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Q9Z2V5

- HDAC6_MOUSE

UniProt

Q9Z2V5 - HDAC6_MOUSE

Protein

Histone deacetylase 6

Gene

Hdac6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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 By similarity. Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin.By similarity2 Publications
    In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 3 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei215 – 21511By similarity
    Active sitei610 – 61012By similarity
    Metal bindingi1047 – 10471Zinc 1By similarity
    Metal bindingi1049 – 10491Zinc 1By similarity
    Metal bindingi1067 – 10671Zinc 3By similarity
    Metal bindingi1070 – 10701Zinc 3By similarity
    Metal bindingi1079 – 10791Zinc 2By similarity
    Metal bindingi1082 – 10821Zinc 2By similarity
    Metal bindingi1087 – 10871Zinc 3By similarity
    Metal bindingi1094 – 10941Zinc 3By similarity
    Metal bindingi1098 – 10981Zinc 2By similarity
    Metal bindingi1104 – 11041Zinc 2By similarity
    Metal bindingi1117 – 11171Zinc 1By similarity
    Metal bindingi1120 – 11201Zinc 1By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1065 – 112662UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. beta-tubulin binding Source: MGI
    2. histone deacetylase activity Source: MGI
    3. microtubule binding Source: UniProtKB
    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: UniProtKB
    9. tubulin deacetylase activity Source: UniProtKB
    10. ubiquitin binding Source: MGI
    11. zinc ion binding Source: InterPro

    GO - Biological processi

    1. aggresome assembly Source: MGI
    2. cellular response to hydrogen peroxide Source: Ensembl
    3. cellular response to misfolded protein Source: MGI
    4. Hsp90 deacetylation Source: MGI
    5. lysosome localization Source: Ensembl
    6. macroautophagy Source: Ensembl
    7. misfolded or incompletely synthesized protein catabolic process Source: Ensembl
    8. negative regulation of microtubule depolymerization Source: MGI
    9. negative regulation of proteolysis Source: Ensembl
    10. peptidyl-lysine deacetylation Source: Ensembl
    11. polyubiquitinated misfolded protein transport Source: Ensembl
    12. positive regulation of chaperone-mediated protein complex assembly Source: Ensembl
    13. positive regulation of epithelial cell migration Source: Ensembl
    14. positive regulation of hydrogen peroxide-mediated programmed cell death Source: Ensembl
    15. positive regulation of receptor biosynthetic process Source: Ensembl
    16. positive regulation of signal transduction Source: Ensembl
    17. protein complex disassembly Source: MGI
    18. protein deacetylation Source: MGI
    19. protein polyubiquitination Source: MGI
    20. regulation of establishment of protein localization Source: MGI
    21. regulation of fat cell differentiation Source: MGI
    22. regulation of receptor activity Source: Ensembl
    23. regulation of transcription, DNA-templated Source: UniProtKB-KW
    24. response to growth factor Source: Ensembl
    25. response to toxic substance Source: Ensembl
    26. transcription, DNA-templated Source: UniProtKB-KW
    27. tubulin deacetylation Source: UniProtKB
    28. ubiquitin-dependent protein catabolic process Source: MGI
    29. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: MGI

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Actin-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_225256. HSF1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 6 (EC:3.5.1.98)
    Short name:
    HD6
    Alternative name(s):
    Histone deacetylase mHDA2
    Gene namesi
    Name:Hdac6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1333752. Hdac6.

    Subcellular locationi

    Nucleus. Cytoplasm. Perikaryon. Cell projectiondendrite. Cell projectionaxon
    Note: It is mainly cytoplasmic, where it is associated with microtubules.

    GO - Cellular componenti

    1. aggresome Source: Ensembl
    2. axon Source: UniProtKB
    3. caveola Source: Ensembl
    4. cell leading edge Source: Ensembl
    5. cytoplasm Source: MGI
    6. cytosol Source: UniProtKB
    7. dendrite Source: UniProtKB
    8. dynein complex Source: Ensembl
    9. histone deacetylase complex Source: Ensembl
    10. microtubule Source: Ensembl
    11. nucleus Source: UniProtKB
    12. perikaryon Source: UniProtKB
    13. perinuclear region of cytoplasm Source: Ensembl
    14. protein complex Source: MGI

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11491149Histone deacetylase 6PRO_0000114704Add
    BLAST

    Post-translational modificationi

    Phosphorylated by AURKA.By similarity
    Ubiquitinated. Its polyubiquitination however does not lead to its degradation By similarity.By similarity
    Sumoylated in vitro.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Z2V5.
    PaxDbiQ9Z2V5.
    PRIDEiQ9Z2V5.

    PTM databases

    PhosphoSiteiQ9Z2V5.

