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Q9UKV0

- HDAC9_HUMAN

UniProt

Q9UKV0 - HDAC9_HUMAN

Protein

Histone deacetylase 9

Gene

HDAC9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (18 Oct 2001)
      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. Represses MEF2-dependent transcription.
    Isoform 3 lacks active site residues and therefore is catalytically inactive. Represses MEF2-dependent transcription by recruiting HDAC1 and/or HDAC3. Seems to inhibit skeletal myogenesis and to be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter.

    Catalytic activityi

    Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

    Enzyme regulationi

    Inhibited by Trichostatin A (TSA) and suberoylanilide hydroxamic acid.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi646 – 6461ZincBy similarity
    Metal bindingi648 – 6481ZincBy similarity
    Metal bindingi654 – 6541ZincBy similarity
    Metal bindingi731 – 7311ZincBy similarity
    Active sitei783 – 7831By similarity

    GO - Molecular functioni

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

    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. heart development 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 transcription, DNA-templated Source: BHF-UCL
    10. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    11. Notch signaling pathway Source: Reactome
    12. peptidyl-lysine deacetylation Source: BHF-UCL
    13. positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
    14. regulation of skeletal muscle fiber development Source: UniProtKB
    15. regulation of striated muscle cell differentiation Source: UniProtKB
    16. 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 9 (EC:3.5.1.98)
    Short name:
    HD9
    Alternative name(s):
    Histone deacetylase 7B
    Short name:
    HD7
    Short name:
    HD7b
    Histone deacetylase-related protein
    MEF2-interacting transcription repressor MITR
    Gene namesi
    Name:HDAC9
    Synonyms:HDAC7, HDAC7B, HDRP, KIAA0744, MITR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:14065. HDAC9.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. histone deacetylase complex Source: UniProtKB
    3. histone methyltransferase complex Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving HDAC9 is found in a family with Peters anomaly. Translocation t(1;7)(q41;p21) with TGFB2 resulting in lack of HDAC9 protein.

    Organism-specific databases

    Orphaneti708. Peters anomaly.
    PharmGKBiPA38377.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10111011Histone deacetylase 9PRO_0000114710Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei22 – 221Phosphoserine2 Publications
    Modified residuei220 – 2201PhosphoserineBy similarity
    Modified residuei240 – 2401PhosphoserineBy similarity
    Modified residuei451 – 4511PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-binding, impairs interaction with MEF2, and antagonizes antimyogenic activity. Phosphorylated on Ser-240; which impairs nuclear accumulation By similarity. Isoform 7 is phosphorylated on Tyr-1010. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import.By similarity2 Publications
    Sumoylated.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UKV0.
    PaxDbiQ9UKV0.
    PRIDEiQ9UKV0.

    PTM databases

    PhosphoSiteiQ9UKV0.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in brain, heart, muscle and testis. Isoform 3 is present in human bladder carcinoma cells (at protein level).4 Publications

    Gene expression databases

    ArrayExpressiQ9UKV0.
    BgeeiQ9UKV0.
    CleanExiHS_HDAC7.
    HS_HDAC9.
    GenevestigatoriQ9UKV0.

    Organism-specific databases

    HPAiHPA028926.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CTBP1. The phosphorylated form interacts with 14-3-3 By similarity. Interacts with HDAC1 and HDAC3, and probably with HDAC4 and HDAC5. Interacts with MEF2, MAPK10, ETV6, NCOR1 and BCL6.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL6P411822EBI-765444,EBI-765407
    ETV6P412123EBI-765476,EBI-1372759
    Ncor1Q609743EBI-1372717,EBI-349004From a different organism.

    Protein-protein interaction databases

    BioGridi115083. 99 interactions.
    DIPiDIP-39904N.
    IntActiQ9UKV0. 28 interactions.
    MINTiMINT-205121.
    STRINGi9606.ENSP00000408617.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKV0.
    SMRiQ9UKV0. Positions 629-1005.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 275Interaction with CTBP1By similarity
    Regioni136 – 15419Interaction with MEF2By similarityAdd
    BLAST
    Regioni175 – 343169Interaction with MAPK10By similarityAdd
    BLAST
    Regioni218 – 26144Interaction with ETV6Add
    BLAST
    Regioni631 – 978348Histone deacetylaseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000232065.
    HOVERGENiHBG057100.
    InParanoidiQ9UKV0.
    KOiK11409.
    OMAiVEYLEAF.
    OrthoDBiEOG7RFTH5.
    PhylomeDBiQ9UKV0.
    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 (11)i

    Sequence statusi: Complete.

