HDAC6
entrez
10013
canonical
uniprot
Q9UBN7
canonical
ensembl
ENSG00000094631
resolver
ensp
ENSP00000334061
resolver
ensp
ENSP00000365795
resolver
ensp
ENSP00000393916
resolver
ensp
ENSP00000402751
resolver
ensp
ENSP00000403370
resolver
ensp
ENSP00000494230
resolver
ensp
ENSP00000494447
resolver
ensp
ENSP00000495932
resolver
ensp
ENSP00000496013
resolver
ensp
ENSP00000496046
resolver
ensp
ENSP00000496727
resolver
ensp
ENSP00000513273
resolver
ensp
ENSP00000513468
resolver
enst
ENST00000438518
resolver
enst
ENST00000441703
resolver
enst
ENST00000462730
resolver
enst
ENST00000465269
resolver
enst
ENST00000647398
resolver
enst
ENST00000697348
resolver
genesymbol
HDAC6
resolver
genesymbol_syn
KIAA0901
resolver
hgnc
HGNC:14064
resolver
uniprot
A0A2R8YD35
resolver
uniprot
A0ACM8PXH0
resolver
uniprot
B4DZH6
resolver
uniprot
C9JEF4
resolver
uniprot
E9PEH1
resolver
uniprot
O94975
resolver
uniprot
Q6NT75
resolver
uniprot
Q7L3E5
resolver
uniprot
Q96CY0
resolver
uniprot
Q9BRX7
resolver
uniprot_entry
A0ACM8PXH0_HUMAN
resolver
uniprot_entry
B4DZH6_HUMAN
resolver
uniprot_entry
HDAC6_HUMAN
resolver
uniprot_entry
Q9BRX7_HUMAN
resolver
uniprot_sec
A0A2R8YD35
resolver
uniprot_sec
C9JEF4
resolver
uniprot_sec
E9PEH1
resolver
uniprot_sec
O94975
resolver
uniprot_sec
Q6NT75
resolver
uniprot_sec
Q7L3E5
resolver
uniprot_sec
Q96CY0
resolver
amino_acid_sequence
MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH
uniprot
proteins
disease_involvement
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 intellectual disability. {ECO:0000269|PubMed:20181727}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
function
FUNCTION: Deacetylates a wide range of non-histone substrates (PubMed:12024216, PubMed:18606987, PubMed:20308065, PubMed:24882211, PubMed:26246421, PubMed:30538141, PubMed:31857589, PubMed:30770470, PubMed:38534334, PubMed:39567688). Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin (PubMed:12024216, PubMed:20308065, PubMed:26246421). Required for cilia disassembly via deacetylation of alpha-tubulin (PubMed:17604723, PubMed:26246421). Alpha-tubulin deacetylation results in destabilization of dynamic microtubules (By similarity). Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (PubMed:30538141). Deacetylates SQSTM1 (PubMed:31857589). Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity (PubMed:18606987). Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI (By similarity). Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities (PubMed:24882211). Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage (PubMed:30770470). Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition (By similarity). Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis (PubMed:38534334). Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons (PubMed:26080397). Deacetylates PRDM16 (By similarity). Acts as a valine sensor by binding to valine through the primate-specific SE14 repeat region (PubMed:39567688). In valine deprivation conditions, translocates from the cytoplasm to the nucleus where it deacetylates TET2 which promotes TET2-dependent DNA demethylation, leading to DNA damage (PubMed:39567688). Promotes odontoblast differentiation following IPO7-mediated nuclear import and subsequent repression of RUNX2 expression (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 (PubMed:17846173). Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy (PubMed:17846173). Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer (PubMed:24413532). {ECO:0000250|UniProtKB:D3ZVD8, ECO:0000250|UniProtKB:Q9Z2V5, ECO:0000269|PubMed:12024216, ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18606987, ECO:0000269|PubMed:20308065, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:24882211, ECO:0000269|PubMed:26080397, ECO:0000269|PubMed:26246421, ECO:0000269|PubMed:30538141, ECO:0000269|PubMed:30770470, ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:38534334, ECO:0000269|PubMed:39567688}.; FUNCTION: (Microbial infection) Deacetylates the SARS-CoV-2 N protein which promotes association of the viral N protein with human G3BP1, leading to disruption of cellular stress granule formation and facilitating viral replication. {ECO:0000269|PubMed:39135075}.
uniprot
proteins
mass_dalton
131419
uniprot
proteins
mutagenesis
MUTAGEN 216; /note="H->A: Reduces histone deacetylase activity. Does not affect HDAC6-mediated deacetylation of alpha-tubulin. Abolishes HDAC6-mediated deacetylation of alpha-tubulin; when associated with A-611."; /evidence="ECO:0000269|PubMed:12354939, ECO:0000269|PubMed:26246421, ECO:0000269|PubMed:38534334"; MUTAGEN 611; /note="H->A: Reduces histone deacetylase activity. Abolishes HDAC6-mediated deacetylation of alpha-tubulin. Abolishes HDAC6-mediated deacetylation of alpha-tubulin; when associated with A-216."; /evidence="ECO:0000269|PubMed:12354939, ECO:0000269|PubMed:26246421, ECO:0000269|PubMed:38534334
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:24882211}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by AURKA; phosphorylation increases HDAC6-mediated deacetylation of alpha-tubulin and subsequent disassembly of cilia. {ECO:0000269|PubMed:17604723}.; PTM: Ubiquitinated. Its polyubiquitination however does not lead to its degradation. {ECO:0000269|PubMed:12354939}.; PTM: Sumoylated in vitro. {ECO:0000269|PubMed:12032081}.
uniprot
proteins
protein_family
HD type 2 subfamily
uniprot
proteins
protein_family
Histone deacetylase family
uniprot
proteins
pubmed
10048485
uniprot
proteins
pubmed
10220385
uniprot
proteins
pubmed
11533236
uniprot
proteins
pubmed
11948178
uniprot
proteins
pubmed
12024216
uniprot
proteins
pubmed
12032081
uniprot
proteins
pubmed
12354939
uniprot
proteins
pubmed
12620231
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
17516032
uniprot
proteins
pubmed
17604723
uniprot
proteins
pubmed
17846173
uniprot
proteins
pubmed
17872950
uniprot
proteins
pubmed
18606987
uniprot
proteins
pubmed
19033385
uniprot
proteins
pubmed
19081074
uniprot
proteins
pubmed
19893491
uniprot
proteins
pubmed
20102703
uniprot
proteins
pubmed
20181727
uniprot
proteins
pubmed
20308065
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23093407
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24413532
uniprot
proteins
pubmed
24687993
uniprot
proteins
pubmed
24882211
uniprot
proteins
pubmed
25422469
uniprot
proteins
pubmed
26080397
uniprot
proteins
pubmed
26246421
uniprot
proteins
pubmed
30538141
uniprot
proteins
pubmed
30770470
uniprot
proteins
pubmed
31505170
uniprot
proteins
pubmed
31857589
uniprot
proteins
pubmed
38534334
uniprot
proteins
pubmed
39135075
uniprot
proteins
pubmed
39567688
uniprot
proteins
sequence_length
1215
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12024216, ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:26246421, ECO:0000269|PubMed:30770470, ECO:0000269|PubMed:39567688}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12024216}. Nucleus {ECO:0000269|PubMed:24882211, ECO:0000269|PubMed:26080397, ECO:0000269|PubMed:30770470, ECO:0000269|PubMed:39567688}. Perikaryon {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, cilium {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26246421}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26246421}. Note=Mainly cytoplasmic where it is associated with microtubules (PubMed:12024216). Can shuttle between the cytoplasm and the nucleus (PubMed:39567688). Retained in the cytoplasm by binding to valine via the primate-specific SE14 repeat region while valine deprivation induces nuclear localization (PubMed:39567688). Found exclusively in the cytoplasm in proliferative cells with a fraction found in the nucleus during differentiation (By similarity). May translocate to the nucleus following DNA damage (PubMed:30770470). {ECO:0000250|UniProtKB:Q9Z2V5, ECO:0000269|PubMed:12024216, ECO:0000269|PubMed:30770470, ECO:0000269|PubMed:39567688}.
uniprot
proteins