Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UBN7 (HDAC6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 6

Short name=HD6
EC=3.5.1.98
Gene names
Name:HDAC6
Synonyms:KIAA0901
ORF Names:JM21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.16

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. Ref.12 Ref.16

Catalytic activity

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

Cofactor

Binds 3 zinc ions per subunit.

Subunit structure

Interacts with CBFA2T3, HDAC11 and SIRT2. Interacts with F-actin. Interacts with BBIP10. Under proteasome impairment conditions, interacts with UBD via its histone deacetylase 1 and UBP-type zinc-finger regions. Interacts with CYLD. Interacts with ZMYND15 By similarity. Interacts with DDIT3/CHOP. Ref.8 Ref.9 Ref.13 Ref.15 Ref.17 Ref.18 Ref.20

Subcellular location

Nucleus. Cytoplasm. Note: It is mainly cytoplasmic, where it is associated with microtubules.

Post-translational modification

Phosphorylated by AURKA. Ref.14

Ubiquitinated. Its polyubiquitination however does not lead to its degradation. Ref.11

Sumoylated in vitro. Ref.10

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Sequence similarities

Belongs to the histone deacetylase family. HD type 2 subfamily.

Contains 1 UBP-type zinc finger.

Sequence caution

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

Ontologies

Keywords
   Biological processAutophagy
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandActin-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processHsp90 deacetylation

Inferred from mutant phenotype PubMed 19158084. Source: BHF-UCL

aggresome assembly

Inferred from mutant phenotype PubMed 14675537. Source: BHF-UCL

cellular response to hydrogen peroxide

Inferred from mutant phenotype PubMed 18606987. Source: BHF-UCL

cellular response to misfolded protein

Inferred from electronic annotation. Source: Ensembl

cellular response to topologically incorrect protein

Inferred from mutant phenotype PubMed 16192271. Source: BHF-UCL

histone deacetylation

Inferred from sequence or structural similarity PubMed 11861901. Source: UniProtKB

intracellular protein transport

Inferred from mutant phenotype PubMed 16192271. Source: BHF-UCL

lysosome localization

Inferred from mutant phenotype PubMed 16192271. Source: BHF-UCL

macroautophagy

Inferred from mutant phenotype PubMed 16192271. Source: BHF-UCL

misfolded or incompletely synthesized protein catabolic process

Inferred from mutant phenotype PubMed 14675537. Source: BHF-UCL

negative regulation of hydrogen peroxide metabolic process

Inferred by curator PubMed 18606987. Source: BHF-UCL

negative regulation of microtubule depolymerization

Inferred from electronic annotation. Source: Ensembl

negative regulation of oxidoreductase activity

Inferred by curator PubMed 18606987. Source: BHF-UCL

negative regulation of protein complex disassembly

Inferred from mutant phenotype PubMed 15916966. Source: BHF-UCL

negative regulation of proteolysis

Inferred from mutant phenotype PubMed 18356165. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity PubMed 11861901. Source: UniProtKB

