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Histone deacetylase 6 (HD6) (EC 3.5.1.98)

 HDAC6_HUMAN             Reviewed;        1215 AA.
Q9UBN7; O94975; Q6NT75; Q7L3E5; Q96CY0;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 2.
22-NOV-2017, entry version 177.
RecName: Full=Histone deacetylase 6;
Short=HD6;
EC=3.5.1.98;
Name=HDAC6; Synonyms=KIAA0901; ORFNames=JM21;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-994.
PubMed=10220385; DOI=10.1073/pnas.96.9.4868;
Grozinger C.M., Hassig C.A., Schreiber S.L.;
"Three proteins define a class of human histone deacetylases related
to yeast Hda1p.";
Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[3]
SEQUENCE REVISION.
Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-994.
TISSUE=Brain;
Strom T.M., Gutwillinger N., Nyakatura G., Hellebrand H., Drescher B.,
Rosenthal A., Meindl A.;
"Transcription map in Xp11.23.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ASP-1200.
TISSUE=Ovary, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH CBFA2T3.
PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
Downing J.R., Meyers S., Hiebert S.W.;
"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
with multiple histone deacetylases and binds mSin3A through its
oligomerization domain.";
Mol. Cell. Biol. 21:6470-6483(2001).
[9]
INTERACTION WITH HDAC11.
PubMed=11948178; DOI=10.1074/jbc.M111871200;
Gao L., Cueto M.A., Asselbergs F., Atadja P.;
"Cloning and functional characterization of HDAC11, a novel member of
the human histone deacetylase family.";
J. Biol. Chem. 277:25748-25755(2002).
[10]
SUMOYLATION.
PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
deacetylase.";
EMBO J. 21:2682-2691(2002).
[11]
UBIQUITINATION, AND MUTAGENESIS OF HIS-216 AND HIS-611.
PubMed=12354939; DOI=10.1073/pnas.172511699;
Hook S.S., Orian A., Cowley S.M., Eisenman R.N.;
"Histone deacetylase 6 binds polyubiquitin through its zinc finger
(PAZ domain) and copurifies with deubiquitinating enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 99:13425-13430(2002).
[12]
FUNCTION.
PubMed=12024216; DOI=10.1038/417455a;
Hubbert C., Guardiola A., Shao R., Kawaguchi Y., Ito A., Nixon A.,
Yoshida M., Wang X.-F., Yao T.-P.;
"HDAC6 is a microtubule-associated deacetylase.";
Nature 417:455-458(2002).
[13]
INTERACTION WITH SIRT2.
PubMed=12620231; DOI=10.1016/S1097-2765(03)00038-8;
North B.J., Marshall B.L., Borra M.T., Denu J.M., Verdin E.;
"The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin
deacetylase.";
Mol. Cell 11:437-444(2003).
[14]
PHOSPHORYLATION BY AURKA.
PubMed=17604723; DOI=10.1016/j.cell.2007.04.035;
Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P.,
Golemis E.A.;
"HEF1-dependent Aurora A activation induces disassembly of the primary
cilium.";
Cell 129:1351-1363(2007).
[15]
INTERACTION WITH DDIT3.
PubMed=17872950; DOI=10.1074/jbc.M703735200;
Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
"Critical and functional regulation of CHOP (C/EBP homologous protein)
through the N-terminal portion.";
J. Biol. Chem. 282:35687-35694(2007).
[16]
FUNCTION.
PubMed=17846173; DOI=10.1083/jcb.200611128;
Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D.,
Chin L.S.;
"Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1
to aggresomes via binding to HDAC6.";
J. Cell Biol. 178:1025-1038(2007).
[17]
INTERACTION WITH SIRT2.
PubMed=17516032; DOI=10.1007/s11010-007-9478-6;
Nahhas F., Dryden S.C., Abrams J., Tainsky M.A.;
"Mutations in SIRT2 deacetylase which regulate enzymatic activity but
not its interaction with HDAC6 and tubulin.";
Mol. Cell. Biochem. 303:221-230(2007).
[18]
INTERACTION WITH BBIP10.
