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Q8C2B3

- HDAC7_MOUSE

UniProt

Q8C2B3 - HDAC7_MOUSE

Protein

Histone deacetylase 7

Gene

Hdac7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      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 factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors.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 bindingi520 – 5201ZincBy similarity
    Metal bindingi522 – 5221ZincBy similarity
    Metal bindingi528 – 5281ZincBy similarity
    Metal bindingi605 – 6051ZincBy similarity
    Active sitei657 – 6571By similarity
    Sitei830 – 8301Contributes to catalysisBy similarity

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: UniProtKB
    2. chromatin binding Source: MGI
    3. histone deacetylase activity Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    7. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    8. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    9. protein binding Source: IntAct
    10. transcription corepressor activity Source: MGI
    11. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. B cell activation Source: UniProtKB
    2. B cell differentiation Source: UniProtKB
    3. cell-cell junction assembly Source: MGI
    4. chromatin modification Source: UniProtKB
    5. histone deacetylation Source: GOC
    6. inflammatory response Source: UniProtKB
    7. negative regulation of interleukin-2 production Source: Ensembl
    8. negative regulation of osteoblast differentiation Source: Ensembl
    9. negative regulation of striated muscle tissue development Source: UniProtKB
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    12. nervous system development Source: UniProtKB
    13. positive regulation of cell migration involved in sprouting angiogenesis Source: Ensembl
    14. transcription, DNA-templated Source: UniProtKB-KW
    15. vasculogenesis Source: MGI

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 7 (EC:3.5.1.98)
    Short name:
    HD7
    Alternative name(s):
    Histone deacetylase 7A
    Short name:
    HD7a
    Gene namesi
    Name:Hdac7
    Synonyms:Hdac7a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1891835. Hdac7.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: In the nucleus, it associates with distinct subnuclear dot-like structures. 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 the 14-3-3 protein YWHAE and is due to its phosphorylation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. histone deacetylase complex Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi178 – 1781S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. 1 Publication
    Mutagenesisi344 – 3441S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. 1 Publication
    Mutagenesisi479 – 4791S → A: Strong reduction of CaMK1-dependent nuclear export. Reduces interaction with YWHAE. 1 Publication
    Mutagenesisi657 – 6571H → A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. 2 Publications
    Mutagenesisi692 – 6921D → A: Disrupts the dot-like nuclear pattern. 1 Publication
    Mutagenesisi694 – 6941D → A: Disrupts the dot-like nuclear pattern. Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. 1 Publication
    Mutagenesisi717 – 7171H → A: Abolishes deacetylase activity, but not the interaction with HDAC2 and HDAC3. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 938938Histone deacetylase 7PRO_0000114706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei132 – 1321PhosphoserineBy similarity
    Modified residuei178 – 1781Phosphoserine; by MARK2, MARK3 and PKD/PRKD12 Publications
    Modified residuei204 – 2041Phosphoserine; by PKD/PRKD2By similarity
    Modified residuei344 – 3441Phosphoserine; by PKD/PRKD12 Publications
    Modified residuei479 – 4791Phosphoserine; by PKD/PRKD12 Publications

    Post-translational modificationi

    May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-178 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-178 is a prerequisite for phosphorylation at Ser-204 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8C2B3.
    PRIDEiQ8C2B3.

    PTM databases

    PhosphoSiteiQ8C2B3.

    Miscellaneous databases

    PMAP-CutDBQ8C2B3.

    Expressioni

    Tissue specificityi

    Highly expressed in heart and lung. Expressed at intermediate level in muscle.2 Publications

    Gene expression databases

    ArrayExpressiQ8C2B3.
    BgeeiQ8C2B3.
    CleanExiMM_HDAC7.
    GenevestigatoriQ8C2B3.

    Interactioni

    Subunit structurei

    Interacts with KDM5B By similarity. Interacts with KAT5 and EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C. Interacts with ZMYND15. Interacts with PML By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YwhaeP622596EBI-643830,EBI-356480

    Protein-protein interaction databases

    BioGridi207862. 5 interactions.
    DIPiDIP-42594N.
    IntActiQ8C2B3. 4 interactions.
    MINTiMINT-1551781.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C2B3.
    SMRiQ8C2B3. Positions 507-887.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 121121Interaction with MEF2CAdd
    BLAST
    Regioni2 – 254253Transcription repression 1Add
    BLAST
    Regioni72 – 172101Interaction with MEF2AAdd
    BLAST
    Regioni241 – 533293Transcription repression 2Add
    BLAST
    Regioni505 – 852348Histone deacetylaseAdd
    BLAST
    Regioni864 – 93875Interaction with SIN3AAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi904 – 93835Nuclear export signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi220 – 2267Poly-Ser

    Domaini

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

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0123.
    GeneTreeiENSGT00530000062809.
    HOGENOMiHOG000232065.
    HOVERGENiHBG057100.
    KOiK11408.
    OMAiAFRIVVM.
    OrthoDBiEOG7RFTH5.
    PhylomeDBiQ8C2B3.
    TreeFamiTF106173.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSiPR01270. HDASUPER.