    Expressioni

    Tissue specificityi

    Expressed in neurons of the cortex. Expressed in Purkinje cells. Detected in keratinocytes (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ9Z2V5.
    BgeeiQ9Z2V5.
    CleanExiMM_HDAC6.
    GenevestigatoriQ9Z2V5.

    Interactioni

    Subunit structurei

    Interacts with BBIP10, DDIT3/CHOP, F-actin and HDAC11. Interacts with SIRT2 (via both phosphorylated, unphosphorylated, active or inactive forms); the interaction is necessary for the complex to interact with alpha-tubulin. Under proteasome impairment conditions, interacts with UBD via its histone deacetylase 1 and UBP-type zinc-finger regions By similarity. Interacts with CBFA2T3, CYLD and ZMYND15.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADRBK1P211462EBI-1009256,EBI-1036401From a different organism.
    CyldQ80TQ23EBI-1009256,EBI-943859

    Protein-protein interaction databases

    BioGridi200263. 16 interactions.
    IntActiQ9Z2V5. 8 interactions.
    MINTiMINT-220628.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2V5.
    SMRiQ9Z2V5. Positions 1043-1144.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni87 – 403317Histone deacetylase 1Add
    BLAST
    Regioni481 – 799319Histone deacetylase 2Add
    BLAST
    Regioni1088 – 10903Ubiquitin bindingBy similarity
    Regioni1116 – 11238Ubiquitin bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi455 – 4606Poly-Glu

    Sequence similaritiesi

    Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1065 – 112662UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0123.
    GeneTreeiENSGT00530000062809.
    HOGENOMiHOG000004769.
    HOVERGENiHBG051894.
    KOiK11407.
    OMAiLQENWVC.
    OrthoDBiEOG7992PT.
    TreeFamiTF106173.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.40.800.20. 2 hits.
    InterProiIPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF00850. Hist_deacetyl. 2 hits.
    PF02148. zf-UBP. 1 hit.
    [Graphical view]
    PRINTSiPR01270. HDASUPER.
    SMARTiSM00290. ZnF_UBP. 1 hit.
    [Graphical view]
    PROSITEiPS50271. ZF_UBP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Z2V5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSTGQDSST RQRKSRHNPQ SPLQESSATL KRGGKKCAVP HSSPNLAEVK     50
    KKGKMKKLSQ PAEEDLVVGL QGLDLNPETR VPVGTGLVFD EQLNDFHCLW 100
    DDSFPESPER LHAIREQLIL EGLLGRCVSF QARFAEKEEL MLVHSLEYID 150
    LMETTQYMNE GELRVLAETY DSVYLHPNSY SCACLATGSV LRLVDALMGA 200
    EIRNGMAVIR PPGHHAQHNL MDGYCMFNHL AVAARYAQKK HRIQRVLIVD 250
    WDVHHGQGTQ FIFDQDPSVL YFSIHRYEHG RFWPHLKASN WSTIGFGQGQ 300
    GYTINVPWNQ TGMRDADYIA AFLHILLPVA SEFQPQLVLV AAGFDALHGD 350
    PKGEMAATPA GFAHLTHLLM GLAGGKLILS LEGGYNLRAL AKGVSASLHT 400
    LLGDPCPMLE SCVVPCASAQ TSIYCTLEAL EPFWEVLERS VETQEEDEVE 450
    EAVLEEEEEE GGWEATALPM DTWPLLQNRT GLVYDEKMMS HCNLWDNHHP 500
    ETPQRILRIM CHLEEVGLAA RCLILPARPA LDSELLTCHS AEYVEHLRTT 550
    EKMKTRDLHR EGANFDSIYI CPSTFACAKL ATGAACRLVE AVLSGEVLNG 600
    IAVVRPPGHH AEPNAACGFC FFNSVAVAAR HAQIIAGRAL RILIVDWDVH 650
    HGNGTQHIFE DDPSVLYVSL HRYDRGTFFP MGDEGASSQV GRDAGIGFTV 700
    NVPWNGPRMG DADYLAAWHR LVLPIAYEFN PELVLISAGF DAAQGDPLGG 750
    CQVTPEGYAH LTHLLMGLAG GRIILILEGG YNLASISESM AACTHSLLGD 800
    PPPQLTLLRP PQSGALVSIS EVIQVHRKYW RSLRLMKMED KEECSSSRLV 850
    IKKLPPTASP VSAKEMTTPK GKVPEESVRK TIAALPGKES TLGQAKSKMA 900
    KAVLAQGQSS EQAAKGTTLD LATSKETVGG ATTDLWASAA APENFPNQTT 950
    SVEALGETEP TPPASHTNKQ TTGASPLQGV TAQQSLQLGV LSTLELSREA 1000
    EEAHDSEEGL LGEAAGGQDM NSLMLTQGFG DFNTQDVFYA VTPLSWCPHL 1050
    MAVCPIPAAG LDVSQPCKTC GTVQENWVCL TCYQVYCSRY VNAHMVCHHE 1100
    ASEHPLVLSC VDLSTWCYVC QAYVHHEDLQ DVKNAAHQNK FGEDMPHSH 1149
    Length:1,149
    Mass (Da):125,787
    Last modified:July 27, 2011 - v3
    Checksum:iD5F73BA3F79AF520
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331R → W in AAD09835. (PubMed:9891014)Curated
    Sequence conflicti394 – 3941V → I in AAD09835. (PubMed:9891014)Curated
    Sequence conflicti421 – 4211T → I in AAD09835. (PubMed:9891014)Curated
    Sequence conflicti532 – 5321D → G in AAD09835. (PubMed:9891014)Curated
    Sequence conflicti836 – 8361M → S in AAD09835. (PubMed:9891014)Curated
    Sequence conflicti851 – 8511I → V in AAD09835. (PubMed:9891014)Curated
    Sequence conflicti1126 – 11272HE → QD in AAD09835. (PubMed:9891014)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006603 mRNA. Translation: AAD09835.2.
    AL670169 Genomic DNA. Translation: CAM17240.1.
    CCDSiCCDS40845.1.
    PIRiT13964.
    RefSeqiNP_001123888.1. NM_001130416.1.
    NP_034543.3. NM_010413.3.
    XP_006527630.1. XM_006527567.1.
    UniGeneiMm.29854.

