HDAC6_MOUSE
ID HDAC6_MOUSE Reviewed; 1149 AA.
AC Q9Z2V5; B1AUA6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Histone deacetylase 6;
DE Short=HD6;
DE EC=3.5.1.98 {ECO:0000269|PubMed:9891014};
DE AltName: Full=Histone deacetylase mHDA2 {ECO:0000303|PubMed:9891014};
DE AltName: Full=Tubulin-lysine deacetylase HDAC6 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q9UBN7};
GN Name=Hdac6 {ECO:0000312|MGI:MGI:1333752};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=C57BL/6J; TISSUE=Fetus;
RX PubMed=9891014; DOI=10.1074/jbc.274.4.2440;
RA Verdel A., Khochbin S.;
RT "Identification of a new family of higher eukaryotic histone deacetylases.
RT Coordinate expression of differentiation-dependent chromatin modifiers.";
RL J. Biol. Chem. 274:2440-2445(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH CBFA2T3.
RX PubMed=11533236; DOI=10.1128/mcb.21.19.6470-6483.2001;
RA Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA Downing J.R., Meyers S., Hiebert S.W.;
RT "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with
RT multiple histone deacetylases and binds mSin3A through its oligomerization
RT domain.";
RL Mol. Cell. Biol. 21:6470-6483(2001).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16933150; DOI=10.1007/s11064-006-9127-6;
RA Southwood C.M., Peppi M., Dryden S., Tainsky M.A., Gow A.;
RT "Microtubule deacetylases, SirT2 and HDAC6, in the nervous system.";
RL Neurochem. Res. 32:187-195(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-43 AND SER-1148, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, INTERACTION WITH CYLD AND MICROTUBULES, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=19893491; DOI=10.1038/emboj.2009.317;
RA Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.;
RT "CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and
RT increasing the levels of acetylated tubulin.";
RL EMBO J. 29:131-144(2010).
RN [7]
RP INTERACTION WITH ZMYND15.
RX PubMed=20675388; DOI=10.1074/jbc.m110.116418;
RA Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
RA Saunders L., Verdin E., Charo I.F.;
RT "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor
RT essential for spermiogenesis and male fertility.";
RL J. Biol. Chem. 285:31418-31426(2010).
RN [8]
RP FUNCTION IN AUTOPHAGY, AND SUBCELLULAR LOCATION.
RX PubMed=22819792; DOI=10.1016/j.neuint.2012.07.010;
RA Gal J., Bang Y., Choi H.J.;
RT "SIRT2 interferes with autophagy-mediated degradation of protein aggregates
RT in neuronal cells under proteasome inhibition.";
RL Neurochem. Int. 61:992-1000(2012).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-32, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4)
CC (PubMed:9891014). Histone deacetylation gives a tag for epigenetic
CC repression and plays an important role in transcriptional regulation,
CC cell cycle progression and developmental events (PubMed:9891014).
CC Histone deacetylases act via the formation of large multiprotein
CC complexes (PubMed:9891014). In addition to histones, deacetylates other
CC proteins: plays a central role in microtubule-dependent cell motility
CC by mediating deacetylation of tubulin (PubMed:19893491). Promotes
CC deacetylation of CTTN, leading to actin polymerization, promotion of
CC autophagosome-lysosome fusion and completion of autophagy (By
CC similarity). In addition to its protein deacetylase activity, plays a
CC key role in the degradation of misfolded proteins: when misfolded
CC proteins are too abundant to be degraded by the chaperone refolding
CC system and the ubiquitin-proteasome, mediates the transport of
CC misfolded proteins to a cytoplasmic juxtanuclear structure called
CC aggresome (By similarity). Probably acts as an adapter that recognizes
CC polyubiquitinated misfolded proteins and target them to the aggresome,
CC facilitating their clearance by autophagy (PubMed:22819792).
