Hdac6
entrez
15185
canonical
uniprot
Q9Z2V5
canonical
ensembl
ENSMUSG00000031161
resolver
ensp
ENSMUSP00000033501
resolver
ensp
ENSMUSP00000111306
resolver
ensp
ENSMUSP00000304736
resolver
ensp
ENSMUSP00000304738
resolver
ensp
ENSMUSP00000304739
resolver
ensp
ENSMUSP00000304741
resolver
ensp
ENSMUSP00000304748
resolver
enst
ENSMUST00000033501
resolver
enst
ENSMUST00000115642
resolver
genesymbol
Hdac6
resolver
uniprot
A0A0A6YYQ7
resolver
uniprot
A0A0K0K1F1
resolver
uniprot
B1AUA6
resolver
uniprot
F6Q3W9
resolver
uniprot
Q3UG37
resolver
uniprot_entry
HDAC6_MOUSE
resolver
uniprot_entry
Q3UG37_MOUSE
resolver
uniprot_sec
A0A0A6YYQ7
resolver
uniprot_sec
A0A0K0K1F1
resolver
uniprot_sec
B1AUA6
resolver
uniprot_sec
F6Q3W9
resolver
amino_acid_sequence
MTSTGQDSSTRQRKSRHNPQSPLQESSATLKRGGKKCAVPHSSPNLAEVKKKGKMKKLSQPAEEDLVVGLQGLDLNPETRVPVGTGLVFDEQLNDFHCLWDDSFPESPERLHAIREQLILEGLLGRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLAETYDSVYLHPNSYSCACLATGSVLRLVDALMGAEIRNGMAVIRPPGHHAQHNLMDGYCMFNHLAVAARYAQKKHRIQRVLIVDWDVHHGQGTQFIFDQDPSVLYFSIHRYEHGRFWPHLKASNWSTIGFGQGQGYTINVPWNQTGMRDADYIAAFLHILLPVASEFQPQLVLVAAGFDALHGDPKGEMAATPAGFAHLTHLLMGLAGGKLILSLEGGYNLRALAKGVSASLHTLLGDPCPMLESCVVPCASAQTSIYCTLEALEPFWEVLERSVETQEEDEVEEAVLEEEEEEGGWEATALPMDTWPLLQNRTGLVYDEKMMSHCNLWDNHHPETPQRILRIMCHLEEVGLAARCLILPARPALDSELLTCHSAEYVEHLRTTEKMKTRDLHREGANFDSIYICPSTFACAKLATGAACRLVEAVLSGEVLNGIAVVRPPGHHAEPNAACGFCFFNSVAVAARHAQIIAGRALRILIVDWDVHHGNGTQHIFEDDPSVLYVSLHRYDRGTFFPMGDEGASSQVGRDAGIGFTVNVPWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLISAGFDAAQGDPLGGCQVTPEGYAHLTHLLMGLAGGRIILILEGGYNLASISESMAACTHSLLGDPPPQLTLLRPPQSGALVSISEVIQVHRKYWRSLRLMKMEDKEECSSSRLVIKKLPPTASPVSAKEMTTPKGKVPEESVRKTIAALPGKESTLGQAKSKMAKAVLAQGQSSEQAAKGTTLDLATSKETVGGATTDLWASAAAPENFPNQTTSVEALGETEPTPPASHTNKQTTGASPLQGVTAQQSLQLGVLSTLELSREAEEAHDSEEGLLGEAAGGQDMNSLMLTQGFGDFNTQDVFYAVTPLSWCPHLMAVCPIPAAGLDVSQPCKTCGTVQENWVCLTCYQVYCSRYVNAHMVCHHEASEHPLVLSCVDLSTWCYVCQAYVHHEDLQDVKNAAHQNKFGEDMPHSH
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
function
FUNCTION: Deacetylates a wide range of non-histone substrates (PubMed:12606581, PubMed:19893491, PubMed:26746851, PubMed:27737934, PubMed:35075301). Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin (PubMed:19893491, PubMed:27737934, PubMed:12606581). Required for cilia disassembly via deacetylation of alpha-tubulin (By similarity). Alpha-tubulin deacetylation results in destabilization of dynamic microtubules (PubMed:12486003). Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (By similarity). Deacetylates SQSTM1 (By similarity). Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity (By similarity). Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI (PubMed:26746851). 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 (By similarity). 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 (By similarity). 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 (By similarity). Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons (By similarity). Deacetylates PRDM16 (PubMed:35075301). Promotes odontoblast differentiation following IPO7-mediated nuclear import and subsequent repression of RUNX2 expression (PubMed:35922041). 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 (By similarity). Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy (PubMed:22819792). {ECO:0000250|UniProtKB:D3ZVD8, ECO:0000250|UniProtKB:Q9UBN7, ECO:0000269|PubMed:12486003, ECO:0000269|PubMed:12606581, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:22819792, ECO:0000269|PubMed:26746851, ECO:0000269|PubMed:27737934, ECO:0000269|PubMed:35075301, ECO:0000269|PubMed:35922041, ECO:0000269|PubMed:9891014}.
