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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: HDAC6_HUMAN A0A024QZ26_HUMAN
LinkDB: HDAC6_HUMAN A0A024QZ26_HUMAN
Original site: HDAC6_HUMAN A0A024QZ26_HUMAN 
ID   HDAC6_HUMAN             Reviewed;        1215 AA.
AC   Q9UBN7; O94975; Q6NT75; Q7L3E5; Q96CY0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   22-NOV-2017, entry version 177.
DE   RecName: Full=Histone deacetylase 6;
DE            Short=HD6;
DE            EC=3.5.1.98;
GN   Name=HDAC6; Synonyms=KIAA0901; ORFNames=JM21;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-994.
RX   PubMed=10220385; DOI=10.1073/pnas.96.9.4868;
RA   Grozinger C.M., Hassig C.A., Schreiber S.L.;
RT   "Three proteins define a class of human histone deacetylases related
RT   to yeast Hda1p.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA   Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [3]
RP   SEQUENCE REVISION.
RA   Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   ILE-994.
RC   TISSUE=Brain;
RA   Strom T.M., Gutwillinger N., Nyakatura G., Hellebrand H., Drescher B.,
RA   Rosenthal A., Meindl A.;
RT   "Transcription map in Xp11.23.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ASP-1200.
RC   TISSUE=Ovary, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
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
RT   with multiple histone deacetylases and binds mSin3A through its
RT   oligomerization domain.";
RL   Mol. Cell. Biol. 21:6470-6483(2001).
RN   [9]
RP   INTERACTION WITH HDAC11.
RX   PubMed=11948178; DOI=10.1074/jbc.M111871200;
RA   Gao L., Cueto M.A., Asselbergs F., Atadja P.;
RT   "Cloning and functional characterization of HDAC11, a novel member of
RT   the human histone deacetylase family.";
RL   J. Biol. Chem. 277:25748-25755(2002).
RN   [10]
RP   SUMOYLATION.
RX   PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
RA   Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
RA   Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
RT   "The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
RT   deacetylase.";
RL   EMBO J. 21:2682-2691(2002).
RN   [11]
RP   UBIQUITINATION, AND MUTAGENESIS OF HIS-216 AND HIS-611.
RX   PubMed=12354939; DOI=10.1073/pnas.172511699;
RA   Hook S.S., Orian A., Cowley S.M., Eisenman R.N.;
RT   "Histone deacetylase 6 binds polyubiquitin through its zinc finger
RT   (PAZ domain) and copurifies with deubiquitinating enzymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13425-13430(2002).
RN   [12]
RP   FUNCTION.
RX   PubMed=12024216; DOI=10.1038/417455a;
RA   Hubbert C., Guardiola A., Shao R., Kawaguchi Y., Ito A., Nixon A.,
RA   Yoshida M., Wang X.-F., Yao T.-P.;
RT   "HDAC6 is a microtubule-associated deacetylase.";
RL   Nature 417:455-458(2002).
RN   [13]
RP   INTERACTION WITH SIRT2.
RX   PubMed=12620231; DOI=10.1016/S1097-2765(03)00038-8;
RA   North B.J., Marshall B.L., Borra M.T., Denu J.M., Verdin E.;
RT   "The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin
RT   deacetylase.";
RL   Mol. Cell 11:437-444(2003).
RN   [14]
RP   PHOSPHORYLATION BY AURKA.
RX   PubMed=17604723; DOI=10.1016/j.cell.2007.04.035;
RA   Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P.,
RA   Golemis E.A.;
RT   "HEF1-dependent Aurora A activation induces disassembly of the primary
RT   cilium.";
RL   Cell 129:1351-1363(2007).
RN   [15]
RP   INTERACTION WITH DDIT3.
RX   PubMed=17872950; DOI=10.1074/jbc.M703735200;
RA   Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
RT   "Critical and functional regulation of CHOP (C/EBP homologous protein)
RT   through the N-terminal portion.";
RL   J. Biol. Chem. 282:35687-35694(2007).
RN   [16]
RP   FUNCTION.
RX   PubMed=17846173; DOI=10.1083/jcb.200611128;
RA   Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D.,
RA   Chin L.S.;
RT   "Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1
RT   to aggresomes via binding to HDAC6.";
RL   J. Cell Biol. 178:1025-1038(2007).
RN   [17]
RP   INTERACTION WITH SIRT2.
RX   PubMed=17516032; DOI=10.1007/s11010-007-9478-6;
RA   Nahhas F., Dryden S.C., Abrams J., Tainsky M.A.;
RT   "Mutations in SIRT2 deacetylase which regulate enzymatic activity but
RT   not its interaction with HDAC6 and tubulin.";
RL   Mol. Cell. Biochem. 303:221-230(2007).
RN   [18]
RP   INTERACTION WITH BBIP10.
RX   PubMed=19081074; DOI=10.1016/j.devcel.2008.11.001;
RA   Loktev A.V., Zhang Q., Beck J.S., Searby C.C., Scheetz T.E., Bazan F.,
RA   Slusarski D.C., Sheffield V.C., Jackson P.K., Nachury M.V.;
RT   "A BBSome subunit links ciliogenesis, microtubule stability and
RT   acetylation.";
RL   Dev. Cell 15:854-865(2008).
RN   [19]
RP   INTERACTION WITH UBD.
RX   PubMed=19033385; DOI=10.1242/jcs.035006;
RA   Kalveram B., Schmidtke G., Groettrup M.;
RT   "The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes
RT   to aggresomes under proteasome inhibition.";
RL   J. Cell Sci. 121:4079-4088(2008).
RN   [20]
RP   ALTERNATIVE SPLICING (ISOFORM 2).
RX   PubMed=20102703; DOI=10.1016/j.bbrc.2010.01.091;
RA   Zhuang Y., Nguyen H.T., Lasky J.A., Cao S., Li C., Hu J., Guo X.,
RA   Burow M.E., Shan B.;
RT   "Requirement of a novel splicing variant of human histone deacetylase
RT   6 for TGF-beta1-mediated gene activation.";
RL   Biochem. Biophys. Res. Commun. 392:608-613(2010).
RN   [21]
RP   INTERACTION WITH CYLD.
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
RT   HDAC6 and increasing the levels of acetylated tubulin.";
RL   EMBO J. 29:131-144(2010).
RN   [22]
RP   INVOLVEMENT IN CDP-PBHM.
RX   PubMed=20181727; DOI=10.1093/hmg/ddq083;
RA   Simon D., Laloo B., Barillot M., Barnetche T., Blanchard C.,
RA   Rooryck C., Marche M., Burgelin I., Coupry I., Chassaing N.,
RA   Gilbert-Dussardier B., Lacombe D., Grosset C., Arveiler B.;
RT   "A mutation in the 3'-UTR of the HDAC6 gene abolishing the post-
RT   transcriptional regulation mediated by hsa-miR-433 is linked to a new
RT   form of dominant X-linked chondrodysplasia.";
RL   Hum. Mol. Genet. 19:2015-2027(2010).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [25]
RP   FUNCTION.
RX   PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
RA   Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
RA   Kim Y.N., Seong J.K., Lee M.O.;
RT   "Differential regulation of estrogen receptor alpha expression in
RT   breast cancer cells by metastasis-associated protein 1.";
RL   Cancer Res. 74:1484-1494(2014).
RN   [26]
RP   INTERACTION WITH DYSF AND RIPOR2.
RX   PubMed=24687993; DOI=10.1096/fj.13-246470;
RA   Balasubramanian A., Kawahara G., Gupta V.A., Rozkalne A., Beauvais A.,
RA   Kunkel L.M., Gussoni E.;
RT   "Fam65b is important for formation of the HDAC6-dysferlin protein
RT   complex during myogenic cell differentiation.";
RL   FASEB J. 28:2955-2969(2014).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1016; THR-1021;
RP   THR-1027; THR-1031; THR-1034; SER-1035 AND THR-1040, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [28]
RP   INTERACTION WITH UBD.
RX   PubMed=25422469; DOI=10.1073/pnas.1403383111;
RA   Theng S.S., Wang W., Mah W.C., Chan C., Zhuo J., Gao Y., Qin H.,
RA   Lim L., Chong S.S., Song J., Lee C.G.;
RT   "Disruption of FAT10-MAD2 binding inhibits tumor progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:E5282-E5291(2014).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1109-1215 IN COMPLEX WITH
RP   ZINC IONS.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human HDAC6 zinc finger domain.";
RL   Submitted (FEB-2008) to the PDB data bank.
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 1109-1215 IN COMPLEX WITH
RP   ZINC IONS AND UBIQUITIN C-TERMINAL PEPTIDE RLRGG.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human HDAC6 zinc finger domain and ubiquitin C-
RT   terminal peptide RLRGG.";
RL   Submitted (APR-2009) to the PDB data bank.
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes (By similarity).
CC       Plays a central role in microtubule-dependent cell motility via
CC       deacetylation of tubulin. Involved in the MTA1-mediated epigenetic
CC       regulation of ESR1 expression in breast cancer. {ECO:0000250,
CC       ECO:0000269|PubMed:12024216, ECO:0000269|PubMed:17846173,
CC       ECO:0000269|PubMed:24413532}.
CC   -!- FUNCTION: 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
CC       refolding system and the ubiquitin-proteasome, mediates the
CC       transport of misfolded proteins to a cytoplasmic juxtanuclear
CC       structure called aggresome. Probably acts as an adapter that
CC       recognizes polyubiquitinated misfolded proteins and target them to
CC       the aggresome, facilitating their clearance by autophagy.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 3 Zn(2+) ions per subunit.;
CC   -!- SUBUNIT: Interacts with ZMYND15 (By similarity). Interacts with
CC       SIRT2 (via both phosphorylated, unphosphorylated, active or
CC       inactive forms); the interaction is necessary for the complex to
CC       interact with alpha-tubulin. Under proteasome impairment
CC       conditions, interacts with UBD via its histone deacetylase 1 and
CC       UBP-type zinc-finger regions. Interacts with BBIP10, CBFA2T3,
CC       CYLD, DDIT3/CHOP, F-actin and HDAC11. Interacts with RIPOR2; this
CC       interaction occurs during early myogenic differentiation and
CC       prevents HDAC6 to deacetylate tubulin (PubMed:24687993). Interacts
CC       with DYSF; this interaction occurs during early myogenic
CC       differentiation (PubMed:24687993). {ECO:0000250,
CC       ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11948178,
CC       ECO:0000269|PubMed:12620231, ECO:0000269|PubMed:17516032,
CC       ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:19033385,
CC       ECO:0000269|PubMed:19081074, ECO:0000269|PubMed:19893491,
CC       ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:25422469,
CC       ECO:0000269|Ref.29, ECO:0000269|Ref.30}.
CC   -!- INTERACTION:
CC       Q9NQ11:ATP13A2; NbExp=2; IntAct=EBI-301697, EBI-6308763;
CC       Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-301697, EBI-714781;
CC       Q62623:Cdc20 (xeno); NbExp=2; IntAct=EBI-301697, EBI-2256532;
CC       Q14247:CTTN; NbExp=3; IntAct=EBI-301697, EBI-351886;
CC       Q60598:Cttn (xeno); NbExp=3; IntAct=EBI-301697, EBI-397955;
CC       Q9NQC7:CYLD; NbExp=4; IntAct=EBI-301697, EBI-2117940;
CC       P00533:EGFR; NbExp=11; IntAct=EBI-301697, EBI-297353;
CC       P21146:GRK2 (xeno); NbExp=3; IntAct=EBI-301697, EBI-1036401;
CC       P17252:PRKCA; NbExp=2; IntAct=EBI-301697, EBI-1383528;
CC       P03409:tax (xeno); NbExp=4; IntAct=EBI-301697, EBI-5236464;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Perikaryon
CC       {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
CC       projection, axon {ECO:0000250}. Note=It is mainly cytoplasmic,
CC       where it is associated with microtubules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=HDAC6p131;
CC         IsoId=Q9UBN7-1; Sequence=Displayed;
CC       Name=2; Synonyms=HDAC6p114;
CC         IsoId=Q9UBN7-2; Sequence=VSP_044576;
CC         Note=Required for TGF-beta1-activated gene expression associated
CC         with epithelial-mesenchymal transition (EMT) in A549 cells.;
CC   -!- PTM: Phosphorylated by AURKA. {ECO:0000269|PubMed:17604723}.
CC   -!- PTM: Ubiquitinated. Its polyubiquitination however does not lead
CC       to its degradation. {ECO:0000269|PubMed:12354939}.
CC   -!- PTM: Sumoylated in vitro. {ECO:0000269|PubMed:12032081}.
CC   -!- DISEASE: Chondrodysplasia with platyspondyly, distinctive
CC       brachydactyly, hydrocephaly, and microphthalmia (CDP-PBHM)
CC       [MIM:300863]: A disease characterized by chondrodysplasia, severe
CC       platyspondyly, hydrocephaly, and facial features with
CC       microphthalmia. Bone abnormalities include a distinctive
CC       metaphyseal cupping of the metacarpals, metatarsals, and
CC       phalanges. Affected females show a milder phenotype with small
CC       stature, sometimes associated with body asymmetry and mild mental
CC       retardation. {ECO:0000269|PubMed:20181727}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA74924.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AF132609; AAD29048.1; -; mRNA.
DR   EMBL; AB020708; BAA74924.2; ALT_INIT; mRNA.
DR   EMBL; AJ011972; CAA09893.1; -; mRNA.
DR   EMBL; AF196971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471224; EAW50748.1; -; Genomic_DNA.
DR   EMBL; BC013737; AAH13737.1; -; mRNA.
DR   EMBL; BC069243; AAH69243.1; -; mRNA.
DR   CCDS; CCDS14306.1; -. [Q9UBN7-1]
DR   RefSeq; NP_001308155.1; NM_001321226.1. [Q9UBN7-1]
DR   RefSeq; NP_001308156.1; NM_001321227.1. [Q9UBN7-1]
DR   RefSeq; NP_001308157.1; NM_001321228.1. [Q9UBN7-1]
DR   RefSeq; NP_001308158.1; NM_001321229.1. [Q9UBN7-1]
DR   RefSeq; NP_006035.2; NM_006044.3. [Q9UBN7-1]
DR   UniGene; Hs.6764; -.
DR   PDB; 3C5K; X-ray; 1.55 A; A=1109-1215.
DR   PDB; 3GV4; X-ray; 1.72 A; A=1109-1215.
DR   PDB; 3PHD; X-ray; 3.00 A; A/B/C/D=1109-1215.
DR   PDB; 5B8D; X-ray; 1.05 A; A=1109-1213.
DR   PDB; 5EDU; X-ray; 2.79 A; A/B=479-835.
DR   PDB; 5KH3; X-ray; 1.60 A; A=1109-1213.
DR   PDB; 5KH7; X-ray; 1.70 A; A=1109-1213.
DR   PDB; 5KH9; X-ray; 1.07 A; A=1109-1213.
DR   PDB; 5WBN; X-ray; 1.64 A; A=1108-1213.
DR   PDB; 5WPB; X-ray; 1.55 A; A=1109-1208.
DR   PDBsum; 3C5K; -.
DR   PDBsum; 3GV4; -.
DR   PDBsum; 3PHD; -.
DR   PDBsum; 5B8D; -.
DR   PDBsum; 5EDU; -.
DR   PDBsum; 5KH3; -.
DR   PDBsum; 5KH7; -.
DR   PDBsum; 5KH9; -.
DR   PDBsum; 5WBN; -.
DR   PDBsum; 5WPB; -.
DR   ProteinModelPortal; Q9UBN7; -.
DR   SMR; Q9UBN7; -.
DR   BioGrid; 115330; 262.
DR   CORUM; Q9UBN7; -.
DR   DIP; DIP-27544N; -.
DR   IntAct; Q9UBN7; 119.
DR   MINT; MINT-4905696; -.
DR   STRING; 9606.ENSP00000334061; -.
DR   BindingDB; Q9UBN7; -.
DR   ChEMBL; CHEMBL1865; -.
DR   DrugBank; DB05015; Belinostat.
DR   DrugBank; DB06603; Panobinostat.
DR   DrugBank; DB06176; Romidepsin.
DR   DrugBank; DB05223; SB939.
DR   DrugBank; DB02546; Vorinostat.
DR   GuidetoPHARMACOLOGY; 2618; -.
DR   iPTMnet; Q9UBN7; -.
DR   PhosphoSitePlus; Q9UBN7; -.
DR   BioMuta; HDAC6; -.
DR   DMDM; 205371758; -.
DR   EPD; Q9UBN7; -.
DR   PaxDb; Q9UBN7; -.
DR   PeptideAtlas; Q9UBN7; -.
DR   PRIDE; Q9UBN7; -.
DR   DNASU; 10013; -.
DR   Ensembl; ENST00000334136; ENSP00000334061; ENSG00000094631. [Q9UBN7-1]
DR   Ensembl; ENST00000376619; ENSP00000365804; ENSG00000094631. [Q9UBN7-1]
DR   GeneID; 10013; -.
DR   KEGG; hsa:10013; -.
DR   UCSC; uc004dks.2; human. [Q9UBN7-1]
DR   CTD; 10013; -.
DR   DisGeNET; 10013; -.
DR   EuPathDB; HostDB:ENSG00000094631.18; -.
DR   GeneCards; HDAC6; -.
DR   H-InvDB; HIX0016783; -.
DR   HGNC; HGNC:14064; HDAC6.
DR   HPA; CAB004236; -.
DR   HPA; HPA003714; -.
DR   HPA; HPA026321; -.
DR   MalaCards; HDAC6; -.
DR   MIM; 300272; gene.
DR   MIM; 300863; phenotype.
DR   neXtProt; NX_Q9UBN7; -.
DR   OpenTargets; ENSG00000094631; -.
DR   Orphanet; 163966; X-linked dominant chondrodysplasia, Chassaing-Lacombe type.
DR   PharmGKB; PA29231; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00530000062809; -.
DR   HOGENOM; HOG000004769; -.
DR   HOVERGEN; HBG051894; -.
DR   InParanoid; Q9UBN7; -.
DR   KO; K11407; -.
DR   OMA; QPHGFCI; -.
DR   OrthoDB; EOG091G0210; -.
DR   PhylomeDB; Q9UBN7; -.
DR   TreeFam; TF106173; -.
DR   BRENDA; 3.5.1.98; 2681.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-3371511; HSF1 activation.
DR   Reactome; R-HSA-5617833; Cilium Assembly.
DR   Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
DR   Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR   SABIO-RK; Q9UBN7; -.
DR   SignaLink; Q9UBN7; -.
DR   SIGNOR; Q9UBN7; -.
DR   ChiTaRS; HDAC6; human.
DR   EvolutionaryTrace; Q9UBN7; -.
DR   GeneWiki; HDAC6; -.
DR   GenomeRNAi; 10013; -.
DR   PRO; PR:Q9UBN7; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000094631; -.
DR   CleanEx; HS_HDAC6; -.
DR   ExpressionAtlas; Q9UBN7; baseline and differential.
DR   Genevisible; Q9UBN7; HS.
DR   GO; GO:0016235; C:aggresome; IDA:BHF-UCL.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR   GO; GO:0031252; C:cell leading edge; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR   GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
DR   GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR   GO; GO:0005875; C:microtubule associated complex; IDA:BHF-UCL.