peptidyl-lysine deacetylation

Inferred from mutant phenotype PubMed 18356165PubMed 18606987. Source: BHF-UCL

polyubiquitinated misfolded protein transport

Inferred from mutant phenotype PubMed 14675537. Source: BHF-UCL

positive regulation of chaperone-mediated protein complex assembly

Inferred from mutant phenotype PubMed 19158084. Source: BHF-UCL

positive regulation of epithelial cell migration

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

positive regulation of hydrogen peroxide-mediated programmed cell death

Inferred from direct assay PubMed 18606987. Source: BHF-UCL

positive regulation of receptor biosynthetic process

Inferred from mutant phenotype PubMed 15916966PubMed 18316616. Source: BHF-UCL

positive regulation of signal transduction

Inferred from mutant phenotype PubMed 19158084. Source: BHF-UCL

protein complex disassembly

Inferred from electronic annotation. Source: Ensembl

protein deacetylation

Inferred from mutant phenotype PubMed 15916966. Source: BHF-UCL

protein polyubiquitination

Inferred from electronic annotation. Source: Ensembl

regulation of androgen receptor signaling pathway

Traceable author statement PubMed 18852123. Source: BHF-UCL

regulation of establishment of protein localization

Inferred from electronic annotation. Source: Ensembl

regulation of microtubule-based movement

Inferred by curator PubMed 19228685. Source: BHF-UCL

regulation of receptor activity

Inferred from mutant phenotype PubMed 19158084. Source: BHF-UCL

response to growth factor

Inferred from mutant phenotype PubMed 18356165. Source: BHF-UCL

response to misfolded protein

Inferred from mutant phenotype PubMed 14675537. Source: BHF-UCL

response to organic substance

Inferred from mutant phenotype PubMed 19158084. Source: BHF-UCL

response to toxic substance

Inferred from mutant phenotype PubMed 19158084. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

tubulin deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaggresome

Inferred from direct assay PubMed 14675537. Source: BHF-UCL

axon

Inferred from sequence or structural similarity. Source: UniProtKB

caveola

Inferred from direct assay PubMed 18356165. Source: BHF-UCL

cell leading edge

Inferred from direct assay Ref.12. Source: BHF-UCL

cytoplasm

Inferred from sequence or structural similarity PubMed 11861901. Source: UniProtKB

cytoplasmic microtubule

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylase complex

Inferred from direct assay Ref.9. Source: UniProtKB

inclusion body

Inferred from direct assay PubMed 16192271. Source: BHF-UCL

microtubule

Inferred from direct assay Ref.13. Source: UniProtKB

microtubule associated complex

Inferred from direct assay PubMed 19228685. Source: BHF-UCL

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perikaryon

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.12. Source: BHF-UCL

   Molecular_functionHsp90 protein binding

Inferred from direct assay PubMed 15916966. Source: BHF-UCL

NAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

alpha-tubulin binding

Inferred from direct assay PubMed 19228685. Source: BHF-UCL

beta-catenin binding

Inferred from physical interaction PubMed 18356165. Source: BHF-UCL

dynein complex binding

Inferred from direct assay PubMed 14675537. Source: BHF-UCL

enzyme binding

Inferred from sequence or structural similarity PubMed 11861901. Source: UniProtKB

histone deacetylase activity

Inferred from direct assay Ref.1. Source: BHF-UCL

histone deacetylase binding

Inferred from physical interaction Ref.13. Source: UniProtKB

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

polyubiquitin binding

Inferred from direct assay PubMed 14675537. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.15Ref.18Ref.17. Source: UniProtKB

tau protein binding

Inferred from direct assay PubMed 18636984. Source: BHF-UCL

tubulin deacetylase activity

Inferred from direct assay Ref.13. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBN7-1)

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.
Isoform 2 (identifier: Q9UBN7-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12151215Histone deacetylase 6
PRO_0000114703

Regions

Zinc finger1131 – 119262UBP-type
Region87 – 404318Histone deacetylase 1
Region482 – 800319Histone deacetylase 2
Region1154 – 11563Ubiquitin binding
Region1182 – 11898Ubiquitin binding

Sites

Active site21611
Active site61112
Metal binding11131Zinc 1
Metal binding11151Zinc 1
Metal binding11331Zinc 3
Metal binding11361Zinc 3
Metal binding11451Zinc 2
Metal binding11481Zinc 2
Metal binding11531Zinc 3
Metal binding11601Zinc 3
Metal binding11641Zinc 2
Metal binding11701Zinc 2
Metal binding11831Zinc 1
Metal binding11861Zinc 1

Natural variations

Alternative sequence1 – 152152Missing in isoform 2.
VSP_044576
Natural variant9941T → I. Ref.1 Ref.4
Corresponds to variant rs1127346 [ dbSNP | Ensembl ].
VAR_046300
Natural variant12001N → D. Ref.7
Corresponds to variant rs151130423 [ dbSNP | Ensembl ].
VAR_068962

Experimental info

Mutagenesis2161H → A: Reduces histone deacetylase activity. Ref.11
Mutagenesis6111H → A: Reduces histone deacetylase activity. Ref.11