uniprot
proteins
mass_dalton
125787
uniprot
proteins
mutagenesis
MUTAGEN 66; /note="L->A: Abolishes accumulation in the cytoplasm; when associated with A-70."; /evidence="ECO:0000269|PubMed:10873806"; MUTAGEN 70; /note="L->A: Abolishes accumulation in the cytoplasm; when associated with A-66."; /evidence="ECO:0000269|PubMed:10873806"; MUTAGEN 250..255; /note="DWDVHH->NWNVVV: Does not affect accumulation in the cytoplasm."; /evidence="ECO:0000269|PubMed:10873806"; MUTAGEN 648..651; /note="DVHH->NVVV: Does not affect accumulation in the cytoplasm."; /evidence="ECO:0000269|PubMed:10873806"; MUTAGEN 988; /note="L->A: Does not affect accumulation in the cytoplasm; when associated with A-991."; /evidence="ECO:0000269|PubMed:10873806"; MUTAGEN 991; /note="L->A: Does not affect accumulation in the cytoplasm; when associated with A-988."; /evidence="ECO:0000269|PubMed:10873806
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9UBN7}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by AURKA; phosphorylation increases HDAC6-mediated deacetylation of alpha-tubulin and subsequent disassembly of cilia. {ECO:0000250|UniProtKB:Q9UBN7}.; PTM: Ubiquitinated. Its polyubiquitination however does not lead to its degradation. {ECO:0000250|UniProtKB:Q9UBN7}.; PTM: Sumoylated in vitro. {ECO:0000250|UniProtKB:Q9UBN7}.
uniprot
proteins
protein_family
HD type 2 subfamily
uniprot
proteins
protein_family
Histone deacetylase family
uniprot
proteins
pubmed
10873806
uniprot
proteins
pubmed
11533236
uniprot
proteins
pubmed
12486003
uniprot
proteins
pubmed
12606581
uniprot
proteins
pubmed
16933150
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19893491
uniprot
proteins
pubmed
20675388
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22819792
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
26746851
uniprot
proteins
pubmed
27737934
uniprot
proteins
pubmed
35075301
uniprot
proteins
pubmed
35922041
uniprot
proteins
pubmed
9891014
uniprot
proteins
sequence_length
1149
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10873806, ECO:0000269|PubMed:12606581, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:35922041}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19893491}. Nucleus {ECO:0000269|PubMed:10873806, ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:35922041}. Perikaryon {ECO:0000269|PubMed:16933150}. Cell projection, dendrite {ECO:0000269|PubMed:16933150}. Cell projection, axon {ECO:0000269|PubMed:16933150}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9UBN7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UBN7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9UBN7}. Note=Mainly cytoplasmic where it is associated with microtubules (PubMed:10873806, PubMed:19893491). Can shuttle between the cytoplasm and the nucleus (PubMed:10873806). Found exclusively in the cytoplasm in proliferative cells with a fraction found in the nucleus during differentiation (PubMed:10873806). {ECO:0000269|PubMed:10873806, ECO:0000269|PubMed:19893491}.
uniprot
proteins