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8C2B3-1) [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

    MHSPGAGCPA LQPDTPGSQP QPMDLRVGQR PTVEPPPEPA LLTLQHPQRL    50
    HRHLFLAGLH QQQRSAEPMR LSMDPPMPEL QGGQQEQELR QLLNKDKSKR 100
    SAVASSVVKQ KLAEVILKKQ QAALERTVHP SSPSIPYRTL EPLDTEGAAR 150
    SVLSSFLPPV PSLPTEPPEH FPLRKTVSEP NLKLRYKPKK SLERRKNPLL 200
    RKESAPPSLR RRPAETLGDS SPSSSSTPAS GCSSPNDSEH GPNPALGSEA 250
    DGDRRTHSTL GPRGPVLGNP HAPLFLHHGL EPEAGGTLPS RLQPILLLDP 300
    SVSHAPLWTV PGLGPLPFHF AQPLLTTERL SGSGLHRPLN RTRSEPLPPS 350
    ATASPLLAPL QPRQDRLKPH VQLIKPAISP PQRPAKPSEK PRLRQIPSAE 400
    DLETDGGGVG PMANDGLEHR ESGRGPPEGR GSISLQQHQQ VPPWEQQHLA 450
    GRLSQGSPGD SVLIPLAQVG HRPLSRTQSS PAAPVSLLSP EPTCQTQVLN 500
    SSETPATGLV YDSVMLKHQC SCGDNSKHPE HAGRIQSIWS RLQERGLRSQ 550
    CECLRGRKAS LEELQSVHSE RHVLLYGTNP LSRLKLDNGK LTGLLAQRTF 600
    VMLPCGGVGV DTDTIWNELH SSNAARWAAG SVTDLAFKVA SRELKNGFAV 650
    VRPPGHHADH STAMGFCFFN SVAIACRQLQ QHGKASKILI VDWDVHHGNG 700
    TQQTFYQDPS VLYISLHRHD DGNFFPGSGA VDEVGTGSGE GFNVNVAWAG 750
    GLDPPMGDPE YLAAFRIVVM PIAREFAPDL VLVSAGFDAA EGHPAPLGGY 800
    HVSAKCFGYM TQQLMNLAGG AVVLALEGGH DLTAICDASE ACVAALLGNK 850
    VDPLSEESWK QKPNLSAIRS LEAVVRVHRK YWGCMQRLAS CPDSWLPRVP 900
    GADAEVEAVT ALASLSVGIL AEDRPSERLV EEEEPMNL 938
    Length:938
    Mass (Da):101,287
    Last modified:May 16, 2003 - v2
    Checksum:i8D4B455CE6F95483
    GO
    Isoform 2 (identifier: Q8C2B3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: Missing.
         249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR
         376-382: Missing.

    Show »
    Length:946
    Mass (Da):102,289
    Checksum:i035DE255A4F44F7E
    GO
    Isoform 3 (identifier: Q8C2B3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: Missing.
         249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR

    Show »
    Length:953
    Mass (Da):102,980
    Checksum:i4D87C0E22274202C
    GO
    Isoform 4 (identifier: Q8C2B3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-161: Missing.
         249-249: E → EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR
         376-382: Missing.

    Show »
    Length:944
    Mass (Da):101,910
    Checksum:i5DD4D8F2A30A8C16
    GO
    Isoform 5 (identifier: Q8C2B3-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: Missing.

    Show »
    Length:916
    Mass (Da):99,131
    Checksum:i1586B7308A24964A
    GO
    Isoform 6 (identifier: Q8C2B3-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-161: Missing.

    Show »
    Length:914
    Mass (Da):98,752
    Checksum:i23AD714981D53FC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti169 – 1691E → G in BAC27161. (PubMed:16141072)Curated
    Sequence conflicti183 – 1831K → M in BAC29493. (PubMed:16141072)Curated
    Sequence conflicti228 – 2281P → T in BAC27161. (PubMed:16141072)Curated
    Sequence conflicti487 – 4871L → M in AAF31419. (PubMed:10640276)Curated
    Sequence conflicti487 – 4871L → M in BAC40598. (PubMed:16141072)Curated
    Sequence conflicti487 – 4871L → M in BAC40666. (PubMed:16141072)Curated
    Sequence conflicti645 – 6451K → R in BAC29493. (PubMed:16141072)Curated
    Sequence conflicti661 – 6611S → P in BAC40598. (PubMed:16141072)Curated
    Sequence conflicti737 – 7371G → A in AAF31419. (PubMed:10640276)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2222Missing in isoform 2, isoform 3 and isoform 5. 1 PublicationVSP_007432Add
    BLAST
    Alternative sequencei138 – 16124Missing in isoform 4 and isoform 6. 1 PublicationVSP_007433Add
    BLAST
    Alternative sequencei249 – 2491E → EALLGQRLRLQETSLAPFAL PTVSLLPAITLGLPAPAR in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_007434
    Alternative sequencei376 – 3827Missing in isoform 2 and isoform 4. 1 PublicationVSP_007435

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF207749 mRNA. Translation: AAF31419.1.
    AK030863 mRNA. Translation: BAC27161.1.
    AK036586 mRNA. Translation: BAC29493.1.
    AK044287 mRNA. Translation: BAC31856.1.
    AK088828 mRNA. Translation: BAC40598.1.
    AK088945 mRNA. Translation: BAC40666.1.
    BC057332 mRNA. Translation: AAH57332.1.
    CCDSiCCDS37188.1. [Q8C2B3-1]
    CCDS57004.1. [Q8C2B3-5]
    CCDS57005.1. [Q8C2B3-2]
    CCDS57006.1. [Q8C2B3-3]
    CCDS57007.1. [Q8C2B3-4]
    RefSeqiNP_001191204.1. NM_001204275.1. [Q8C2B3-3]
    NP_001191205.1. NM_001204276.1. [Q8C2B3-2]
    NP_001191206.1. NM_001204277.1. [Q8C2B3-4]
    NP_001191207.1. NM_001204278.1. [Q8C2B3-5]
    NP_062518.2. NM_019572.3. [Q8C2B3-1]
    XP_006521268.1. XM_006521205.1.
    XP_006521269.1. XM_006521206.1. [Q8C2B3-3]
    XP_006521270.1. XM_006521207.1. [Q8C2B3-3]
    XP_006521271.1. XM_006521208.1. [Q8C2B3-3]
    XP_006521272.1. XM_006521209.1. [Q8C2B3-3]
    XP_006521273.1. XM_006521210.1. [Q8C2B3-3]
    UniGeneiMm.384027.

    Genome annotation databases

    EnsembliENSMUST00000079838; ENSMUSP00000078766; ENSMUSG00000022475. [Q8C2B3-4]
    ENSMUST00000088402; ENSMUSP00000085744; ENSMUSG00000022475. [Q8C2B3-1]
    ENSMUST00000116408; ENSMUSP00000112109; ENSMUSG00000022475. [Q8C2B3-5]
    ENSMUST00000116409; ENSMUSP00000112110; ENSMUSG00000022475. [Q8C2B3-3]
    ENSMUST00000118294; ENSMUSP00000113380; ENSMUSG00000022475. [Q8C2B3-2]
    GeneIDi56233.
    KEGGimmu:56233.
    UCSCiuc007xle.2. mouse. [Q8C2B3-1]
    uc007xlf.2. mouse. [Q8C2B3-2]
    uc007xlg.2. mouse. [Q8C2B3-4]
    uc007xlh.2. mouse. [Q8C2B3-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF207749 mRNA. Translation: AAF31419.1 .
    AK030863 mRNA. Translation: BAC27161.1 .
    AK036586 mRNA. Translation: BAC29493.1 .
    AK044287 mRNA. Translation: BAC31856.1 .
    AK088828 mRNA. Translation: BAC40598.1 .
    AK088945 mRNA. Translation: BAC40666.1 .
    BC057332 mRNA. Translation: AAH57332.1 .
    CCDSi CCDS37188.1. [Q8C2B3-1 ]
    CCDS57004.1. [Q8C2B3-5 ]
    CCDS57005.1. [Q8C2B3-2 ]
    CCDS57006.1. [Q8C2B3-3 ]
    CCDS57007.1. [Q8C2B3-4 ]
    RefSeqi NP_001191204.1. NM_001204275.1. [Q8C2B3-3 ]
    NP_001191205.1. NM_001204276.1. [Q8C2B3-2 ]
    NP_001191206.1. NM_001204277.1. [Q8C2B3-4 ]
    NP_001191207.1. NM_001204278.1. [Q8C2B3-5 ]
    NP_062518.2. NM_019572.3. [Q8C2B3-1 ]
    XP_006521268.1. XM_006521205.1.
    XP_006521269.1. XM_006521206.1. [Q8C2B3-3 ]
    XP_006521270.1. XM_006521207.1. [Q8C2B3-3 ]
    XP_006521271.1. XM_006521208.1. [Q8C2B3-3 ]
    XP_006521272.1. XM_006521209.1. [Q8C2B3-3 ]
    XP_006521273.1. XM_006521210.1. [Q8C2B3-3 ]
    UniGenei Mm.384027.