Secondary structure

........................ 1215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HDAC6p131) [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 6F17731268A33114

FASTA1,215131,419
        10         20         30         40         50         60 
MTSTGQDSTT TRQRRSRQNP QSPPQDSSVT SKRNIKKGAV PRSIPNLAEV KKKGKMKKLG 

        70         80         90        100        110        120 
QAMEEDLIVG LQGMDLNLEA EALAGTGLVL DEQLNEFHCL WDDSFPEGPE RLHAIKEQLI 

       130        140        150        160        170        180 
QEGLLDRCVS FQARFAEKEE LMLVHSLEYI DLMETTQYMN EGELRVLADT YDSVYLHPNS 

       190        200        210        220        230        240 
YSCACLASGS VLRLVDAVLG AEIRNGMAII RPPGHHAQHS LMDGYCMFNH VAVAARYAQQ 

       250        260        270        280        290        300 
KHRIRRVLIV DWDVHHGQGT QFTFDQDPSV LYFSIHRYEQ GRFWPHLKAS NWSTTGFGQG 

       310        320        330        340        350        360 
QGYTINVPWN QVGMRDADYI AAFLHVLLPV ALEFQPQLVL VAAGFDALQG DPKGEMAATP 

       370        380        390        400        410        420 
AGFAQLTHLL MGLAGGKLIL SLEGGYNLRA LAEGVSASLH TLLGDPCPML ESPGAPCRSA 

       430        440        450        460        470        480 
QASVSCALEA LEPFWEVLVR STETVERDNM EEDNVEESEE EGPWEPPVLP ILTWPVLQSR 

       490        500        510        520        530        540 
TGLVYDQNMM NHCNLWDSHH PEVPQRILRI MCRLEELGLA GRCLTLTPRP ATEAELLTCH 

       550        560        570        580        590        600 
SAEYVGHLRA TEKMKTRELH RESSNFDSIY ICPSTFACAQ LATGAACRLV EAVLSGEVLN 

       610        620        630        640        650        660 
GAAVVRPPGH HAEQDAACGF CFFNSVAVAA RHAQTISGHA LRILIVDWDV HHGNGTQHMF 

       670        680        690        700        710        720 
EDDPSVLYVS LHRYDHGTFF PMGDEGASSQ IGRAAGTGFT VNVAWNGPRM GDADYLAAWH 

       730        740        750        760        770        780 
RLVLPIAYEF NPELVLVSAG FDAARGDPLG GCQVSPEGYA HLTHLLMGLA SGRIILILEG 

       790        800        810        820        830        840 
GYNLTSISES MAACTRSLLG DPPPLLTLPR PPLSGALASI TETIQVHRRY WRSLRVMKVE 

       850        860        870        880        890        900 
DREGPSSSKL VTKKAPQPAK PRLAERMTTR EKKVLEAGMG KVTSASFGEE STPGQTNSET 

       910        920        930        940        950        960 
AVVALTQDQP SEAATGGATL AQTISEAAIG GAMLGQTTSE EAVGGATPDQ TTSEETVGGA 

       970        980        990       1000       1010       1020 
ILDQTTSEDA VGGATLGQTT SEEAVGGATL AQTTSEAAME GATLDQTTSE EAPGGTELIQ 

      1030       1040       1050       1060       1070       1080 
TPLASSTDHQ TPPTSPVQGT TPQISPSTLI GSLRTLELGS ESQGASESQA PGEENLLGEA 

      1090       1100       1110       1120       1130       1140 
AGGQDMADSM LMQGSRGLTD QAIFYAVTPL PWCPHLVAVC PIPAAGLDVT QPCGDCGTIQ 

      1150       1160       1170       1180       1190       1200 
ENWVCLSCYQ VYCGRYINGH MLQHHGNSGH PLVLSYIDLS AWCYYCQAYV HHQALLDVKN 

      1210 
IAHQNKFGED MPHPH 

« Hide

Isoform 2 (HDAC6p114) [UniParc].