PubMed=19081074; DOI=10.1016/j.devcel.2008.11.001;
Loktev A.V., Zhang Q., Beck J.S., Searby C.C., Scheetz T.E., Bazan F.,
Slusarski D.C., Sheffield V.C., Jackson P.K., Nachury M.V.;
"A BBSome subunit links ciliogenesis, microtubule stability and
acetylation.";
Dev. Cell 15:854-865(2008).
[19]
INTERACTION WITH UBD.
PubMed=19033385; DOI=10.1242/jcs.035006;
Kalveram B., Schmidtke G., Groettrup M.;
"The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes
to aggresomes under proteasome inhibition.";
J. Cell Sci. 121:4079-4088(2008).
[20]
ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=20102703; DOI=10.1016/j.bbrc.2010.01.091;
Zhuang Y., Nguyen H.T., Lasky J.A., Cao S., Li C., Hu J., Guo X.,
Burow M.E., Shan B.;
"Requirement of a novel splicing variant of human histone deacetylase
6 for TGF-beta1-mediated gene activation.";
Biochem. Biophys. Res. Commun. 392:608-613(2010).
[21]
INTERACTION WITH CYLD.
PubMed=19893491; DOI=10.1038/emboj.2009.317;
Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.;
"CYLD negatively regulates cell-cycle progression by inactivating
HDAC6 and increasing the levels of acetylated tubulin.";
EMBO J. 29:131-144(2010).
[22]
INVOLVEMENT IN CDP-PBHM.
PubMed=20181727; DOI=10.1093/hmg/ddq083;
Simon D., Laloo B., Barillot M., Barnetche T., Blanchard C.,
Rooryck C., Marche M., Burgelin I., Coupry I., Chassaing N.,
Gilbert-Dussardier B., Lacombe D., Grosset C., Arveiler B.;
"A mutation in the 3'-UTR of the HDAC6 gene abolishing the post-
transcriptional regulation mediated by hsa-miR-433 is linked to a new
form of dominant X-linked chondrodysplasia.";
Hum. Mol. Genet. 19:2015-2027(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
FUNCTION.
PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
Kim Y.N., Seong J.K., Lee M.O.;
"Differential regulation of estrogen receptor alpha expression in
breast cancer cells by metastasis-associated protein 1.";
Cancer Res. 74:1484-1494(2014).
[26]
INTERACTION WITH DYSF AND RIPOR2.
PubMed=24687993; DOI=10.1096/fj.13-246470;
Balasubramanian A., Kawahara G., Gupta V.A., Rozkalne A., Beauvais A.,
Kunkel L.M., Gussoni E.;
"Fam65b is important for formation of the HDAC6-dysferlin protein
complex during myogenic cell differentiation.";
FASEB J. 28:2955-2969(2014).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1016; THR-1021;
THR-1027; THR-1031; THR-1034; SER-1035 AND THR-1040, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
INTERACTION WITH UBD.
PubMed=25422469; DOI=10.1073/pnas.1403383111;
Theng S.S., Wang W., Mah W.C., Chan C., Zhuo J., Gao Y., Qin H.,
Lim L., Chong S.S., Song J., Lee C.G.;
"Disruption of FAT10-MAD2 binding inhibits tumor progression.";
Proc. Natl. Acad. Sci. U.S.A. 111:E5282-E5291(2014).
[29]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1109-1215 IN COMPLEX WITH
ZINC IONS.
Structural genomics consortium (SGC);
"Crystal structure of human HDAC6 zinc finger domain.";
Submitted (FEB-2008) to the PDB data bank.
[30]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 1109-1215 IN COMPLEX WITH
ZINC IONS AND UBIQUITIN C-TERMINAL PEPTIDE RLRGG.
Structural genomics consortium (SGC);
"Crystal structure of human HDAC6 zinc finger domain and ubiquitin C-
terminal peptide RLRGG.";
Submitted (APR-2009) to the PDB data bank.
-!- FUNCTION: 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. {ECO:0000250,
ECO:0000269|PubMed:12024216, ECO:0000269|PubMed:17846173,
ECO:0000269|PubMed:24413532}.