CC {ECO:0000250|UniProtKB:Q9UBN7, ECO:0000269|PubMed:19893491,
CC ECO:0000269|PubMed:22819792, ECO:0000269|PubMed:9891014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000269|PubMed:9891014};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000269|PubMed:9891014};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[alpha-tubulin] = acetate + L-lysyl-
CC [alpha-tubulin]; Xref=Rhea:RHEA:21548, Rhea:RHEA-COMP:11278,
CC Rhea:RHEA-COMP:11279, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000250|UniProtKB:Q9UBN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21549;
CC Evidence={ECO:0000250|UniProtKB:Q9UBN7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UBN7};
CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UBN7};
CC -!- SUBUNIT: Interacts with SIRT2 (via both phosphorylated,
CC unphosphorylated, active or inactive forms); the interaction is
CC necessary for the complex to interact with alpha-tubulin (By
CC similarity). Under proteasome impairment conditions, interacts with UBD
CC via its histone deacetylase 1 and UBP-type zinc-finger regions (By
CC similarity). Interacts with BBIP1, CBFA2T3, CYLD, DDIT3/CHOP, ZMYND15,
CC F-actin and HDAC11 (PubMed:11533236, PubMed:19893491, PubMed:20675388).
CC Interacts with RIPOR2; this interaction occurs during early myogenic
CC differentiation and prevents HDAC6 to deacetylate tubulin (By
CC similarity). Interacts with DYSF; this interaction occurs during early
CC myogenic differentiation (By similarity). Interacts with TPPP;
CC inhibiting the tubulin deacetylase activity of HDAC6 (By similarity).
CC Interacts with DYNLL1 (By similarity). Interacts with ATP13A2; the
CC interaction results in recruitment of HDAC6 to lysosomes to promote
CC CTTN deacetylation (By similarity). {ECO:0000250|UniProtKB:Q9UBN7,
CC ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:19893491,
CC ECO:0000269|PubMed:20675388}.
CC -!- INTERACTION:
CC Q9Z2V5; P31750: Akt1; NbExp=2; IntAct=EBI-1009256, EBI-298707;
CC Q9Z2V5; Q80TQ2: Cyld; NbExp=3; IntAct=EBI-1009256, EBI-943859;
CC Q9Z2V5; Q99N13: Hdac9; NbExp=2; IntAct=EBI-1009256, EBI-645361;
CC Q9Z2V5; O55131: Septin7; NbExp=3; IntAct=EBI-1009256, EBI-772161;
CC Q9Z2V5; D3ZEY0: Ccdc141; Xeno; NbExp=3; IntAct=EBI-1009256, EBI-21448776;
CC Q9Z2V5; P21146: GRK2; Xeno; NbExp=2; IntAct=EBI-1009256, EBI-1036401;
CC Q9Z2V5; P62973; Xeno; NbExp=2; IntAct=EBI-1009256, EBI-16124826;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19893491}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19893491}. Nucleus
CC {ECO:0000269|PubMed:19893491}. Perikaryon
CC {ECO:0000269|PubMed:16933150}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16933150}. Cell projection, axon
CC {ECO:0000269|PubMed:16933150}. Note=It is mainly cytoplasmic, where it
CC is associated with microtubules. {ECO:0000269|PubMed:19893491}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the cortex. Expressed in
CC Purkinje cells. Detected in keratinocytes (at protein level).
CC {ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:19893491}.
CC -!- PTM: Phosphorylated by AURKA. {ECO:0000250|UniProtKB:Q9UBN7}.
CC -!- PTM: Ubiquitinated. Its polyubiquitination however does not lead to its
CC degradation. {ECO:0000250|UniProtKB:Q9UBN7}.
CC -!- PTM: Sumoylated in vitro. {ECO:0000250|UniProtKB:Q9UBN7}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AF006603; AAD09835.2; -; mRNA.
DR EMBL; AL670169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40845.1; -.
DR PIR; T13964; T13964.
DR RefSeq; NP_001123888.1; NM_001130416.1.
DR RefSeq; NP_034543.3; NM_010413.3.
DR RefSeq; XP_006527630.1; XM_006527567.2.
DR RefSeq; XP_017173877.1; XM_017318388.1.