Checksum: E77E732ACF187AB7
Show »

FASTA1,063114,361

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase."
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.
EMBO J. 21:2682-2691(2002) [PubMed] [Europe PMC] [Abstract]
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]"HDAC6 is a microtubule-associated deacetylase."
Hubbert C., Guardiola A., Shao R., Kawaguchi Y., Ito A., Nixon A., Yoshida M., Wang X.-F., Yao T.-P.
Nature 417:455-458(2002) [PubMed] [Europe PMC] [Abstract]
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]"A BBSome subunit links ciliogenesis, microtubule stability and acetylation."
Loktev A.V., Zhang Q., Beck J.S., Searby C.C., Scheetz T.E., Bazan F., Slusarski D.C., Sheffield V.C., Jackson P.K., Nachury M.V.
Dev. Cell 15:854-865(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BBIP10.
[18]"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.
[19]"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).
[20]"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.
[21]"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.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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.
[24]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14306.1. [Q9UBN7-1]
RefSeqNP_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]
UniGeneHs.6764.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3C5KX-ray1.55A1109-1215[»]
3GV4X-ray1.72A1109-1215[»]
3PHDX-ray3.00A/B/C/D1109-1215[»]
ProteinModelPortalQ9UBN7.
SMRQ9UBN7. Positions 86-435, 481-835, 1109-1210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115330. 224 interactions.
DIPDIP-27544N.
IntActQ9UBN7. 74 interactions.
MINTMINT-4905696.
STRING9606.ENSP00000334061.

Chemistry

BindingDBQ9UBN7.
ChEMBLCHEMBL2093865.
DrugBankDB02546. Vorinostat.
GuidetoPHARMACOLOGY2618.

PTM databases

PhosphoSiteQ9UBN7.

Polymorphism databases

DMDM205371758.

Proteomic databases

MaxQBQ9UBN7.
PaxDbQ9UBN7.
PRIDEQ9UBN7.

Protocols and materials databases

DNASU10013.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334136; ENSP00000334061; ENSG00000094631. [Q9UBN7-1]
ENST00000376619; ENSP00000365804; ENSG00000094631. [Q9UBN7-1]
ENST00000595349; ENSP00000470544; ENSG00000269101. [Q9UBN7-1]
ENST00000597097; ENSP00000471818; ENSG00000269101. [Q9UBN7-1]
GeneID10013.
KEGGhsa:10013.
UCSCuc004dks.1. human. [Q9UBN7-1]

Organism-specific databases

CTD10013.
GeneCardsGC0XP048659.
H-InvDBHIX0016783.
HGNCHGNC:14064. HDAC6.
HPACAB004236.
HPA003714.
HPA026321.
MIM300272. gene.
300863. phenotype.
neXtProtNX_Q9UBN7.
Orphanet163966. X-linked dominant chondrodysplasia, Chassaing-Lacombe type.
PharmGKBPA29231.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000004769.
HOVERGENHBG051894.
InParanoidQ9UBN7.
KOK11407.
PhylomeDBQ9UBN7.
TreeFamTF106173.

Enzyme and pathway databases

BRENDA3.5.1.98. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
SABIO-RKQ9UBN7.
SignaLinkQ9UBN7.

Gene expression databases

ArrayExpressQ9UBN7.
BgeeQ9UBN7.
CleanExHS_HDAC6.
GenevestigatorQ9UBN7.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.40.800.20. 2 hits.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 2 hits.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PRINTSPR01270. HDASUPER.
SMARTSM00290. ZnF_UBP. 1 hit.
[Graphical view]
PROSITEPS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHDAC6. human.
EvolutionaryTraceQ9UBN7.
GeneWikiHDAC6.
GenomeRNAi10013.
NextBio37827.
PROQ9UBN7.
SOURCESearch...

Entry information

Entry nameHDAC6_HUMAN
AccessionPrimary (citable) accession number: Q9UBN7
Secondary accession number(s): O94975 expand/collapse secondary AC list , Q6NT75, Q7L3E5, Q96CY0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 2, 2008
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM