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Protein

Histone deacetylase 6

Gene

HDAC6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.By similarity3 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.

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 3 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei21611
Active sitei61121
Metal bindingi1113Zinc 11
Metal bindingi1115Zinc 11
Metal bindingi1133Zinc 31
Metal bindingi1136Zinc 31
Metal bindingi1145Zinc 21
Metal bindingi1148Zinc 21
Metal bindingi1153Zinc 31
Metal bindingi1160Zinc 31
Metal bindingi1164Zinc 21
Metal bindingi1170Zinc 21
Metal bindingi1183Zinc 11
Metal bindingi1186Zinc 11

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1131 – 1192UBP-typePROSITE-ProRule annotationAdd BLAST62

GO - Molecular functioni

  • alpha-tubulin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • core promoter binding Source: UniProtKB
  • dynein complex binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • histone deacetylase activity Source: BHF-UCL
  • histone deacetylase binding Source: UniProtKB
  • Hsp90 protein binding Source: BHF-UCL
  • microtubule binding Source: UniProtKB
  • misfolded protein binding Source: Reactome
  • NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  • polyubiquitin binding Source: BHF-UCL
  • tau protein binding Source: BHF-UCL
  • tubulin deacetylase activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • aggresome assembly Source: BHF-UCL
  • cellular response to hydrogen peroxide Source: BHF-UCL
  • cellular response to misfolded protein Source: Ensembl
  • cellular response to topologically incorrect protein Source: BHF-UCL
  • collateral sprouting Source: Ensembl
  • dendritic spine morphogenesis Source: Ensembl
  • histone deacetylation Source: UniProtKB
  • Hsp90 deacetylation Source: BHF-UCL
  • intracellular protein transport Source: BHF-UCL
  • lysosome localization Source: BHF-UCL
  • macroautophagy Source: BHF-UCL
  • misfolded or incompletely synthesized protein catabolic process Source: BHF-UCL
  • mitochondrion localization Source: Ensembl
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • negative regulation of hydrogen peroxide metabolic process Source: BHF-UCL
  • negative regulation of microtubule depolymerization Source: Ensembl
  • negative regulation of oxidoreductase activity Source: BHF-UCL
  • negative regulation of protein complex disassembly Source: BHF-UCL
  • negative regulation of proteolysis Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • organelle organization Source: Reactome
  • peptidyl-lysine deacetylation Source: BHF-UCL
  • polyubiquitinated misfolded protein transport Source: BHF-UCL
  • positive regulation of chaperone-mediated protein complex assembly Source: BHF-UCL
  • positive regulation of epithelial cell migration Source: BHF-UCL
  • positive regulation of hydrogen peroxide-mediated programmed cell death Source: BHF-UCL
  • positive regulation of receptor biosynthetic process Source: BHF-UCL
  • positive regulation of signal transduction Source: BHF-UCL
  • protein complex disassembly Source: Ensembl
  • protein deacetylation Source: BHF-UCL
  • protein polyubiquitination Source: Ensembl
  • regulation of androgen receptor signaling pathway Source: BHF-UCL
  • regulation of autophagy Source: ParkinsonsUK-UCL
  • regulation of establishment of protein localization Source: Ensembl
  • regulation of fat cell differentiation Source: Ensembl
  • regulation of gene expression, epigenetic Source: UniProtKB
  • regulation of microtubule-based movement Source: BHF-UCL
  • regulation of mitophagy Source: ParkinsonsUK-UCL
  • regulation of protein stability Source: ParkinsonsUK-UCL
  • regulation of receptor activity Source: BHF-UCL
  • response to growth factor Source: BHF-UCL
  • response to misfolded protein Source: BHF-UCL
  • response to organic substance Source: BHF-UCL
  • response to toxic substance Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
  • tubulin deacetylation Source: UniProtKB
  • 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

BioCyciZFISH:HS01799-MONOMER.
BRENDAi3.5.1.98. 2681.
ReactomeiR-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3371511. HSF1 activation.
R-HSA-5617833. Assembly of the primary cilium.
SABIO-RKQ9UBN7.
SignaLinkiQ9UBN7.
SIGNORiQ9UBN7.

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
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:14064. HDAC6.

Subcellular locationi

GO - Cellular componenti

  • aggresome Source: BHF-UCL
  • axon Source: UniProtKB
  • caveola Source: BHF-UCL
  • cell leading edge Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytoplasmic microtubule Source: Ensembl
  • cytosol Source: UniProtKB
  • dendrite Source: UniProtKB
  • histone deacetylase complex Source: UniProtKB
  • inclusion body Source: BHF-UCL
  • microtubule Source: UniProtKB
  • microtubule associated complex Source: BHF-UCL
  • multivesicular body Source: ParkinsonsUK-UCL
  • nucleus Source: UniProtKB
  • perikaryon Source: UniProtKB
  • 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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300863

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi216H → A: Reduces histone deacetylase activity. 1 Publication1
Mutagenesisi611H → A: Reduces histone deacetylase activity. 1 Publication1

Organism-specific databases

DisGeNETi10013.
MalaCardsiHDAC6.
MIMi300863. phenotype.
OpenTargetsiENSG00000094631.
Orphaneti163966. X-linked dominant chondrodysplasia, Chassaing-Lacombe type.
PharmGKBiPA29231.

Chemistry databases

ChEMBLiCHEMBL1865.
DrugBankiDB06603. Panobinostat.
DB06176. Romidepsin.
DB02546. Vorinostat.
GuidetoPHARMACOLOGYi2618.

Polymorphism and mutation databases

BioMutaiHDAC6.
DMDMi205371758.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001147031 – 1215Histone deacetylase 6Add BLAST1215

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22PhosphoserineCombined sources1
Modified residuei33Omega-N-methylarginineBy similarity1
Modified residuei1016PhosphothreonineCombined sources1
Modified residuei1021PhosphothreonineCombined sources1
Modified residuei1027PhosphothreonineCombined sources1
Modified residuei1031PhosphothreonineCombined sources1
Modified residuei1034PhosphothreonineCombined sources1
Modified residuei1035PhosphoserineCombined sources1
Modified residuei1040PhosphothreonineCombined sources1

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

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UBN7.
PaxDbiQ9UBN7.
PeptideAtlasiQ9UBN7.
PRIDEiQ9UBN7.

PTM databases

iPTMnetiQ9UBN7.
PhosphoSitePlusiQ9UBN7.

Expressioni

Gene expression databases

BgeeiENSG00000094631.
CleanExiHS_HDAC6.
ExpressionAtlasiQ9UBN7. baseline and differential.
GenevisibleiQ9UBN7. HS.

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. Interacts with FAM65B (PubMed:24687993).By similarity11 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
EGFRP0053311EBI-301697,EBI-297353
PRKCAP172522EBI-301697,EBI-1383528
taxP034094EBI-301697,EBI-5236464From a different organism.

GO - Molecular functioni

  • alpha-tubulin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • dynein complex binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • Hsp90 protein binding Source: BHF-UCL
  • microtubule binding Source: UniProtKB
  • misfolded protein binding Source: Reactome
  • polyubiquitin binding Source: BHF-UCL
  • tau protein binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi115330. 242 interactors.
DIPiDIP-27544N.
IntActiQ9UBN7. 119 interactors.
MINTiMINT-4905696.
STRINGi9606.ENSP00000334061.

Chemistry databases

BindingDBiQ9UBN7.

Structurei

Secondary structure

11215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi481 – 484Combined sources4
Helixi487 – 490Combined sources4
Helixi505 – 516Combined sources12
Turni517 – 522Combined sources6
Beta strandi523 – 526Combined sources4
Helixi533 – 536Combined sources4
Turni537 – 539Combined sources3
Helixi542 – 550Combined sources9
Helixi551 – 553Combined sources3
Helixi556 – 563Combined sources8
Beta strandi566 – 568Combined sources3
Helixi575 – 593Combined sources19
Turni594 – 596Combined sources3
Beta strandi599 – 603Combined sources5
Beta strandi621 – 623Combined sources3
Helixi625 – 637Combined sources13
Beta strandi643 – 647Combined sources5
Beta strandi649 – 651Combined sources3
Helixi654 – 659Combined sources6
Turni660 – 662Combined sources3
Beta strandi666 – 673Combined sources8
Turni675 – 678Combined sources4
Helixi694 – 696Combined sources3
Beta strandi699 – 705Combined sources7
Helixi712 – 721Combined sources10
Helixi723 – 730Combined sources8
Beta strandi733 – 739Combined sources7
Beta strandi742 – 744Combined sources3
Turni748 – 750Combined sources3
Helixi756 – 766Combined sources11
Helixi770 – 772Combined sources3
Beta strandi774 – 778Combined sources5
Helixi784 – 798Combined sources15
Helixi814 – 827Combined sources14
Turni828 – 830Combined sources3
Helixi1116 – 1118Combined sources3
Turni1134 – 1136Combined sources3
Beta strandi1140 – 1145Combined sources6
Turni1146 – 1148Combined sources3
Beta strandi1151 – 1153Combined sources3
Turni1155 – 1158Combined sources4
Helixi1160 – 1168Combined sources9
Beta strandi1172 – 1175Combined sources4
Turni1176 – 1178Combined sources3
Beta strandi1181 – 1183Combined sources3
Turni1184 – 1187Combined sources4
Beta strandi1188 – 1190Combined sources3
Helixi1193 – 1195Combined sources3
Helixi1196 – 1206Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C5KX-ray1.55A1109-1215[»]
3GV4X-ray1.72A1109-1215[»]
3PHDX-ray3.00A/B/C/D1109-1215[»]
5B8DX-ray1.05A1109-1213[»]
5EDUX-ray2.79A/B479-835[»]
5KH3X-ray1.60A1109-1213[»]
5KH7X-ray1.70A1109-1213[»]
5KH9X-ray1.07A1109-1213[»]
ProteinModelPortaliQ9UBN7.
SMRiQ9UBN7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBN7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni87 – 404Histone deacetylase 1Add BLAST318
Regioni482 – 800Histone deacetylase 2Add BLAST319
Regioni1154 – 1156Ubiquitin binding3
Regioni1182 – 1189Ubiquitin binding8

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1131 – 1192UBP-typePROSITE-ProRule annotationAdd BLAST62

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1343. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062809.
HOGENOMiHOG000004769.
HOVERGENiHBG051894.
InParanoidiQ9UBN7.
KOiK11407.
OMAiRYINAHM.
OrthoDBiEOG091G0210.
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. 2 hits.
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. AlignAdd to basket

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

        10         20         30         40         50
MTSTGQDSTT TRQRRSRQNP QSPPQDSSVT SKRNIKKGAV PRSIPNLAEV
60 70 80 90 100
KKKGKMKKLG QAMEEDLIVG LQGMDLNLEA EALAGTGLVL DEQLNEFHCL
110 120 130 140 150
WDDSFPEGPE RLHAIKEQLI QEGLLDRCVS FQARFAEKEE LMLVHSLEYI
160 170 180 190 200
DLMETTQYMN EGELRVLADT YDSVYLHPNS YSCACLASGS VLRLVDAVLG
210 220 230 240 250
AEIRNGMAII RPPGHHAQHS LMDGYCMFNH VAVAARYAQQ KHRIRRVLIV
260 270 280 290 300
DWDVHHGQGT QFTFDQDPSV LYFSIHRYEQ GRFWPHLKAS NWSTTGFGQG
310 320 330 340 350
QGYTINVPWN QVGMRDADYI AAFLHVLLPV ALEFQPQLVL VAAGFDALQG
360 370 380 390 400
DPKGEMAATP AGFAQLTHLL MGLAGGKLIL SLEGGYNLRA LAEGVSASLH
410 420 430 440 450
TLLGDPCPML ESPGAPCRSA QASVSCALEA LEPFWEVLVR STETVERDNM
460 470 480 490 500
EEDNVEESEE EGPWEPPVLP ILTWPVLQSR TGLVYDQNMM NHCNLWDSHH
510 520 530 540 550
PEVPQRILRI MCRLEELGLA GRCLTLTPRP ATEAELLTCH SAEYVGHLRA
560 570 580 590 600
TEKMKTRELH RESSNFDSIY ICPSTFACAQ LATGAACRLV EAVLSGEVLN
610 620 630 640 650
GAAVVRPPGH HAEQDAACGF CFFNSVAVAA RHAQTISGHA LRILIVDWDV
660 670 680 690 700
HHGNGTQHMF EDDPSVLYVS LHRYDHGTFF PMGDEGASSQ IGRAAGTGFT
710 720 730 740 750
VNVAWNGPRM GDADYLAAWH RLVLPIAYEF NPELVLVSAG FDAARGDPLG
760 770 780 790 800
GCQVSPEGYA HLTHLLMGLA SGRIILILEG GYNLTSISES MAACTRSLLG
810 820 830 840 850
DPPPLLTLPR PPLSGALASI TETIQVHRRY WRSLRVMKVE DREGPSSSKL
860 870 880 890 900
VTKKAPQPAK PRLAERMTTR EKKVLEAGMG KVTSASFGEE STPGQTNSET
910 920 930 940 950
AVVALTQDQP SEAATGGATL AQTISEAAIG GAMLGQTTSE EAVGGATPDQ
960 970 980 990 1000
TTSEETVGGA ILDQTTSEDA VGGATLGQTT SEEAVGGATL AQTTSEAAME
1010 1020 1030 1040 1050
GATLDQTTSE EAPGGTELIQ TPLASSTDHQ TPPTSPVQGT TPQISPSTLI
1060 1070 1080 1090 1100
GSLRTLELGS ESQGASESQA PGEENLLGEA AGGQDMADSM LMQGSRGLTD
1110 1120 1130 1140 1150
QAIFYAVTPL PWCPHLVAVC PIPAAGLDVT QPCGDCGTIQ ENWVCLSCYQ
1160 1170 1180 1190 1200
VYCGRYINGH MLQHHGNSGH PLVLSYIDLS AWCYYCQAYV HHQALLDVKN
1210
IAHQNKFGED MPHPH
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_046300994T → I.2 PublicationsCorresponds to variant rs1127346dbSNPEnsembl.1
Natural variantiVAR_0689621200N → D.1 PublicationCorresponds to variant rs151130423dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0445761 – 152Missing in isoform 2. 1 PublicationAdd BLAST152

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001308155.1. NM_001321226.1. [Q9UBN7-1]
NP_001308156.1. NM_001321227.1. [Q9UBN7-1]
NP_001308157.1. NM_001321228.1. [Q9UBN7-1]
NP_001308158.1. NM_001321229.1. [Q9UBN7-1]
NP_006035.2. NM_006044.3. [Q9UBN7-1]
UniGeneiHs.6764.

Genome annotation databases

EnsembliENST00000334136; ENSP00000334061; ENSG00000094631. [Q9UBN7-1]
ENST00000376619; ENSP00000365804; ENSG00000094631. [Q9UBN7-1]
GeneIDi10013.
KEGGihsa:10013.
UCSCiuc004dks.2. human. [Q9UBN7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001308155.1. NM_001321226.1. [Q9UBN7-1]
NP_001308156.1. NM_001321227.1. [Q9UBN7-1]
NP_001308157.1. NM_001321228.1. [Q9UBN7-1]
NP_001308158.1. NM_001321229.1. [Q9UBN7-1]
NP_006035.2. NM_006044.3. [Q9UBN7-1]
UniGeneiHs.6764.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C5KX-ray1.55A1109-1215[»]
3GV4X-ray1.72A1109-1215[»]
3PHDX-ray3.00A/B/C/D1109-1215[»]
5B8DX-ray1.05A1109-1213[»]
5EDUX-ray2.79A/B479-835[»]
5KH3X-ray1.60A1109-1213[»]
5KH7X-ray1.70A1109-1213[»]
5KH9X-ray1.07A1109-1213[»]
ProteinModelPortaliQ9UBN7.
SMRiQ9UBN7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115330. 242 interactors.
DIPiDIP-27544N.
IntActiQ9UBN7. 119 interactors.
MINTiMINT-4905696.
STRINGi9606.ENSP00000334061.

Chemistry databases

BindingDBiQ9UBN7.
ChEMBLiCHEMBL1865.
DrugBankiDB06603. Panobinostat.
DB06176. Romidepsin.
DB02546. Vorinostat.
GuidetoPHARMACOLOGYi2618.

PTM databases

iPTMnetiQ9UBN7.
PhosphoSitePlusiQ9UBN7.

Polymorphism and mutation databases

BioMutaiHDAC6.
DMDMi205371758.

Proteomic databases

EPDiQ9UBN7.
PaxDbiQ9UBN7.
PeptideAtlasiQ9UBN7.
PRIDEiQ9UBN7.

Protocols and materials databases

DNASUi10013.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334136; ENSP00000334061; ENSG00000094631. [Q9UBN7-1]
ENST00000376619; ENSP00000365804; ENSG00000094631. [Q9UBN7-1]
GeneIDi10013.
KEGGihsa:10013.
UCSCiuc004dks.2. human. [Q9UBN7-1]

Organism-specific databases

CTDi10013.
DisGeNETi10013.
GeneCardsiHDAC6.
H-InvDBHIX0016783.
HGNCiHGNC:14064. HDAC6.
HPAiCAB004236.
HPA003714.
HPA026321.
MalaCardsiHDAC6.
MIMi300272. gene.
300863. phenotype.
neXtProtiNX_Q9UBN7.
OpenTargetsiENSG00000094631.
Orphaneti163966. X-linked dominant chondrodysplasia, Chassaing-Lacombe type.
PharmGKBiPA29231.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1343. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062809.
HOGENOMiHOG000004769.
HOVERGENiHBG051894.
InParanoidiQ9UBN7.
KOiK11407.
OMAiRYINAHM.
OrthoDBiEOG091G0210.
PhylomeDBiQ9UBN7.
TreeFamiTF106173.

Enzyme and pathway databases

BioCyciZFISH:HS01799-MONOMER.
BRENDAi3.5.1.98. 2681.
ReactomeiR-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3371511. HSF1 activation.
R-HSA-5617833. Assembly of the primary cilium.
SABIO-RKQ9UBN7.
SignaLinkiQ9UBN7.
SIGNORiQ9UBN7.

Miscellaneous databases

ChiTaRSiHDAC6. human.
EvolutionaryTraceiQ9UBN7.
GeneWikiiHDAC6.
GenomeRNAii10013.
PROiQ9UBN7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000094631.
CleanExiHS_HDAC6.
ExpressionAtlasiQ9UBN7. baseline and differential.
GenevisibleiQ9UBN7. HS.

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. 2 hits.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.