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Q9UBN7

- HDAC6_HUMAN

UniProt

Q9UBN7 - HDAC6_HUMAN

Protein

Histone deacetylase 6

Gene

HDAC6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      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. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.By similarity
    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.

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei216 – 21611
    Active sitei611 – 61112
    Metal bindingi1113 – 11131Zinc 1
    Metal bindingi1115 – 11151Zinc 1
    Metal bindingi1133 – 11331Zinc 3
    Metal bindingi1136 – 11361Zinc 3
    Metal bindingi1145 – 11451Zinc 2
    Metal bindingi1148 – 11481Zinc 2
    Metal bindingi1153 – 11531Zinc 3
    Metal bindingi1160 – 11601Zinc 3
    Metal bindingi1164 – 11641Zinc 2
    Metal bindingi1170 – 11701Zinc 2
    Metal bindingi1183 – 11831Zinc 1
    Metal bindingi1186 – 11861Zinc 1

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1131 – 119262UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. alpha-tubulin binding Source: BHF-UCL
    2. beta-catenin binding Source: BHF-UCL
    3. dynein complex binding Source: BHF-UCL
    4. enzyme binding Source: UniProtKB
    5. histone deacetylase activity Source: BHF-UCL
    6. histone deacetylase binding Source: UniProtKB
    7. Hsp90 protein binding Source: BHF-UCL
    8. microtubule binding Source: UniProtKB
    9. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    10. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    11. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    12. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    13. polyubiquitin binding Source: BHF-UCL
    14. protein binding Source: UniProtKB
    15. tau protein binding Source: BHF-UCL
    16. tubulin deacetylase activity Source: UniProtKB
    17. zinc ion binding Source: InterPro

    GO - Biological processi

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

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Autophagy, Transcription, Transcription regulation

    Keywords - Ligandi

    Actin-binding, 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.
    REACT_200744. HSF1 activation.
    SABIO-RKQ9UBN7.
    SignaLinkiQ9UBN7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 6 (EC:3.5.1.98)
    Short name:
    HD6
    Gene namesi
    Name:HDAC6
    Synonyms:KIAA0901
    ORF Names:JM21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:14064. HDAC6.

    Subcellular locationi

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

    GO - Cellular componenti

    1. aggresome Source: BHF-UCL
    2. axon Source: UniProtKB
    3. caveola Source: BHF-UCL
    4. cell leading edge Source: BHF-UCL
    5. cytoplasm Source: UniProtKB
    6. cytoplasmic microtubule Source: Ensembl
    7. cytosol Source: UniProtKB
    8. dendrite Source: UniProtKB
    9. histone deacetylase complex Source: UniProtKB
    10. inclusion body Source: BHF-UCL
    11. microtubule Source: UniProtKB
    12. microtubule associated complex Source: BHF-UCL
    13. nucleus Source: UniProtKB
    14. perikaryon Source: UniProtKB
    15. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Chondrodysplasia with platyspondyly, distinctive brachydactyly, hydrocephaly, and microphthalmia (CDP-PBHM) [MIM:300863]: A disease characterized by chondrodysplasia, severe platyspondyly, hydrocephaly, and facial features with microphthalmia. Bone abnormalities include a distinctive metaphyseal cupping of the metacarpals, metatarsals, and phalanges. Affected females show a milder phenotype with small stature, sometimes associated with body asymmetry and mild mental retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi216 – 2161H → A: Reduces histone deacetylase activity. 1 Publication
    Mutagenesisi611 – 6111H → A: Reduces histone deacetylase activity. 1 Publication

    Organism-specific databases

    MIMi300863. phenotype.
    Orphaneti163966. X-linked dominant chondrodysplasia, Chassaing-Lacombe type.
    PharmGKBiPA29231.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12151215Histone deacetylase 6PRO_0000114703Add
    BLAST

    Post-translational modificationi

    Phosphorylated by AURKA.1 Publication
    Ubiquitinated. Its polyubiquitination however does not lead to its degradation.1 Publication
    Sumoylated in vitro.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UBN7.
    PaxDbiQ9UBN7.
    PRIDEiQ9UBN7.

    PTM databases

    PhosphoSiteiQ9UBN7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UBN7.
    BgeeiQ9UBN7.
    CleanExiHS_HDAC6.
    GenevestigatoriQ9UBN7.

    Organism-specific databases

    HPAiCAB004236.
    HPA003714.
    HPA026321.