DR   GO; GO:0005771; C:multivesicular body; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0043014; F:alpha-tubulin binding; IDA:BHF-UCL.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR   GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR   GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
DR   GO; GO:0070840; F:dynein complex binding; IDA:BHF-UCL.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0051879; F:Hsp90 protein binding; IDA:BHF-UCL.
DR   GO; GO:0008017; F:microtubule binding; IDA:BHF-UCL.
DR   GO; GO:0051787; F:misfolded protein binding; EXP:Reactome.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:BHF-UCL.
DR   GO; GO:0048156; F:tau protein binding; IDA:BHF-UCL.
DR   GO; GO:0042903; F:tubulin deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070842; P:aggresome assembly; IMP:BHF-UCL.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:BHF-UCL.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IEA:Ensembl.
DR   GO; GO:0035967; P:cellular response to topologically incorrect protein; IMP:BHF-UCL.
DR   GO; GO:0060271; P:cilium assembly; TAS:Reactome.
DR   GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR   GO; GO:0016575; P:histone deacetylation; IDA:BHF-UCL.
DR   GO; GO:0070846; P:Hsp90 deacetylation; IMP:BHF-UCL.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:BHF-UCL.
DR   GO; GO:0032418; P:lysosome localization; IMP:BHF-UCL.
DR   GO; GO:0051646; P:mitochondrion localization; IEA:Ensembl.
DR   GO; GO:0010727; P:negative regulation of hydrogen peroxide metabolic process; IC:BHF-UCL.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR   GO; GO:0051354; P:negative regulation of oxidoreductase activity; IC:BHF-UCL.
DR   GO; GO:0043242; P:negative regulation of protein complex disassembly; IMP:BHF-UCL.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0034983; P:peptidyl-lysine deacetylation; IMP:BHF-UCL.
DR   GO; GO:0070845; P:polyubiquitinated misfolded protein transport; IMP:BHF-UCL.
DR   GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; IMP:BHF-UCL.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:BHF-UCL.
DR   GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IDA:BHF-UCL.
DR   GO; GO:0010870; P:positive regulation of receptor biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0009967; P:positive regulation of signal transduction; IMP:BHF-UCL.
DR   GO; GO:0043241; P:protein complex disassembly; IEA:Ensembl.
DR   GO; GO:0006476; P:protein deacetylation; IMP:BHF-UCL.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:BHF-UCL.
DR   GO; GO:0060765; P:regulation of androgen receptor signaling pathway; TAS:BHF-UCL.
DR   GO; GO:0010506; P:regulation of autophagy; TAS:ParkinsonsUK-UCL.
DR   GO; GO:1903146; P:regulation of autophagy of mitochondrion; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR   GO; GO:0016241; P:regulation of macroautophagy; IMP:BHF-UCL.
DR   GO; GO:0060632; P:regulation of microtubule-based movement; IC:BHF-UCL.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0010469; P:regulation of receptor activity; IMP:BHF-UCL.
DR   GO; GO:0070848; P:response to growth factor; IMP:BHF-UCL.
DR   GO; GO:0051788; P:response to misfolded protein; IMP:BHF-UCL.
DR   GO; GO:0010033; P:response to organic substance; IMP:BHF-UCL.
DR   GO; GO:0009636; P:response to toxic substance; IMP:BHF-UCL.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0090042; P:tubulin deacetylation; IDA:BHF-UCL.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
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   PANTHER; PTHR10625; PTHR10625; 5.
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   3D-structure; Actin-binding; Alternative splicing; Autophagy;
KW   Cell projection; Chromatin regulator; Complete proteome; Cytoplasm;
KW   Hydrolase; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1215       Histone deacetylase 6.
FT                                /FTId=PRO_0000114703.
FT   ZN_FING    1131   1192       UBP-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00502}.
FT   REGION       87    404       Histone deacetylase 1.
FT   REGION      482    800       Histone deacetylase 2.
FT   REGION     1154   1156       Ubiquitin binding.
FT   REGION     1182   1189       Ubiquitin binding.
FT   ACT_SITE    216    216       1.
FT   ACT_SITE    611    611       2.
FT   METAL      1113   1113       Zinc 1.
FT   METAL      1115   1115       Zinc 1.
FT   METAL      1133   1133       Zinc 3.
FT   METAL      1136   1136       Zinc 3.
FT   METAL      1145   1145       Zinc 2.
FT   METAL      1148   1148       Zinc 2.
FT   METAL      1153   1153       Zinc 3.
FT   METAL      1160   1160       Zinc 3.
FT   METAL      1164   1164       Zinc 2.
FT   METAL      1170   1170       Zinc 2.
FT   METAL      1183   1183       Zinc 1.
FT   METAL      1186   1186       Zinc 1.
FT   MOD_RES      22     22       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      33     33       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q9Z2V5}.
FT   MOD_RES    1016   1016       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1021   1021       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1027   1027       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1031   1031       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1034   1034       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1035   1035       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1040   1040       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   VAR_SEQ       1    152       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_044576.
FT   VARIANT     994    994       T -> I (in dbSNP:rs1127346).
FT                                {ECO:0000269|PubMed:10220385,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_046300.
FT   VARIANT    1200   1200       N -> D (in dbSNP:rs151130423).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_068962.
FT   MUTAGEN     216    216       H->A: Reduces histone deacetylase
FT                                activity. {ECO:0000269|PubMed:12354939}.
FT   MUTAGEN     611    611       H->A: Reduces histone deacetylase
FT                                activity. {ECO:0000269|PubMed:12354939}.
FT   STRAND      481    484       {ECO:0000244|PDB:5EDU}.
FT   HELIX       487    490       {ECO:0000244|PDB:5EDU}.
FT   HELIX       505    516       {ECO:0000244|PDB:5EDU}.
FT   TURN        517    522       {ECO:0000244|PDB:5EDU}.
FT   STRAND      523    526       {ECO:0000244|PDB:5EDU}.
FT   HELIX       533    536       {ECO:0000244|PDB:5EDU}.
FT   TURN        537    539       {ECO:0000244|PDB:5EDU}.
FT   HELIX       542    550       {ECO:0000244|PDB:5EDU}.
FT   HELIX       551    553       {ECO:0000244|PDB:5EDU}.
FT   HELIX       556    563       {ECO:0000244|PDB:5EDU}.
FT   STRAND      566    568       {ECO:0000244|PDB:5EDU}.
FT   HELIX       575    593       {ECO:0000244|PDB:5EDU}.
FT   TURN        594    596       {ECO:0000244|PDB:5EDU}.
FT   STRAND      599    603       {ECO:0000244|PDB:5EDU}.
FT   STRAND      621    623       {ECO:0000244|PDB:5EDU}.
FT   HELIX       625    637       {ECO:0000244|PDB:5EDU}.
FT   STRAND      643    647       {ECO:0000244|PDB:5EDU}.
FT   STRAND      649    651       {ECO:0000244|PDB:5EDU}.
FT   HELIX       654    659       {ECO:0000244|PDB:5EDU}.
FT   TURN        660    662       {ECO:0000244|PDB:5EDU}.
FT   STRAND      666    673       {ECO:0000244|PDB:5EDU}.
FT   TURN        675    678       {ECO:0000244|PDB:5EDU}.
FT   HELIX       694    696       {ECO:0000244|PDB:5EDU}.
FT   STRAND      699    705       {ECO:0000244|PDB:5EDU}.
FT   HELIX       712    721       {ECO:0000244|PDB:5EDU}.
FT   HELIX       723    730       {ECO:0000244|PDB:5EDU}.
FT   STRAND      733    739       {ECO:0000244|PDB:5EDU}.
FT   STRAND      742    744       {ECO:0000244|PDB:5EDU}.
FT   TURN        748    750       {ECO:0000244|PDB:5EDU}.
FT   HELIX       756    766       {ECO:0000244|PDB:5EDU}.
FT   HELIX       770    772       {ECO:0000244|PDB:5EDU}.
FT   STRAND      774    778       {ECO:0000244|PDB:5EDU}.
FT   HELIX       784    798       {ECO:0000244|PDB:5EDU}.
FT   HELIX       814    827       {ECO:0000244|PDB:5EDU}.
FT   TURN        828    830       {ECO:0000244|PDB:5EDU}.
FT   HELIX      1116   1118       {ECO:0000244|PDB:5B8D}.
FT   TURN       1134   1136       {ECO:0000244|PDB:5B8D}.
FT   STRAND     1140   1145       {ECO:0000244|PDB:5B8D}.
FT   TURN       1146   1148       {ECO:0000244|PDB:5B8D}.
FT   STRAND     1151   1153       {ECO:0000244|PDB:5B8D}.
FT   TURN       1155   1158       {ECO:0000244|PDB:5B8D}.
FT   HELIX      1160   1168       {ECO:0000244|PDB:5B8D}.
FT   STRAND     1172   1175       {ECO:0000244|PDB:5B8D}.
FT   TURN       1176   1178       {ECO:0000244|PDB:5B8D}.
FT   STRAND     1181   1183       {ECO:0000244|PDB:5B8D}.
FT   TURN       1184   1187       {ECO:0000244|PDB:5B8D}.
FT   STRAND     1188   1190       {ECO:0000244|PDB:5B8D}.
FT   HELIX      1193   1195       {ECO:0000244|PDB:5B8D}.
FT   HELIX      1196   1206       {ECO:0000244|PDB:5B8D}.