-!- FUNCTION: 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 ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 3 Zn(2+) ions per subunit.;
-!- SUBUNIT: 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 RIPOR2; this
interaction occurs during early myogenic differentiation and
prevents HDAC6 to deacetylate tubulin (PubMed:24687993). Interacts
with DYSF; this interaction occurs during early myogenic
differentiation (PubMed:24687993). {ECO:0000250,
ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11948178,
ECO:0000269|PubMed:12620231, ECO:0000269|PubMed:17516032,
ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:19033385,
ECO:0000269|PubMed:19081074, ECO:0000269|PubMed:19893491,
ECO:0000269|PubMed:24687993, ECO:0000269|PubMed:25422469,
ECO:0000269|Ref.29, ECO:0000269|Ref.30}.
-!- INTERACTION:
Q9NQ11:ATP13A2; NbExp=2; IntAct=EBI-301697, EBI-6308763;
Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-301697, EBI-714781;
Q62623:Cdc20 (xeno); NbExp=2; IntAct=EBI-301697, EBI-2256532;
Q14247:CTTN; NbExp=3; IntAct=EBI-301697, EBI-351886;
Q60598:Cttn (xeno); NbExp=3; IntAct=EBI-301697, EBI-397955;
Q9NQC7:CYLD; NbExp=4; IntAct=EBI-301697, EBI-2117940;
P00533:EGFR; NbExp=11; IntAct=EBI-301697, EBI-297353;
P21146:GRK2 (xeno); NbExp=3; IntAct=EBI-301697, EBI-1036401;
P17252:PRKCA; NbExp=2; IntAct=EBI-301697, EBI-1383528;
P03409:tax (xeno); NbExp=4; IntAct=EBI-301697, EBI-5236464;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Perikaryon
{ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
projection, axon {ECO:0000250}. Note=It is mainly cytoplasmic,
where it is associated with microtubules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=HDAC6p131;
IsoId=Q9UBN7-1; Sequence=Displayed;
Name=2; Synonyms=HDAC6p114;
IsoId=Q9UBN7-2; Sequence=VSP_044576;
Note=Required for TGF-beta1-activated gene expression associated
with epithelial-mesenchymal transition (EMT) in A549 cells.;
-!- PTM: Phosphorylated by AURKA. {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}.
-!- 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 mental
retardation. {ECO:0000269|PubMed:20181727}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA74924.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF132609; AAD29048.1; -; mRNA.
EMBL; AB020708; BAA74924.2; ALT_INIT; mRNA.
EMBL; AJ011972; CAA09893.1; -; mRNA.
EMBL; AF196971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471224; EAW50748.1; -; Genomic_DNA.
EMBL; BC013737; AAH13737.1; -; mRNA.
EMBL; BC069243; AAH69243.1; -; mRNA.
CCDS; CCDS14306.1; -. [Q9UBN7-1]
RefSeq; NP_001308155.1; NM_001321226.1. [Q9UBN7-1]
RefSeq; NP_001308156.1; NM_001321227.1. [Q9UBN7-1]
RefSeq; NP_001308157.1; NM_001321228.1. [Q9UBN7-1]
RefSeq; NP_001308158.1; NM_001321229.1. [Q9UBN7-1]
RefSeq; NP_006035.2; NM_006044.3. [Q9UBN7-1]
UniGene; Hs.6764; -.
PDB; 3C5K; X-ray; 1.55 A; A=1109-1215.
PDB; 3GV4; X-ray; 1.72 A; A=1109-1215.
PDB; 3PHD; X-ray; 3.00 A; A/B/C/D=1109-1215.
PDB; 5B8D; X-ray; 1.05 A; A=1109-1213.
PDB; 5EDU; X-ray; 2.79 A; A/B=479-835.
PDB; 5KH3; X-ray; 1.60 A; A=1109-1213.
PDB; 5KH7; X-ray; 1.70 A; A=1109-1213.
PDB; 5KH9; X-ray; 1.07 A; A=1109-1213.
PDB; 5WBN; X-ray; 1.64 A; A=1108-1213.
PDB; 5WPB; X-ray; 1.55 A; A=1109-1208.
PDBsum; 3C5K; -.
PDBsum; 3GV4; -.
PDBsum; 3PHD; -.