    Interactioni

    Subunit structurei

    Interacts with ZMYND15 By similarity. 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. Interacts with BBIP10, CBFA2T3, CYLD, DDIT3/CHOP, F-actin and HDAC11.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADRBK1P211463EBI-301697,EBI-1036401From a different organism.
    ATP13A2Q9NQ112EBI-301697,EBI-6308763
    BRMS1Q9HCU92EBI-301697,EBI-714781
    Cdc20Q626232EBI-301697,EBI-2256532From a different organism.
    CTTNQ142473EBI-301697,EBI-351886
    CttnQ605983EBI-301697,EBI-397955From a different organism.
    CYLDQ9NQC74EBI-301697,EBI-2117940
    EGFRP005338EBI-301697,EBI-297353
    PRKCAP172522EBI-301697,EBI-1383528
    taxP034094EBI-301697,EBI-5236464From a different organism.

    Protein-protein interaction databases

    BioGridi115330. 227 interactions.
    DIPiDIP-27544N.
    IntActiQ9UBN7. 85 interactions.
    MINTiMINT-4905696.
    STRINGi9606.ENSP00000334061.

    Structurei

    Secondary structure

    1
    1215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1116 – 11183
    Turni1134 – 11363
    Beta strandi1140 – 11456
    Turni1146 – 11483
    Beta strandi1151 – 11533
    Turni1155 – 11584
    Helixi1160 – 11689
    Beta strandi1172 – 11754
    Turni1176 – 11783
    Beta strandi1181 – 11833
    Turni1184 – 11874
    Beta strandi1188 – 11903
    Helixi1193 – 11953
    Helixi1196 – 120712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C5KX-ray1.55A1109-1215[»]
    3GV4X-ray1.72A1109-1215[»]
    3PHDX-ray3.00A/B/C/D1109-1215[»]
    ProteinModelPortaliQ9UBN7.
    SMRiQ9UBN7. Positions 86-435, 481-835, 1109-1210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBN7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni87 – 404318Histone deacetylase 1Add
    BLAST
    Regioni482 – 800319Histone deacetylase 2Add
    BLAST
    Regioni1154 – 11563Ubiquitin binding
    Regioni1182 – 11898Ubiquitin binding

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1131 – 119262UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000004769.
    HOVERGENiHBG051894.
    InParanoidiQ9UBN7.
    KOiK11407.
    PhylomeDBiQ9UBN7.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBN7-1) [UniParc]FASTAAdd to Basket

    Also known as: HDAC6p131

    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

    MTSTGQDSTT TRQRRSRQNP QSPPQDSSVT SKRNIKKGAV PRSIPNLAEV     50
    KKKGKMKKLG QAMEEDLIVG LQGMDLNLEA EALAGTGLVL DEQLNEFHCL 100
    WDDSFPEGPE RLHAIKEQLI QEGLLDRCVS FQARFAEKEE LMLVHSLEYI 150
    DLMETTQYMN EGELRVLADT YDSVYLHPNS YSCACLASGS VLRLVDAVLG 200
    AEIRNGMAII RPPGHHAQHS LMDGYCMFNH VAVAARYAQQ KHRIRRVLIV 250
    DWDVHHGQGT QFTFDQDPSV LYFSIHRYEQ GRFWPHLKAS NWSTTGFGQG 300
    QGYTINVPWN QVGMRDADYI AAFLHVLLPV ALEFQPQLVL VAAGFDALQG 350
    DPKGEMAATP AGFAQLTHLL MGLAGGKLIL SLEGGYNLRA LAEGVSASLH 400
    TLLGDPCPML ESPGAPCRSA QASVSCALEA LEPFWEVLVR STETVERDNM 450
    EEDNVEESEE EGPWEPPVLP ILTWPVLQSR TGLVYDQNMM NHCNLWDSHH 500
    PEVPQRILRI MCRLEELGLA GRCLTLTPRP ATEAELLTCH SAEYVGHLRA 550
    TEKMKTRELH RESSNFDSIY ICPSTFACAQ LATGAACRLV EAVLSGEVLN 600
    GAAVVRPPGH HAEQDAACGF CFFNSVAVAA RHAQTISGHA LRILIVDWDV 650
    HHGNGTQHMF EDDPSVLYVS LHRYDHGTFF PMGDEGASSQ IGRAAGTGFT 700
    VNVAWNGPRM GDADYLAAWH RLVLPIAYEF NPELVLVSAG FDAARGDPLG 750
    GCQVSPEGYA HLTHLLMGLA SGRIILILEG GYNLTSISES MAACTRSLLG 800
    DPPPLLTLPR PPLSGALASI TETIQVHRRY WRSLRVMKVE DREGPSSSKL 850
    VTKKAPQPAK PRLAERMTTR EKKVLEAGMG KVTSASFGEE STPGQTNSET 900
    AVVALTQDQP SEAATGGATL AQTISEAAIG GAMLGQTTSE EAVGGATPDQ 950
    TTSEETVGGA ILDQTTSEDA VGGATLGQTT SEEAVGGATL AQTTSEAAME 1000
    GATLDQTTSE EAPGGTELIQ TPLASSTDHQ TPPTSPVQGT TPQISPSTLI 1050
    GSLRTLELGS ESQGASESQA PGEENLLGEA AGGQDMADSM LMQGSRGLTD 1100
    QAIFYAVTPL PWCPHLVAVC PIPAAGLDVT QPCGDCGTIQ ENWVCLSCYQ 1150
    VYCGRYINGH MLQHHGNSGH PLVLSYIDLS AWCYYCQAYV HHQALLDVKN 1200
    IAHQNKFGED MPHPH 1215
    Length:1,215
    Mass (Da):131,419
    Last modified:September 2, 2008 - v2
    Checksum:i6F17731268A33114
    GO
    Isoform 2 (identifier: Q9UBN7-2) [UniParc]FASTAAdd to Basket