SQ   SEQUENCE   1215 AA;  131419 MW;  6F17731268A33114 CRC64;
     MTSTGQDSTT TRQRRSRQNP QSPPQDSSVT SKRNIKKGAV PRSIPNLAEV KKKGKMKKLG
     QAMEEDLIVG LQGMDLNLEA EALAGTGLVL DEQLNEFHCL WDDSFPEGPE RLHAIKEQLI
     QEGLLDRCVS FQARFAEKEE LMLVHSLEYI DLMETTQYMN EGELRVLADT YDSVYLHPNS
     YSCACLASGS VLRLVDAVLG AEIRNGMAII RPPGHHAQHS LMDGYCMFNH VAVAARYAQQ
     KHRIRRVLIV DWDVHHGQGT QFTFDQDPSV LYFSIHRYEQ GRFWPHLKAS NWSTTGFGQG
     QGYTINVPWN QVGMRDADYI AAFLHVLLPV ALEFQPQLVL VAAGFDALQG DPKGEMAATP
     AGFAQLTHLL MGLAGGKLIL SLEGGYNLRA LAEGVSASLH TLLGDPCPML ESPGAPCRSA
     QASVSCALEA LEPFWEVLVR STETVERDNM EEDNVEESEE EGPWEPPVLP ILTWPVLQSR
     TGLVYDQNMM NHCNLWDSHH PEVPQRILRI MCRLEELGLA GRCLTLTPRP ATEAELLTCH
     SAEYVGHLRA TEKMKTRELH RESSNFDSIY ICPSTFACAQ LATGAACRLV EAVLSGEVLN
     GAAVVRPPGH HAEQDAACGF CFFNSVAVAA RHAQTISGHA LRILIVDWDV HHGNGTQHMF
     EDDPSVLYVS LHRYDHGTFF PMGDEGASSQ IGRAAGTGFT VNVAWNGPRM GDADYLAAWH
     RLVLPIAYEF NPELVLVSAG FDAARGDPLG GCQVSPEGYA HLTHLLMGLA SGRIILILEG
     GYNLTSISES MAACTRSLLG DPPPLLTLPR PPLSGALASI TETIQVHRRY WRSLRVMKVE
     DREGPSSSKL VTKKAPQPAK PRLAERMTTR EKKVLEAGMG KVTSASFGEE STPGQTNSET
     AVVALTQDQP SEAATGGATL AQTISEAAIG GAMLGQTTSE EAVGGATPDQ TTSEETVGGA
     ILDQTTSEDA VGGATLGQTT SEEAVGGATL AQTTSEAAME GATLDQTTSE EAPGGTELIQ
     TPLASSTDHQ TPPTSPVQGT TPQISPSTLI GSLRTLELGS ESQGASESQA PGEENLLGEA
     AGGQDMADSM LMQGSRGLTD QAIFYAVTPL PWCPHLVAVC PIPAAGLDVT QPCGDCGTIQ
     ENWVCLSCYQ VYCGRYINGH MLQHHGNSGH PLVLSYIDLS AWCYYCQAYV HHQALLDVKN
     IAHQNKFGED MPHPH
//
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Ontology (84)   
   GO (84)   
Disease (2)   
   OMIM (2)   
Drug (6)   
   DrugBank (5)   
   CHEMBL-UP (1)   
Chemical reaction (2)   
   KEGG ENZYME (1)   
   SABIO-RK-UP (1)   
Gene (10)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   HGNC (1)   
   ENSEMBL-UP (5)   
Protein sequence (5)   
   RefSeq(pep) (5)   
DNA sequence (7)   
   EMBL (7)   
3D Structure (10)   
   PDB (10)   
Protein domain (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (25)   
   PubMed (25)   
Enzyme (1)   
   BRENDA (1)   
All databases (162)   

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ID   A0A024QZ26_HUMAN        Unreviewed;      1215 AA.
AC   A0A024QZ26;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   22-NOV-2017, entry version 33.
DE   RecName: Full=Histone deacetylase {ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|SAAS:SAAS00894283};
GN   Name=HDAC6 {ECO:0000313|EMBL:EAW50747.1};
GN   ORFNames=hCG_19817 {ECO:0000313|EMBL:EAW50747.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:EAW50747.1};
RN   [1] {ECO:0000313|EMBL:EAW50747.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D.,
RA   Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q.,
RA   Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G.,
RA   Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S.,
RA   Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J.,
RA   Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R.,
RA   Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A.,
RA   Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K.,
RA   Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V.,
RA   Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z.,
RA   Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A.,
RA   Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V.,
RA   Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B.,
RA   Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J.,
RA   Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C.,
RA   Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L.,
RA   Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S.,
RA   Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A.,
RA   Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D.,
RA   Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L.,
RA   Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N.,
RA   Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S.,
RA   Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F.,
RA   Kline L., Koduru S., Love A., Mann F., May D., McCawley S.,
RA   McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K.,
RA   Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N.,
RA   Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M.,
RA   Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F.,
RA   Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A.,
RA   Mi H., Lazareva B., Hatton T., Narechania A., Diemer K.,
RA   Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R.,
RA   Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J.,
RA   Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H.,
RA   Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D.,
RA   Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A.,
RA   Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S.,
RA   Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L.,
RA   Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W.,
RA   McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M.,
RA   Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW50747.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00894298}.
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DR   EMBL; CH471224; EAW50746.1; -; Genomic_DNA.