DR RefSeq; XP_017173878.1; XM_017318389.1.
DR AlphaFoldDB; Q9Z2V5; -.
DR SMR; Q9Z2V5; -.
DR BioGRID; 200263; 61.
DR DIP; DIP-36461N; -.
DR IntAct; Q9Z2V5; 43.
DR MINT; Q9Z2V5; -.
DR STRING; 10090.ENSMUSP00000111306; -.
DR BindingDB; Q9Z2V5; -.
DR ChEMBL; CHEMBL2878; -.
DR DrugCentral; Q9Z2V5; -.
DR iPTMnet; Q9Z2V5; -.
DR PhosphoSitePlus; Q9Z2V5; -.
DR EPD; Q9Z2V5; -.
DR jPOST; Q9Z2V5; -.
DR MaxQB; Q9Z2V5; -.
DR PaxDb; Q9Z2V5; -.
DR PeptideAtlas; Q9Z2V5; -.
DR PRIDE; Q9Z2V5; -.
DR ProteomicsDB; 269771; -.
DR Antibodypedia; 3788; 1139 antibodies from 48 providers.
DR DNASU; 15185; -.
DR Ensembl; ENSMUST00000033501; ENSMUSP00000033501; ENSMUSG00000031161.
DR Ensembl; ENSMUST00000115642; ENSMUSP00000111306; ENSMUSG00000031161.
DR GeneID; 15185; -.
DR KEGG; mmu:15185; -.
DR UCSC; uc009snh.2; mouse.
DR CTD; 10013; -.
DR MGI; MGI:1333752; Hdac6.
DR VEuPathDB; HostDB:ENSMUSG00000031161; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000159563; -.
DR HOGENOM; CLU_007727_2_1_1; -.
DR InParanoid; Q9Z2V5; -.
DR OMA; HEASGHP; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; Q9Z2V5; -.
DR TreeFam; TF106173; -.
DR BRENDA; 3.5.1.98; 3474.
DR Reactome; R-MMU-3371511; HSF1 activation.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-5617833; Cilium Assembly.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR BioGRID-ORCS; 15185; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q9Z2V5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z2V5; protein.
DR Bgee; ENSMUSG00000031161; Expressed in entorhinal cortex and 251 other tissues.
DR ExpressionAtlas; Q9Z2V5; baseline and differential.
DR Genevisible; Q9Z2V5; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR GO; GO:0070840; F:dynein complex binding; ISO:MGI.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:MGI.
DR GO; GO:0033558; F:protein lysine deacetylase activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0042903; F:tubulin deacetylase activity; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070842; P:aggresome assembly; IGI:MGI.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0071218; P:cellular response to misfolded protein; IMP:MGI.
DR GO; GO:0035967; P:cellular response to topologically incorrect protein; ISO:MGI.
DR GO; GO:0061523; P:cilium disassembly; ISO:MGI.
DR GO; GO:0048668; P:collateral sprouting; IMP:MGI.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; IMP:CACAO.
DR GO; GO:0070846; P:Hsp90 deacetylation; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
DR GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR GO; GO:0051646; P:mitochondrion localization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0043242; P:negative regulation of protein-containing complex disassembly; ISO:MGI.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISO:MGI.
DR GO; GO:0034983; P:peptidyl-lysine deacetylation; IMP:ARUK-UCL.
DR GO; GO:0070845; P:polyubiquitinated misfolded protein transport; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
DR GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IGI:ParkinsonsUK-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ARUK-UCL.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:0006476; P:protein deacetylation; IDA:MGI.
DR GO; GO:0031648; P:protein destabilization; IMP:CACAO.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISO:MGI.
DR GO; GO:0032984; P:protein-containing complex disassembly; IGI:MGI.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0070848; P:response to growth factor; ISO:MGI.
DR GO; GO:0051788; P:response to misfolded protein; ISO:MGI.
DR GO; GO:0090042; P:tubulin deacetylation; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.800.20; -; 2.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00850; Hist_deacetyl; 2.
DR Pfam; PF02148; zf-UBP; 1.
DR PRINTS; PR01270; HDASUPER.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF52768; SSF52768; 2.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Chromatin regulator; Cytoplasm;
KW Cytoskeleton; Hydrolase; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1149
FT /note="Histone deacetylase 6"
FT /id="PRO_0000114704"
FT ZN_FING 1045..1143
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..403
FT /note="Histone deacetylase 1"
FT REGION 481..799
FT /note="Histone deacetylase 2"
FT REGION 954..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1090
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT REGION 1116..1123
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT ACT_SITE 610
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT BINDING 1047
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1049
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1067
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1079
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1082
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1087
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1094
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1098
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 1120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 958
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT MOD_RES 961
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT MOD_RES 967
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT MOD_RES 971
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN7"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 133
FT /note="R -> W (in Ref. 1; AAD09835)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="V -> I (in Ref. 1; AAD09835)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="T -> I (in Ref. 1; AAD09835)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="D -> G (in Ref. 1; AAD09835)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="M -> S (in Ref. 1; AAD09835)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="I -> V (in Ref. 1; AAD09835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126..1127
FT /note="HE -> QD (in Ref. 1; AAD09835)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1149 AA; 125787 MW; D5F73BA3F79AF520 CRC64;
MTSTGQDSST RQRKSRHNPQ SPLQESSATL KRGGKKCAVP HSSPNLAEVK KKGKMKKLSQ
PAEEDLVVGL QGLDLNPETR VPVGTGLVFD EQLNDFHCLW DDSFPESPER LHAIREQLIL
EGLLGRCVSF QARFAEKEEL MLVHSLEYID LMETTQYMNE GELRVLAETY DSVYLHPNSY
SCACLATGSV LRLVDALMGA EIRNGMAVIR PPGHHAQHNL MDGYCMFNHL AVAARYAQKK
HRIQRVLIVD WDVHHGQGTQ FIFDQDPSVL YFSIHRYEHG RFWPHLKASN WSTIGFGQGQ
GYTINVPWNQ TGMRDADYIA AFLHILLPVA SEFQPQLVLV AAGFDALHGD PKGEMAATPA
GFAHLTHLLM GLAGGKLILS LEGGYNLRAL AKGVSASLHT LLGDPCPMLE SCVVPCASAQ
TSIYCTLEAL EPFWEVLERS VETQEEDEVE EAVLEEEEEE GGWEATALPM DTWPLLQNRT
GLVYDEKMMS HCNLWDNHHP ETPQRILRIM CHLEEVGLAA RCLILPARPA LDSELLTCHS
AEYVEHLRTT EKMKTRDLHR EGANFDSIYI CPSTFACAKL ATGAACRLVE AVLSGEVLNG
IAVVRPPGHH AEPNAACGFC FFNSVAVAAR HAQIIAGRAL RILIVDWDVH HGNGTQHIFE
DDPSVLYVSL HRYDRGTFFP MGDEGASSQV GRDAGIGFTV NVPWNGPRMG DADYLAAWHR
LVLPIAYEFN PELVLISAGF DAAQGDPLGG CQVTPEGYAH LTHLLMGLAG GRIILILEGG
YNLASISESM AACTHSLLGD PPPQLTLLRP PQSGALVSIS EVIQVHRKYW RSLRLMKMED
KEECSSSRLV IKKLPPTASP VSAKEMTTPK GKVPEESVRK TIAALPGKES TLGQAKSKMA
KAVLAQGQSS EQAAKGTTLD LATSKETVGG ATTDLWASAA APENFPNQTT SVEALGETEP
TPPASHTNKQ TTGASPLQGV TAQQSLQLGV LSTLELSREA EEAHDSEEGL LGEAAGGQDM
NSLMLTQGFG DFNTQDVFYA VTPLSWCPHL MAVCPIPAAG LDVSQPCKTC GTVQENWVCL
TCYQVYCSRY VNAHMVCHHE ASEHPLVLSC VDLSTWCYVC QAYVHHEDLQ DVKNAAHQNK
FGEDMPHSH