PDBsum; 5B8D; -.
PDBsum; 5EDU; -.
PDBsum; 5KH3; -.
PDBsum; 5KH7; -.
PDBsum; 5KH9; -.
PDBsum; 5WBN; -.
PDBsum; 5WPB; -.
ProteinModelPortal; Q9UBN7; -.
SMR; Q9UBN7; -.
BioGrid; 115330; 262.
CORUM; Q9UBN7; -.
DIP; DIP-27544N; -.
IntAct; Q9UBN7; 119.
MINT; MINT-4905696; -.
STRING; 9606.ENSP00000334061; -.
BindingDB; Q9UBN7; -.
ChEMBL; CHEMBL1865; -.
DrugBank; DB05015; Belinostat.
DrugBank; DB06603; Panobinostat.
DrugBank; DB06176; Romidepsin.
DrugBank; DB05223; SB939.
DrugBank; DB02546; Vorinostat.
GuidetoPHARMACOLOGY; 2618; -.
iPTMnet; Q9UBN7; -.
PhosphoSitePlus; Q9UBN7; -.
BioMuta; HDAC6; -.
DMDM; 205371758; -.
EPD; Q9UBN7; -.
PaxDb; Q9UBN7; -.
PeptideAtlas; Q9UBN7; -.
PRIDE; Q9UBN7; -.
DNASU; 10013; -.
Ensembl; ENST00000334136; ENSP00000334061; ENSG00000094631. [Q9UBN7-1]
Ensembl; ENST00000376619; ENSP00000365804; ENSG00000094631. [Q9UBN7-1]
GeneID; 10013; -.
KEGG; hsa:10013; -.
UCSC; uc004dks.2; human. [Q9UBN7-1]
CTD; 10013; -.
DisGeNET; 10013; -.
EuPathDB; HostDB:ENSG00000094631.18; -.
GeneCards; HDAC6; -.
H-InvDB; HIX0016783; -.
HGNC; HGNC:14064; HDAC6.
HPA; CAB004236; -.
HPA; HPA003714; -.
HPA; HPA026321; -.
MalaCards; HDAC6; -.
MIM; 300272; gene.
MIM; 300863; phenotype.
neXtProt; NX_Q9UBN7; -.
OpenTargets; ENSG00000094631; -.
Orphanet; 163966; X-linked dominant chondrodysplasia, Chassaing-Lacombe type.
PharmGKB; PA29231; -.
eggNOG; KOG1343; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062809; -.
HOGENOM; HOG000004769; -.
HOVERGEN; HBG051894; -.
InParanoid; Q9UBN7; -.
KO; K11407; -.
OMA; QPHGFCI; -.
OrthoDB; EOG091G0210; -.
PhylomeDB; Q9UBN7; -.
TreeFam; TF106173; -.
BRENDA; 3.5.1.98; 2681.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3371511; HSF1 activation.
Reactome; R-HSA-5617833; Cilium Assembly.
Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
SABIO-RK; Q9UBN7; -.
SignaLink; Q9UBN7; -.
SIGNOR; Q9UBN7; -.
ChiTaRS; HDAC6; human.
EvolutionaryTrace; Q9UBN7; -.
GeneWiki; HDAC6; -.
GenomeRNAi; 10013; -.
PRO; PR:Q9UBN7; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000094631; -.
CleanEx; HS_HDAC6; -.
ExpressionAtlas; Q9UBN7; baseline and differential.
Genevisible; Q9UBN7; HS.
GO; GO:0016235; C:aggresome; IDA:BHF-UCL.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005901; C:caveola; IDA:BHF-UCL.
GO; GO:0031252; C:cell leading edge; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0005875; C:microtubule associated complex; IDA:BHF-UCL.
GO; GO:0005771; C:multivesicular body; TAS:ParkinsonsUK-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0043014; F:alpha-tubulin binding; IDA:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0070840; F:dynein complex binding; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IDA:BHF-UCL.
GO; GO:0008017; F:microtubule binding; IDA:BHF-UCL.
GO; GO:0051787; F:misfolded protein binding; EXP:Reactome.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:BHF-UCL.
GO; GO:0048156; F:tau protein binding; IDA:BHF-UCL.
GO; GO:0042903; F:tubulin deacetylase activity; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0070842; P:aggresome assembly; IMP:BHF-UCL.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:BHF-UCL.
GO; GO:0071218; P:cellular response to misfolded protein; IEA:Ensembl.
GO; GO:0035967; P:cellular response to topologically incorrect protein; IMP:BHF-UCL.
GO; GO:0060271; P:cilium assembly; TAS:Reactome.
GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:0016575; P:histone deacetylation; IDA:BHF-UCL.
GO; GO:0070846; P:Hsp90 deacetylation; IMP:BHF-UCL.
GO; GO:0006886; P:intracellular protein transport; IMP:BHF-UCL.
GO; GO:0032418; P:lysosome localization; IMP:BHF-UCL.
GO; GO:0051646; P:mitochondrion localization; IEA:Ensembl.
GO; GO:0010727; P:negative regulation of hydrogen peroxide metabolic process; IC:BHF-UCL.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
GO; GO:0051354; P:negative regulation of oxidoreductase activity; IC:BHF-UCL.
GO; GO:0043242; P:negative regulation of protein complex disassembly; IMP:BHF-UCL.
GO; GO:0045861; P:negative regulation of proteolysis; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; IGI:ParkinsonsUK-UCL.
GO; GO:0034983; P:peptidyl-lysine deacetylation; IMP:BHF-UCL.
GO; GO:0070845; P:polyubiquitinated misfolded protein transport; IMP:BHF-UCL.
GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; IMP:BHF-UCL.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:BHF-UCL.
GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IDA:BHF-UCL.
GO; GO:0010870; P:positive regulation of receptor biosynthetic process; IMP:BHF-UCL.
GO; GO:0009967; P:positive regulation of signal transduction; IMP:BHF-UCL.
GO; GO:0043241; P:protein complex disassembly; IEA:Ensembl.
GO; GO:0006476; P:protein deacetylation; IMP:BHF-UCL.
GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:BHF-UCL.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; TAS:BHF-UCL.
GO; GO:0010506; P:regulation of autophagy; TAS:ParkinsonsUK-UCL.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; TAS:ParkinsonsUK-UCL.
GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; IMP:BHF-UCL.
GO; GO:0060632; P:regulation of microtubule-based movement; IC:BHF-UCL.
GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
GO; GO:0010469; P:regulation of receptor activity; IMP:BHF-UCL.
GO; GO:0070848; P:response to growth factor; IMP:BHF-UCL.
GO; GO:0051788; P:response to misfolded protein; IMP:BHF-UCL.
GO; GO:0010033; P:response to organic substance; IMP:BHF-UCL.
GO; GO:0009636; P:response to toxic substance; IMP:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0090042; P:tubulin deacetylation; IDA:BHF-UCL.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.40.800.20; -; 2.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_dom_sf.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR001607; Znf_UBP.
PANTHER; PTHR10625; PTHR10625; 5.
Pfam; PF00850; Hist_deacetyl; 2.
Pfam; PF02148; zf-UBP; 1.
PRINTS; PR01270; HDASUPER.
SMART; SM00290; ZnF_UBP; 1.
SUPFAM; SSF52768; SSF52768; 2.
PROSITE; PS50271; ZF_UBP; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Autophagy;
Cell projection; Chromatin regulator; Complete proteome; Cytoplasm;
Hydrolase; Metal-binding; Methylation; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1215 Histone deacetylase 6.
/FTId=PRO_0000114703.
ZN_FING 1131 1192 UBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00502}.
REGION 87 404 Histone deacetylase 1.
REGION 482 800 Histone deacetylase 2.
REGION 1154 1156 Ubiquitin binding.
REGION 1182 1189 Ubiquitin binding.
ACT_SITE 216 216 1.
ACT_SITE 611 611 2.
METAL 1113 1113 Zinc 1.
METAL 1115 1115 Zinc 1.
METAL 1133 1133 Zinc 3.
METAL 1136 1136 Zinc 3.
METAL 1145 1145 Zinc 2.
METAL 1148 1148 Zinc 2.
