29047.1 .
    AB011172 mRNA. Translation: BAA25526.2 . Different initiation.
    AC023855 Genomic DNA. No translation available.
    BC013140 mRNA. Translation: AAH13140.1 . Different termination.
    BC051824 mRNA. Translation: AAH51824.1 .
    BX458255 mRNA. No translation available.
    AF039691 mRNA. Translation: AAC18040.1 . Frameshift.
    BK000028 Genomic DNA. Translation: DAA00017.1 .
    CCDSi CCDS32663.1. [Q9UQL6-3 ]
    CCDS45696.1. [Q9UQL6-1 ]
    RefSeqi NP_001015053.1. NM_001015053.1. [Q9UQL6-3 ]
    NP_005465.2. NM_005474.4. [Q9UQL6-1 ]
    XP_005256961.1. XM_005256904.2. [Q9UQL6-3 ]
    XP_005256963.1. XM_005256906.2. [Q9UQL6-1 ]
    UniGenei Hs.438782.

    3D structure databases

    ProteinModelPortali Q9UQL6.
    SMRi Q9UQL6. Positions 96-133, 681-1061.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115331. 332 interactions.
    DIPi DIP-38260N.
    IntActi Q9UQL6. 28 interactions.
    MINTi MINT-1407477.
    STRINGi 9606.ENSP00000225983.

    Chemistry

    ChEMBLi CHEMBL3038483.
    GuidetoPHARMACOLOGYi 2660.

    PTM databases

    PhosphoSitei Q9UQL6.

    Polymorphism databases

    DMDMi 296434519.

    Proteomic databases

    MaxQBi Q9UQL6.
    PaxDbi Q9UQL6.
    PRIDEi Q9UQL6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225983 ; ENSP00000225983 ; ENSG00000108840 . [Q9UQL6-3 ]
    ENST00000336057 ; ENSP00000337290 ; ENSG00000108840 . [Q9UQL6-2 ]
    ENST00000586802 ; ENSP00000468004 ; ENSG00000108840 . [Q9UQL6-1 ]
    GeneIDi 10014.
    KEGGi hsa:10014.
    UCSCi uc002ifd.1. human. [Q9UQL6-1 ]
    uc002iff.1. human. [Q9UQL6-3 ]
    uc010czp.1. human. [Q9UQL6-2 ]

    Organism-specific databases

    CTDi 10014.
    GeneCardsi GC17M042159.
    H-InvDB HIX0013862.
    HGNCi HGNC:14068. HDAC5.
    HPAi CAB019400.
    HPA030991.
    MIMi 605315. gene.
    neXtProti NX_Q9UQL6.
    PharmGKBi PA29230.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000232065.
    HOVERGENi HBG057100.
    InParanoidi Q9UQL6.
    KOi K11406.
    OMAi LGPYDSR.
    OrthoDBi EOG7RFTH5.
    PhylomeDBi Q9UQL6.
    TreeFami TF106174.

    Enzyme and pathway databases

    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

    ChiTaRSi HDAC5. human.
    GeneWikii Histone_deacetylase_5.
    GenomeRNAii 10014.
    NextBioi 37831.
    PROi Q9UQL6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UQL6.
    Bgeei Q9UQL6.
    CleanExi HS_HDAC5.
    Genevestigatori Q9UQL6.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi 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 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] (ISOFORM 1).
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Eye and Testis.
    6. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORM 3).
      Tissue: Neuroblastoma.
    7. "Characterization of human colon cancer antigens recognized by autologous antibodies."
      Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
      Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-1122 (ISOFORM 1).
      Tissue: Colon carcinoma.
    8. "Chromosomal organization and localization of the human histone deacetylase 5 gene (HDAC5)."
      Mahlknecht U., Schnittger S., Ottmann O.G., Schoch C., Mosebach M., Hiddemann W., Hoelzer D.
      Biochim. Biophys. Acta 1493:342-348(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE ORGANIZATION.
    9. "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.
    10. "Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation."
      McKinsey T.A., Zhang C.-L., Lu J., Olson E.N.
      Nature 408:106-111(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-259; SER-279; SER-498; SER-661 AND SER-713.
    11. "Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5."
      McKinsey T.A., Zhang C.-L., Olson E.N.
      Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH 14-3-3, PHOSPHORYLATION AT SER-259 AND SER-498.
    12. "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-1086 AND LEU-1092.
    13. "Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes."
      Hook S.S., Orian A., Cowley S.M., Eisenman R.N.
      Proc. Natl. Acad. Sci. U.S.A. 99:13425-13430(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    14. "Point mutations in BCL6 DNA-binding domain reveal distinct roles for the six zinc fingers."
      Mascle X., Albagli O., Lemercier C.
      Biochem. Biophys. Res. Commun. 300:391-396(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCL6.
    15. "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.
    16. "Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion."
      Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.
      J. Biol. Chem. 282:35687-35694(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDIT3.
    17. "AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5."
      McGee S.L., van Denderen B.J., Howlett K.F., Mollica J., Schertzer J.D., Kemp B.E., Hargreaves M.
      Diabetes 57:860-867(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-259 AND SER-498, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-259 AND SER-498.
    18. "Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis."
      Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K., McKinsey T.A., Olson E.N., Jin Z.G.
      J. Biol. Chem. 283:14590-14599(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-259 AND SER-498.
    19. Cited for: INTERACTION WITH BAHD1.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases."
      Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B., McKinsey T.A.
      FEBS Lett. 584:1103-1110(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-292, MUTAGENESIS OF SER-259; SER-291 AND THR-292.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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.

    Entry informationi

    Entry nameiHDAC5_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQL6
    Secondary accession number(s): C9JFV9
    , O60340, O60528, Q96DY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 155 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3