    This entry describes 11 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9UKV0-1) [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

    MHSMISSVDV KSEVPVGLEP ISPLDLRTDL RMMMPVVDPV VREKQLQQEL     50
    LLIQQQQQIQ KQLLIAEFQK QHENLTRQHQ AQLQEHIKEL LAIKQQQELL 100
    EKEQKLEQQR QEQEVERHRR EQQLPPLRGK DRGRERAVAS TEVKQKLQEF 150
    LLSKSATKDT PTNGKNHSVS RHPKLWYTAA HHTSLDQSSP PLSGTSPSYK 200
    YTLPGAQDAK DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGNV 250
    VTSFKKRMFE VTESSVSSSS PGSGPSSPNN GPTGSVTENE TSVLPPTPHA 300
    EQMVSQQRIL IHEDSMNLLS LYTSPSLPNI TLGLPAVPSQ LNASNSLKEK 350
    QKCETQTLRQ GVPLPGQYGG SIPASSSHPH VTLEGKPPNS SHQALLQHLL 400
    LKEQMRQQKL LVAGGVPLHP QSPLATKERI SPGIRGTHKL PRHRPLNRTQ 450
    SAPLPQSTLA QLVIQQQHQQ FLEKQKQYQQ QIHMNKLLSK SIEQLKQPGS 500
    HLEEAEEELQ GDQAMQEDRA PSSGNSTRSD SSACVDDTLG QVGAVKVKEE 550
    PVDSDEDAQI QEMESGEQAA FMQQPFLEPT HTRALSVRQA PLAAVGMDGL 600
    EKHRLVSRTH SSPAASVLPH PAMDRPLQPG SATGIAYDPL MLKHQCVCGN 650
    STTHPEHAGR IQSIWSRLQE TGLLNKCERI QGRKASLEEI QLVHSEHHSL 700
    LYGTNPLDGQ KLDPRILLGD DSQKFFSSLP CGGLGVDSDT IWNELHSSGA 750
    ARMAVGCVIE LASKVASGEL KNGFAVVRPP GHHAEESTAM GFCFFNSVAI 800
    TAKYLRDQLN ISKILIVDLD VHHGNGTQQA FYADPSILYI SLHRYDEGNF 850
    FPGSGAPNEV GTGLGEGYNI NIAWTGGLDP PMGDVEYLEA FRTIVKPVAK 900
    EFDPDMVLVS AGFDALEGHT PPLGGYKVTA KCFGHLTKQL MTLADGRVVL 950
    ALEGGHDLTA ICDASEACVN ALLGNELEPL AEDILHQSPN MNAVISLQKI 1000
    IEIQSMSLKF S 1011
    Length:1,011
    Mass (Da):111,297
    Last modified:October 18, 2001 - v2
    Checksum:i43ED2785E73CD924
    GO
    Isoform 2 (identifier: Q9UKV0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         487-574: Missing.

    Show »
    Length:923
    Mass (Da):101,805
    Checksum:i095F634F623A684F
    GO
    Isoform 3 (identifier: Q9UKV0-3) [UniParc]FASTAAdd to Basket

    Also known as: HDRP, MITR

    The sequence of this isoform differs from the canonical sequence as follows:
         575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
         591-1011: Missing.

    Note: Major form in most tissues. Inactive due to lack of active site residues.

    Show »
    Length:590
    Mass (Da):65,887
    Checksum:i02931057CF0E4C25
    GO
    Isoform 4 (identifier: Q9UKV0-4) [UniParc]FASTAAdd to Basket

    Also known as: HDAC9a

    The sequence of this isoform differs from the canonical sequence as follows:
         861-879: GTGLGEGYNINIAWTGGLD → RFISLEPHFYLYLSGNCIA
         880-1011: Missing.

