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Q9UBN7

- HDAC6_HUMAN

UniProt

Q9UBN7 - HDAC6_HUMAN

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Protein

Histone deacetylase 6

Gene
HDAC6, KIAA0901, JM21
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 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.2 Publications

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-typeAdd
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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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.

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. 74 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.

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1131 – 119262UBP-typeAdd
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. VSP_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]
ENST00000595349; ENSP00000470544; ENSG00000269101. [Q9UBN7-1]
ENST00000597097; ENSP00000471818; ENSG00000269101. [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. 74 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 ]
ENST00000595349 ; ENSP00000470544 ; ENSG00000269101 . [Q9UBN7-1 ]
ENST00000597097 ; ENSP00000471818 ; ENSG00000269101 . [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

« Hide 'large scale' publications
  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. "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.
  25. "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: September 3, 2014
This is version 143 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

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