    Genome annotation databases

    EnsembliENSMUST00000033501; ENSMUSP00000033501; ENSMUSG00000031161.
    ENSMUST00000115642; ENSMUSP00000111306; ENSMUSG00000031161.
    GeneIDi15185.
    KEGGimmu:15185.
    UCSCiuc009snh.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006603 mRNA. Translation: AAD09835.2 .
    AL670169 Genomic DNA. Translation: CAM17240.1 .
    CCDSi CCDS40845.1.
    PIRi T13964.
    RefSeqi NP_001123888.1. NM_001130416.1.
    NP_034543.3. NM_010413.3.
    XP_006527630.1. XM_006527567.1.
    UniGenei Mm.29854.

    3D structure databases

    ProteinModelPortali Q9Z2V5.
    SMRi Q9Z2V5. Positions 1043-1144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200263. 16 interactions.
    IntActi Q9Z2V5. 8 interactions.
    MINTi MINT-220628.

    Chemistry

    BindingDBi Q9Z2V5.
    ChEMBLi CHEMBL2878.

    PTM databases

    PhosphoSitei Q9Z2V5.

    Proteomic databases

    MaxQBi Q9Z2V5.
    PaxDbi Q9Z2V5.
    PRIDEi Q9Z2V5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033501 ; ENSMUSP00000033501 ; ENSMUSG00000031161 .
    ENSMUST00000115642 ; ENSMUSP00000111306 ; ENSMUSG00000031161 .
    GeneIDi 15185.
    KEGGi mmu:15185.
    UCSCi uc009snh.2. mouse.

    Organism-specific databases

    CTDi 10013.
    MGIi MGI:1333752. Hdac6.

    Phylogenomic databases

    eggNOGi COG0123.
    GeneTreei ENSGT00530000062809.
    HOGENOMi HOG000004769.
    HOVERGENi HBG051894.
    KOi K11407.
    OMAi LQENWVC.
    OrthoDBi EOG7992PT.
    TreeFami TF106173.

    Enzyme and pathway databases

    Reactomei REACT_225256. HSF1 activation.

    Miscellaneous databases

    NextBioi 287707.
    PROi Q9Z2V5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2V5.
    Bgeei Q9Z2V5.
    CleanExi MM_HDAC6.
    Genevestigatori Q9Z2V5.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    3.40.800.20. 2 hits.
    InterProi IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF00850. Hist_deacetyl. 2 hits.
    PF02148. zf-UBP. 1 hit.
    [Graphical view ]
    PRINTSi PR01270. HDASUPER.
    SMARTi SM00290. ZnF_UBP. 1 hit.
    [Graphical view ]
    PROSITEi PS50271. ZF_UBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers."
      Verdel A., Khochbin S.
      J. Biol. Chem. 274:2440-2445(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Fetus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain."
      Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W.
      Mol. Cell. Biol. 21:6470-6483(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBFA2T3.
    4. "Microtubule deacetylases, SirT2 and HDAC6, in the nervous system."
      Southwood C.M., Peppi M., Dryden S., Tainsky M.A., Gow A.
      Neurochem. Res. 32:187-195(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin."
      Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.
      EMBO J. 29:131-144(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CYLD AND MICROTUBULES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "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.
    7. "SIRT2 interferes with autophagy-mediated degradation of protein aggregates in neuronal cells under proteasome inhibition."
      Gal J., Bang Y., Choi H.J.
      Neurochem. Int. 61:992-1000(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiHDAC6_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2V5
    Secondary accession number(s): B1AUA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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