    Show »
    Length:879
    Mass (Da):97,471
    Checksum:iD3BFC3CE99E817DB
    GO
    Isoform 5 (identifier: Q9UKV0-5) [UniParc]FASTAAdd to Basket

    Also known as: HDAC9b, HDAC9fl

    The sequence of this isoform differs from the canonical sequence as follows:
         1006-1011: MSLKFS → KYWKSVRMVAVPRGCALAGAQLQEETETVSALASLTVDVEQPFAQEDSRTAGEPMEEEPAL

    Note: Contains a phosphotyrosine at position 1007.Curated

    Show »
    Length:1,066
    Mass (Da):117,208
    Checksum:iEE7D908DF45D20CB
    GO
    Isoform 6 (identifier: Q9UKV0-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         88-88: K → KLQQ
         218-261: Missing.
         1006-1011: MSLKFS → KYWKSVRMVAVPRGCALAGAQLQEETETVSALASLTVDVEQPFAQEDSRTAGEPMEEEPAL

    Note: Contains a phosphotyrosine at position 966 (Probable). Excluded from the nucleus. Does not interact with ETV6..Curated

    Show »
    Length:1,025
    Mass (Da):112,451
    Checksum:i3BEFD662BF24E677
    GO
    Isoform 7 (identifier: Q9UKV0-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         88-88: K → KLQQ
         1006-1011: MSLKFS → KYWKSVRMVAVPRGCALAGAQLQEETETVSALASLTVDVEQPFAQEDSRTAGEPMEEEPAL

    Show »
    Length:1,069
    Mass (Da):117,577
    Checksum:i5DFBB8DD4C6547C5
    GO
    Isoform 8 (identifier: Q9UKV0-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MMSSPAQPDLMWNLVPWVLFCGCCRIFPDGVAGREQLLAQQRM
         218-261: Missing.
         575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
         591-1011: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:588
    Mass (Da):65,508
    Checksum:iE58854328ED1B5BE
    GO
    Isoform 9 (identifier: Q9UKV0-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         218-261: Missing.
         575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
         591-1011: Missing.

    Show »
    Length:546
    Mass (Da):60,761
    Checksum:iCFC8BA27CFD1AA31
    GO
    Isoform 10 (identifier: Q9UKV0-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: Missing.
         88-88: K → KLQQ
         575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
         591-1011: Missing.

    Show »
    Length:562
    Mass (Da):62,852
    Checksum:i6557FECB5FFF1A5A
    GO
    Isoform 11 (identifier: Q9UKV0-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: Missing.
         177-178: Missing.
         218-261: Missing.
         575-590: PFLEPTHTRALSVRQA → VIGKDLAPGFVIKVII
         591-1011: Missing.

    Show »
    Length:513
    Mass (Da):57,092
    Checksum:i3868A8C73426BCC2
    GO

    Sequence cautioni

    Isoform 6 : The sequence AAI11736.1 differs from that shown. Reason: Frameshift at position 1021.
    The sequence BAA34464.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161V → A in BAH12570. (PubMed:14702039)Curated
    Sequence conflicti99 – 991L → I in AAF04254. (PubMed:10523670)Curated
    Sequence conflicti153 – 1531S → I in BAH14164. (PubMed:14702039)Curated
    Sequence conflicti315 – 3151S → F in BAH14176. (PubMed:14702039)Curated
    Sequence conflicti332 – 3321L → M in BAH14164. (PubMed:14702039)Curated
    Sequence conflicti416 – 4161V → F in BAH14164. (PubMed:14702039)Curated
    Sequence conflicti437 – 4371T → P in AAF04254. (PubMed:10523670)Curated
    Sequence conflicti644 – 6474HQCV → KPNS in AAF04254. (PubMed:10523670)Curated
    Sequence conflicti746 – 7461H → R in AAO27363. (PubMed:12590135)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti921 – 9211P → T Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064719

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131Missing in isoform 10 and isoform 11. 1 PublicationVSP_046827Add
    BLAST
    Alternative sequencei1 – 11M → MMSSPAQPDLMWNLVPWVLF CGCCRIFPDGVAGREQLLAQ QRM in isoform 8. 1 PublicationVSP_043428
    Alternative sequencei88 – 881K → KLQQ in isoform 6, isoform 7 and isoform 10. 3 PublicationsVSP_023766
    Alternative sequencei177 – 1782Missing in isoform 11. 1 PublicationVSP_046828
    Alternative sequencei218 – 26144Missing in isoform 6, isoform 8, isoform 9 and isoform 11. 2 PublicationsVSP_023767Add
    BLAST
    Alternative sequencei487 – 57488Missing in isoform 2. 1 PublicationVSP_002082Add
    BLAST
    Alternative sequencei575 – 59016PFLEP…SVRQA → VIGKDLAPGFVIKVII in isoform 3, isoform 8, isoform 9, isoform 10 and isoform 11. 3 PublicationsVSP_002083Add
    BLAST
    Alternative sequencei591 – 1011421Missing in isoform 3, isoform 8, isoform 9, isoform 10 and isoform 11. 3 PublicationsVSP_002084Add
    BLAST
    Alternative sequencei861 – 87919GTGLG…TGGLD → RFISLEPHFYLYLSGNCIA in isoform 4. 1 PublicationVSP_002085Add
    BLAST
    Alternative sequencei880 – 1011132Missing in isoform 4. 1 PublicationVSP_002086Add
    BLAST
    Alternative sequencei1006 – 10116MSLKFS → KYWKSVRMVAVPRGCALAGA QLQEETETVSALASLTVDVE QPFAQEDSRTAGEPMEEEPA L in isoform 5, isoform 6 and isoform 7. 3 PublicationsVSP_023768

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY032737 mRNA. Translation: AAK66821.1.
    AY032738 mRNA. Translation: AAK66822.1.
    AJ459808 mRNA. Translation: CAD30851.1.
    AY197371 mRNA. Translation: AAO27363.1.
    AB018287 mRNA. Translation: BAA34464.2. Different initiation.
    AK297404 mRNA. Translation: BAH12570.1.
    AK304298 mRNA. Translation: BAH14153.1.
    AK304343 mRNA. Translation: BAH14164.1.
    AK304410 mRNA. Translation: BAH14176.1.
    AC002088 Genomic DNA. No translation available.
    AC002124 Genomic DNA. No translation available.
    AC002410 Genomic DNA. No translation available.
    AC002433 Genomic DNA. No translation available.
    AC004744 Genomic DNA. No translation available.
    AC004994 Genomic DNA. No translation available.
    AC005249 Genomic DNA. No translation available.
    AC010082 Genomic DNA. No translation available.
    AC074193 Genomic DNA. No translation available.
    AC091697 Genomic DNA. No translation available.
    CH471073 Genomic DNA. Translation: EAW93702.1.
    CH471073 Genomic DNA. Translation: EAW93703.1.
    BC111735 mRNA. Translation: AAI11736.1. Frameshift.
    BC150328 mRNA. Translation: AAI50329.1.
    BC152405 mRNA. Translation: AAI52406.1.
    AF124924 mRNA. Translation: AAF04254.1.
    CCDSiCCDS47553.1. [Q9UKV0-7]
    CCDS47554.1. [Q9UKV0-5]
    CCDS47555.1. [Q9UKV0-1]
    CCDS47557.1. [Q9UKV0-3]
    CCDS56465.1. [Q9UKV0-8]
    CCDS56466.1. [Q9UKV0-9]
    CCDS56467.1. [Q9UKV0-10]
    CCDS56468.1. [Q9UKV0-11]
    RefSeqiNP_001191073.1. NM_001204144.1. [Q9UKV0-8]
    NP_001191074.1. NM_001204145.1. [Q9UKV0-9]
    NP_001191075.1. NM_001204146.1.
    NP_001191076.1. NM_001204147.1. [Q9UKV0-11]
    NP_001191077.1. NM_001204148.1. [Q9UKV0-10]
    NP_055522.1. NM_014707.1. [Q9UKV0-3]
    NP_478056.1. NM_058176.2. [Q9UKV0-1]
    NP_848510.1. NM_178423.1. [Q9UKV0-5]
    NP_848512.1. NM_178425.2. [Q9UKV0-7]
    UniGeneiHs.196054.

    Genome annotation databases

    EnsembliENST00000401921; ENSP00000383912; ENSG00000048052. [Q9UKV0-6]
    ENST00000405010; ENSP00000384382; ENSG00000048052. [Q9UKV0-3]
    ENST00000406451; ENSP00000384657; ENSG00000048052. [Q9UKV0-5]
    ENST00000417496; ENSP00000401669; ENSG00000048052. [Q9UKV0-8]
    ENST00000428307; ENSP00000395655; ENSG00000048052. [Q9UKV0-9]
    ENST00000432645; ENSP00000410337; ENSG00000048052. [Q9UKV0-1]
    ENST00000441542; ENSP00000408617; ENSG00000048052. [Q9UKV0-7]
    ENST00000456174; ENSP00000388568; ENSG00000048052. [Q9UKV0-10]
    ENST00000524023; ENSP00000430036; ENSG00000048052. [Q9UKV0-11]
    GeneIDi9734.
    KEGGihsa:9734.
    UCSCiuc003sua.1. human. [Q9UKV0-6]
    uc003sud.2. human. [Q9UKV0-3]
    uc003sue.3. human. [Q9UKV0-5]
    uc003suf.2. human. [Q9UKV0-7]
    uc003suh.3. human. [Q9UKV0-1]
    uc011jya.2. human. [Q9UKV0-8]
    uc011jyd.2. human. [Q9UKV0-4]
    uc011jye.2. human.

    Polymorphism databases

    DMDMi19865267.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY032737 mRNA. Translation: AAK66821.1 .
    AY032738 mRNA. Translation: AAK66822.1 .
    AJ459808 mRNA. Translation: CAD30851.1 .
    AY197371 mRNA. Translation: AAO27363.1 .
    AB018287 mRNA. Translation: BAA34464.2 . Different initiation.
    AK297404 mRNA. Translation: BAH12570.1 .
    AK304298 mRNA. Translation: BAH14153.1 .
    AK304343 mRNA. Translation: BAH14164.1 .
    AK304410 mRNA. Translation: BAH14176.1 .
    AC002088 Genomic DNA. No translation available.
    AC002124 Genomic DNA. No translation available.
    AC002410 Genomic DNA. No translation available.
    AC002433 Genomic DNA. No translation available.
    AC004744 Genomic DNA. No translation available.
    AC004994 Genomic DNA. No translation available.
    AC005249 Genomic DNA. No translation available.
    AC010082 Genomic DNA. No translation available.
    AC074193 Genomic DNA. No translation available.
    AC091697 Genomic DNA. No translation available.
    CH471073 Genomic DNA. Translation: EAW93702.1 .
    CH471073 Genomic DNA. Translation: EAW93703.1 .
    BC111735 mRNA. Translation: AAI11736.1 . Frameshift.
    BC150328 mRNA. Translation: AAI50329.1 .
    BC152405 mRNA. Translation: AAI52406.1 .
    AF124924 mRNA. Translation: AAF04254.1 .
    CCDSi CCDS47553.1. [Q9UKV0-7 ]
    CCDS47554.1. [Q9UKV0-5 ]
    CCDS47555.1. [Q9UKV0-1 ]
    CCDS47557.1. [Q9UKV0-3 ]
    CCDS56465.1. [Q9UKV0-8 ]
    CCDS56466.1. [Q9UKV0-9 ]
    CCDS56467.1. [Q9UKV0-10 ]
    CCDS56468.1. [Q9UKV0-11 ]
    RefSeqi NP_001191073.1. NM_001204144.1. [Q9UKV0-8 ]
    NP_001191074.1. NM_001204145.1. [Q9UKV0-9 ]
    NP_001191075.1. NM_001204146.1.
    NP_001191076.1. NM_001204147.1. [Q9UKV0-11 ]
    NP_001191077.1. NM_001204148.1. [Q9UKV0-10 ]
    NP_055522.1. NM_014707.1. [Q9UKV0-3 ]
    NP_478056.1. NM_058176.2. [Q9UKV0-1 ]
    NP_848510.1. NM_178423.1. [Q9UKV0-5 ]
    NP_848512.1. NM_178425.2. [Q9UKV0-7 ]
    UniGenei Hs.196054.

    3D structure databases

    ProteinModelPortali Q9UKV0.
    SMRi Q9UKV0. Positions 629-1005.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115083. 99 interactions.
    DIPi DIP-39904N.
    IntActi Q9UKV0. 28 interactions.
    MINTi MINT-205121.
    STRINGi 9606.ENSP00000408617.

    Chemistry

    BindingDBi Q9UKV0.
    ChEMBLi CHEMBL2093865.
    DrugBanki DB00313. Valproic Acid.
    GuidetoPHARMACOLOGYi 2620.

    PTM databases

    PhosphoSitei Q9UKV0.

    Polymorphism databases

    DMDMi 19865267.

    Proteomic databases

    MaxQBi Q9UKV0.
    PaxDbi Q9UKV0.
    PRIDEi Q9UKV0.