    Also known as: HDAC6p114

    The sequence of this isoform differs from the canonical sequence as follows:
         1-152: Missing.

    Note: Required for TGF-beta1-activated gene expression associated with epithelial-mesenchymal transition (EMT) in A549 cells.

    Show »
    Length:1,063
    Mass (Da):114,361
    Checksum:iE77E732ACF187AB7
    GO

    Sequence cautioni

    The sequence BAA74924.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti994 – 9941T → I.2 Publications
    Corresponds to variant rs1127346 [ dbSNP | Ensembl ].
    VAR_046300
    Natural varianti1200 – 12001N → D.1 Publication
    Corresponds to variant rs151130423 [ dbSNP | Ensembl ].
    VAR_068962

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 152152Missing in isoform 2. 1 PublicationVSP_044576Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132609 mRNA. Translation: AAD29048.1.
    AB020708 mRNA. Translation: BAA74924.2. Different initiation.
    AJ011972 mRNA. Translation: CAA09893.1.
    AF196971 Genomic DNA. No translation available.
    CH471224 Genomic DNA. Translation: EAW50748.1.
    BC013737 mRNA. Translation: AAH13737.1.
    BC069243 mRNA. Translation: AAH69243.1.
    CCDSiCCDS14306.1. [Q9UBN7-1]
    RefSeqiNP_006035.2. NM_006044.2. [Q9UBN7-1]
    XP_005272622.1. XM_005272565.1. [Q9UBN7-1]
    XP_005272623.1. XM_005272566.1. [Q9UBN7-1]
    XP_005272625.1. XM_005272568.1. [Q9UBN7-1]
    XP_006724588.1. XM_006724525.1. [Q9UBN7-1]
    UniGeneiHs.6764.

    Genome annotation databases

    EnsembliENST00000334136; ENSP00000334061; ENSG00000094631. [Q9UBN7-1]
    ENST00000376619; ENSP00000365804; ENSG00000094631. [Q9UBN7-1]
    GeneIDi10013.
    KEGGihsa:10013.
    UCSCiuc004dks.1. human. [Q9UBN7-1]

    Polymorphism databases

    DMDMi205371758.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132609 mRNA. Translation: AAD29048.1 .
    AB020708 mRNA. Translation: BAA74924.2 . Different initiation.
    AJ011972 mRNA. Translation: CAA09893.1 .
    AF196971 Genomic DNA. No translation available.
    CH471224 Genomic DNA. Translation: EAW50748.1 .
    BC013737 mRNA. Translation: AAH13737.1 .
    BC069243 mRNA. Translation: AAH69243.1 .
    CCDSi CCDS14306.1. [Q9UBN7-1 ]
    RefSeqi NP_006035.2. NM_006044.2. [Q9UBN7-1 ]
    XP_005272622.1. XM_005272565.1. [Q9UBN7-1 ]
    XP_005272623.1. XM_005272566.1. [Q9UBN7-1 ]
    XP_005272625.1. XM_005272568.1. [Q9UBN7-1 ]
    XP_006724588.1. XM_006724525.1. [Q9UBN7-1 ]
    UniGenei Hs.6764.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3C5K X-ray 1.55 A 1109-1215 [» ]
    3GV4 X-ray 1.72 A 1109-1215 [» ]
    3PHD X-ray 3.00 A/B/C/D 1109-1215 [» ]
    ProteinModelPortali Q9UBN7.
    SMRi Q9UBN7. Positions 86-435, 481-835, 1109-1210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115330. 227 interactions.
    DIPi DIP-27544N.
    IntActi Q9UBN7. 85 interactions.
    MINTi MINT-4905696.
    STRINGi 9606.ENSP00000334061.

    Chemistry

    BindingDBi Q9UBN7.
    ChEMBLi CHEMBL2093865.
    DrugBanki DB02546. Vorinostat.
    GuidetoPHARMACOLOGYi 2618.

    PTM databases

    PhosphoSitei Q9UBN7.

    Polymorphism databases

    DMDMi 205371758.

    Proteomic databases

    MaxQBi Q9UBN7.
    PaxDbi Q9UBN7.
    PRIDEi Q9UBN7.