DR   EMBL; CH471224; EAW50747.1; -; Genomic_DNA.
DR   RefSeq; NP_001308155.1; NM_001321226.1.
DR   RefSeq; NP_001308156.1; NM_001321227.1.
DR   RefSeq; NP_001308157.1; NM_001321228.1.
DR   RefSeq; NP_001308158.1; NM_001321229.1.
DR   RefSeq; NP_006035.2; NM_006044.3.
DR   UniGene; Hs.6764; -.
DR   SMR; A0A024QZ26; -.
DR   GeneID; 10013; -.
DR   KEGG; hsa:10013; -.
DR   CTD; 10013; -.
DR   EuPathDB; HostDB:ENSG00000094631.18; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   KO; K11407; -.
DR   OMA; QPHGFCI; -.
DR   OrthoDB; EOG091G0210; -.
DR   GenomeRNAi; 10013; -.
DR   Bgee; ENSG00000094631; -.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR   GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0042903; F:tubulin deacetylase activity; IEA:Ensembl.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070842; P:aggresome assembly; IEA:Ensembl.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IEA:Ensembl.
DR   GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR   GO; GO:0070846; P:Hsp90 deacetylation; IEA:Ensembl.
DR   GO; GO:0051646; P:mitochondrion localization; IEA:Ensembl.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR   GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0043241; P:protein complex disassembly; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR   GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
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   PANTHER; PTHR10625; PTHR10625; 5.
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   4: Predicted;
KW   Chromatin regulator {ECO:0000256|SAAS:SAAS00894233};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00870288};
KW   Nucleus {ECO:0000256|SAAS:SAAS00894277};
KW   Transcription {ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|SAAS:SAAS00894290}.
FT   DOMAIN     1131   1192       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   ZN_FING    1131   1192       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
SQ   SEQUENCE   1215 AA;  131419 MW;  6F17731268A33114 CRC64;
     MTSTGQDSTT TRQRRSRQNP QSPPQDSSVT SKRNIKKGAV PRSIPNLAEV KKKGKMKKLG
     QAMEEDLIVG LQGMDLNLEA EALAGTGLVL DEQLNEFHCL WDDSFPEGPE RLHAIKEQLI
     QEGLLDRCVS FQARFAEKEE LMLVHSLEYI DLMETTQYMN EGELRVLADT YDSVYLHPNS
     YSCACLASGS VLRLVDAVLG AEIRNGMAII RPPGHHAQHS LMDGYCMFNH VAVAARYAQQ
     KHRIRRVLIV DWDVHHGQGT QFTFDQDPSV LYFSIHRYEQ GRFWPHLKAS NWSTTGFGQG
     QGYTINVPWN QVGMRDADYI AAFLHVLLPV ALEFQPQLVL VAAGFDALQG DPKGEMAATP
     AGFAQLTHLL MGLAGGKLIL SLEGGYNLRA LAEGVSASLH TLLGDPCPML ESPGAPCRSA
     QASVSCALEA LEPFWEVLVR STETVERDNM EEDNVEESEE EGPWEPPVLP ILTWPVLQSR
     TGLVYDQNMM NHCNLWDSHH PEVPQRILRI MCRLEELGLA GRCLTLTPRP ATEAELLTCH
     SAEYVGHLRA TEKMKTRELH RESSNFDSIY ICPSTFACAQ LATGAACRLV EAVLSGEVLN
     GAAVVRPPGH HAEQDAACGF CFFNSVAVAA RHAQTISGHA LRILIVDWDV HHGNGTQHMF
     EDDPSVLYVS LHRYDHGTFF PMGDEGASSQ IGRAAGTGFT VNVAWNGPRM GDADYLAAWH
     RLVLPIAYEF NPELVLVSAG FDAARGDPLG GCQVSPEGYA HLTHLLMGLA SGRIILILEG
     GYNLTSISES MAACTRSLLG DPPPLLTLPR PPLSGALASI TETIQVHRRY WRSLRVMKVE
     DREGPSSSKL VTKKAPQPAK PRLAERMTTR EKKVLEAGMG KVTSASFGEE STPGQTNSET
     AVVALTQDQP SEAATGGATL AQTISEAAIG GAMLGQTTSE EAVGGATPDQ TTSEETVGGA
     ILDQTTSEDA VGGATLGQTT SEEAVGGATL AQTTSEAAME GATLDQTTSE EAPGGTELIQ
     TPLASSTDHQ TPPTSPVQGT TPQISPSTLI GSLRTLELGS ESQGASESQA PGEENLLGEA
     AGGQDMADSM LMQGSRGLTD QAIFYAVTPL PWCPHLVAVC PIPAAGLDVT QPCGDCGTIQ
     ENWVCLSCYQ VYCGRYINGH MLQHHGNSGH PLVLSYIDLS AWCYYCQAYV HHQALLDVKN
     IAHQNKFGED MPHPH
//
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Ontology (28)   
   GO (28)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (5)   
   RefSeq(pep) (5)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (50)   

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