    Protocols and materials databases

    DNASUi 9734.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000401921 ; ENSP00000383912 ; ENSG00000048052 . [Q9UKV0-6 ]
    ENST00000405010 ; ENSP00000384382 ; ENSG00000048052 . [Q9UKV0-3 ]
    ENST00000406451 ; ENSP00000384657 ; ENSG00000048052 . [Q9UKV0-5 ]
    ENST00000417496 ; ENSP00000401669 ; ENSG00000048052 . [Q9UKV0-8 ]
    ENST00000428307 ; ENSP00000395655 ; ENSG00000048052 . [Q9UKV0-9 ]
    ENST00000432645 ; ENSP00000410337 ; ENSG00000048052 . [Q9UKV0-1 ]
    ENST00000441542 ; ENSP00000408617 ; ENSG00000048052 . [Q9UKV0-7 ]
    ENST00000456174 ; ENSP00000388568 ; ENSG00000048052 . [Q9UKV0-10 ]
    ENST00000524023 ; ENSP00000430036 ; ENSG00000048052 . [Q9UKV0-11 ]
    GeneIDi 9734.
    KEGGi hsa:9734.
    UCSCi uc003sua.1. human. [Q9UKV0-6 ]
    uc003sud.2. human. [Q9UKV0-3 ]
    uc003sue.3. human. [Q9UKV0-5 ]
    uc003suf.2. human. [Q9UKV0-7 ]
    uc003suh.3. human. [Q9UKV0-1 ]
    uc011jya.2. human. [Q9UKV0-8 ]
    uc011jyd.2. human. [Q9UKV0-4 ]
    uc011jye.2. human.

    Organism-specific databases

    CTDi 9734.
    GeneCardsi GC07P018179.
    HGNCi HGNC:14065. HDAC9.
    HPAi HPA028926.
    MIMi 606543. gene.
    neXtProti NX_Q9UKV0.
    Orphaneti 708. Peters anomaly.
    PharmGKBi PA38377.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000232065.
    HOVERGENi HBG057100.
    InParanoidi Q9UKV0.
    KOi K11409.
    OMAi VEYLEAF.
    OrthoDBi EOG7RFTH5.
    PhylomeDBi Q9UKV0.
    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

    GeneWikii HDAC9.
    GenomeRNAii 9734.
    NextBioi 36620.
    PROi Q9UKV0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKV0.
    Bgeei Q9UKV0.
    CleanExi HS_HDAC7.
    HS_HDAC9.
    Genevestigatori Q9UKV0.

    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. "Cloning and characterization of a histone deacetylase, HDAC9."
      Zhou X., Marks P.A., Rifkind R.A., Richon V.M.
      Proc. Natl. Acad. Sci. U.S.A. 98:10572-10577(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), TISSUE SPECIFICITY, INTERACTION WITH MEF2, FUNCTION, ENZYME REGULATION.
      Tissue: Brain.
    2. "Molecular characterization of a familial translocation implicates disruption of HDAC9 and possible position effect on TGFbeta2 in the pathogenesis of Peters' anomaly."
      David D., Cardoso J., Marques B., Marques R., Silva E.D., Santos H., Boavida M.G.
      Genomics 81:489-503(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH TGFB2.
      Tissue: Lens.
    3. "The histone deacetylase 9 gene encodes multiple protein isoforms."
      Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M., Zelent A.
      J. Biol. Chem. 278:16059-16072(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 3; 6 AND 7), INTERACTION WITH ETV6; NCOR1 AND BCL6, FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION.
      Tissue: Brain.
    4. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8; 9; 10 AND 11).
      Tissue: Brain and Trachea.
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1011 (ISOFORM 6).
    9. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 99-650 (ISOFORM 2).
      Tissue: Brain.
    10. Cited for: IDENTIFICATION (ISOFORM 3), INTERACTION WITH HDAC1, FUNCTION.
    11. "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: IDENTIFICATION (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH HDAC1 AND HDAC3, FUNCTION.
    12. "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: INTERACTION WITH MEF2.
    13. Cited for: SUMOYLATION.
    14. Cited for: FUNCTION.
    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-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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.
    17. Cited for: VARIANT THR-921.

    Entry informationi

    Entry nameiHDAC9_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKV0
    Secondary accession number(s): A7E2F3
    , B7Z4I4, B7Z917, B7Z928, B7Z940, C9JS87, E7EX34, F8W9E0, O94845, O95028, Q2M2R6, Q86SL1, Q86US3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 148 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 7
      Human chromosome 7: 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