    3D structure databases

    ProteinModelPortali Q8C2B3.
    SMRi Q8C2B3. Positions 507-887.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207862. 5 interactions.
    DIPi DIP-42594N.
    IntActi Q8C2B3. 4 interactions.
    MINTi MINT-1551781.

    Chemistry

    BindingDBi Q8C2B3.

    PTM databases

    PhosphoSitei Q8C2B3.

    Proteomic databases

    PaxDbi Q8C2B3.
    PRIDEi Q8C2B3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000079838 ; ENSMUSP00000078766 ; ENSMUSG00000022475 . [Q8C2B3-4 ]
    ENSMUST00000088402 ; ENSMUSP00000085744 ; ENSMUSG00000022475 . [Q8C2B3-1 ]
    ENSMUST00000116408 ; ENSMUSP00000112109 ; ENSMUSG00000022475 . [Q8C2B3-5 ]
    ENSMUST00000116409 ; ENSMUSP00000112110 ; ENSMUSG00000022475 . [Q8C2B3-3 ]
    ENSMUST00000118294 ; ENSMUSP00000113380 ; ENSMUSG00000022475 . [Q8C2B3-2 ]
    GeneIDi 56233.
    KEGGi mmu:56233.
    UCSCi uc007xle.2. mouse. [Q8C2B3-1 ]
    uc007xlf.2. mouse. [Q8C2B3-2 ]
    uc007xlg.2. mouse. [Q8C2B3-4 ]
    uc007xlh.2. mouse. [Q8C2B3-3 ]

    Organism-specific databases

    CTDi 51564.
    MGIi MGI:1891835. Hdac7.

    Phylogenomic databases

    eggNOGi COG0123.
    GeneTreei ENSGT00530000062809.
    HOGENOMi HOG000232065.
    HOVERGENi HBG057100.
    KOi K11408.
    OMAi AFRIVVM.
    OrthoDBi EOG7RFTH5.
    PhylomeDBi Q8C2B3.
    TreeFami TF106173.

    Enzyme and pathway databases

    Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

    Miscellaneous databases

    ChiTaRSi HDAC7. mouse.
    NextBioi 312136.
    PMAP-CutDB Q8C2B3.
    PROi Q8C2B3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C2B3.
    Bgeei Q8C2B3.
    CleanExi MM_HDAC7.
    Genevestigatori Q8C2B3.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSi PR01270. HDASUPER.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression."
      Kao H.-Y., Downes M., Ordentlich P., Evans R.M.
      Genes Dev. 14:55-66(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NCOR2 AND SIN3A.
      Strain: C57BL/6.
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6).
      Strain: C57BL/6J and NOD.
      Tissue: Bone, Retina and Thymus.
    3. "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).
      Strain: C57BL/6.
      Tissue: Brain.
    4. Cited for: INTERACTION WITH HDAC1; HDAC2; HDAC3; HDAC4; HDAC5; NCOR1; NCOR2; SIN3A; SIN3B; RBBP4; RBBP7; MTA1L1; SAP30 AND MBD3, MUTAGENESIS OF HIS-657; ASP-692; ASP-694 AND HIS-717.
    5. "A dynamic role for HDAC7 in MEF2-mediated muscle differentiation."
      Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M., Muscat G.E.O.
      J. Biol. Chem. 276:17007-17013(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MEF2C, MUTAGENESIS OF HIS-657.
    6. "Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7."
      Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.
      J. Biol. Chem. 276:47496-47507(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH YWHAE; MEF2A; MEF2B AND MEF2C, MUTAGENESIS OF SER-178; SER-344 AND SER-479.
    7. "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.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7."
      Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.
      Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-178; SER-344 AND SER-479.
    10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor essential for spermiogenesis and male fertility."
      Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A., Saunders L., Verdin E., Charo I.F.
      J. Biol. Chem. 285:31418-31426(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZMYND15.

    Entry informationi

    Entry nameiHDAC7_MOUSE
    AccessioniPrimary (citable) accession number: Q8C2B3
    Secondary accession number(s): Q8C2C9
    , Q8C8X4, Q8CB80, Q8CDA3, Q9JL72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: May 16, 2003
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3