    Protocols and materials databases

    DNASUi 10013.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334136 ; ENSP00000334061 ; ENSG00000094631 . [Q9UBN7-1 ]
    ENST00000376619 ; ENSP00000365804 ; ENSG00000094631 . [Q9UBN7-1 ]
    GeneIDi 10013.
    KEGGi hsa:10013.
    UCSCi uc004dks.1. human. [Q9UBN7-1 ]

    Organism-specific databases

    CTDi 10013.
    GeneCardsi GC0XP048659.
    H-InvDB HIX0016783.
    HGNCi HGNC:14064. HDAC6.
    HPAi CAB004236.
    HPA003714.
    HPA026321.
    MIMi 300272. gene.
    300863. phenotype.
    neXtProti NX_Q9UBN7.
    Orphaneti 163966. X-linked dominant chondrodysplasia, Chassaing-Lacombe type.
    PharmGKBi PA29231.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000004769.
    HOVERGENi HBG051894.
    InParanoidi Q9UBN7.
    KOi K11407.
    PhylomeDBi Q9UBN7.
    TreeFami TF106173.

    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.
    REACT_200744. HSF1 activation.
    SABIO-RK Q9UBN7.
    SignaLinki Q9UBN7.

    Miscellaneous databases

    ChiTaRSi HDAC6. human.
    EvolutionaryTracei Q9UBN7.
    GeneWikii HDAC6.
    GenomeRNAii 10013.
    NextBioi 37827.
    PROi Q9UBN7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBN7.
    Bgeei Q9UBN7.
    CleanExi HS_HDAC6.
    Genevestigatori Q9UBN7.

    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. "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), VARIANT ILE-994.
    2. "Prediction of the coding sequences of unidentified human genes. XII. 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., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "Transcription map in Xp11.23."
      Strom T.M., Gutwillinger N., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-994.
      Tissue: Brain.
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 2), VARIANT ASP-1200.
      Tissue: Ovary and Placenta.
    8. "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.
    9. "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family."
      Gao L., Cueto M.A., Asselbergs F., Atadja P.
      J. Biol. Chem. 277:25748-25755(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC11.
    10. Cited for: SUMOYLATION.
    11. "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, MUTAGENESIS OF HIS-216 AND HIS-611.
    12. Cited for: FUNCTION.
    13. "The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase."
      North B.J., Marshall B.L., Borra M.T., Denu J.M., Verdin E.
      Mol. Cell 11:437-444(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIRT2.
    14. "HEF1-dependent Aurora A activation induces disassembly of the primary cilium."
      Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P., Golemis E.A.
      Cell 129:1351-1363(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY AURKA.
    15. "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.
    16. "Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6."
      Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D., Chin L.S.
      J. Cell Biol. 178:1025-1038(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin."
      Nahhas F., Dryden S.C., Abrams J., Tainsky M.A.
      Mol. Cell. Biochem. 303:221-230(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIRT2.
    18. Cited for: INTERACTION WITH BBIP10.
    19. "The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition."
      Kalveram B., Schmidtke G., Groettrup M.
      J. Cell Sci. 121:4079-4088(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBD.
    20. "Requirement of a novel splicing variant of human histone deacetylase 6 for TGF-beta1-mediated gene activation."
      Zhuang Y., Nguyen H.T., Lasky J.A., Cao S., Li C., Hu J., Guo X., Burow M.E., Shan B.
      Biochem. Biophys. Res. Commun. 392:608-613(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
    21. "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: INTERACTION WITH CYLD.
    22. "A mutation in the 3'-UTR of the HDAC6 gene abolishing the post-transcriptional regulation mediated by hsa-miR-433 is linked to a new form of dominant X-linked chondrodysplasia."
      Simon D., Laloo B., Barillot M., Barnetche T., Blanchard C., Rooryck C., Marche M., Burgelin I., Coupry I., Chassaing N., Gilbert-Dussardier B., Lacombe D., Grosset C., Arveiler B.
      Hum. Mol. Genet. 19:2015-2027(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CDP-PBHM.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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.
    25. "Crystal structure of human HDAC6 zinc finger domain."
      Structural genomics consortium (SGC)
      Submitted (FEB-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1109-1215 IN COMPLEX WITH ZINC IONS.
    26. "Crystal structure of human HDAC6 zinc finger domain and ubiquitin C-terminal peptide RLRGG."
      Structural genomics consortium (SGC)
      Submitted (APR-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 1109-1215 IN COMPLEX WITH ZINC IONS AND UBIQUITIN C-TERMINAL PEPTIDE RLRGG.

    Entry informationi

    Entry nameiHDAC6_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBN7
    Secondary accession number(s): O94975
    , Q6NT75, Q7L3E5, Q96CY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 144 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3