METAL 1153 1153 Zinc 3.
METAL 1160 1160 Zinc 3.
METAL 1164 1164 Zinc 2.
METAL 1170 1170 Zinc 2.
METAL 1183 1183 Zinc 1.
METAL 1186 1186 Zinc 1.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 33 33 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9Z2V5}.
MOD_RES 1016 1016 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1021 1021 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1027 1027 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1031 1031 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1034 1034 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1035 1035 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1040 1040 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 152 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044576.
VARIANT 994 994 T -> I (in dbSNP:rs1127346).
{ECO:0000269|PubMed:10220385,
ECO:0000269|Ref.4}.
/FTId=VAR_046300.
VARIANT 1200 1200 N -> D (in dbSNP:rs151130423).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_068962.
MUTAGEN 216 216 H->A: Reduces histone deacetylase
activity. {ECO:0000269|PubMed:12354939}.
MUTAGEN 611 611 H->A: Reduces histone deacetylase
activity. {ECO:0000269|PubMed:12354939}.
STRAND 481 484 {ECO:0000244|PDB:5EDU}.
HELIX 487 490 {ECO:0000244|PDB:5EDU}.
HELIX 505 516 {ECO:0000244|PDB:5EDU}.
TURN 517 522 {ECO:0000244|PDB:5EDU}.
STRAND 523 526 {ECO:0000244|PDB:5EDU}.
HELIX 533 536 {ECO:0000244|PDB:5EDU}.
TURN 537 539 {ECO:0000244|PDB:5EDU}.
HELIX 542 550 {ECO:0000244|PDB:5EDU}.
HELIX 551 553 {ECO:0000244|PDB:5EDU}.
HELIX 556 563 {ECO:0000244|PDB:5EDU}.
STRAND 566 568 {ECO:0000244|PDB:5EDU}.
HELIX 575 593 {ECO:0000244|PDB:5EDU}.
TURN 594 596 {ECO:0000244|PDB:5EDU}.
STRAND 599 603 {ECO:0000244|PDB:5EDU}.
STRAND 621 623 {ECO:0000244|PDB:5EDU}.
HELIX 625 637 {ECO:0000244|PDB:5EDU}.
STRAND 643 647 {ECO:0000244|PDB:5EDU}.
STRAND 649 651 {ECO:0000244|PDB:5EDU}.
HELIX 654 659 {ECO:0000244|PDB:5EDU}.
TURN 660 662 {ECO:0000244|PDB:5EDU}.
STRAND 666 673 {ECO:0000244|PDB:5EDU}.
TURN 675 678 {ECO:0000244|PDB:5EDU}.
HELIX 694 696 {ECO:0000244|PDB:5EDU}.
STRAND 699 705 {ECO:0000244|PDB:5EDU}.
HELIX 712 721 {ECO:0000244|PDB:5EDU}.
HELIX 723 730 {ECO:0000244|PDB:5EDU}.
STRAND 733 739 {ECO:0000244|PDB:5EDU}.
STRAND 742 744 {ECO:0000244|PDB:5EDU}.
TURN 748 750 {ECO:0000244|PDB:5EDU}.
HELIX 756 766 {ECO:0000244|PDB:5EDU}.
HELIX 770 772 {ECO:0000244|PDB:5EDU}.
STRAND 774 778 {ECO:0000244|PDB:5EDU}.
HELIX 784 798 {ECO:0000244|PDB:5EDU}.
HELIX 814 827 {ECO:0000244|PDB:5EDU}.
TURN 828 830 {ECO:0000244|PDB:5EDU}.
HELIX 1116 1118 {ECO:0000244|PDB:5B8D}.
TURN 1134 1136 {ECO:0000244|PDB:5B8D}.
STRAND 1140 1145 {ECO:0000244|PDB:5B8D}.
TURN 1146 1148 {ECO:0000244|PDB:5B8D}.
STRAND 1151 1153 {ECO:0000244|PDB:5B8D}.
TURN 1155 1158 {ECO:0000244|PDB:5B8D}.
HELIX 1160 1168 {ECO:0000244|PDB:5B8D}.
STRAND 1172 1175 {ECO:0000244|PDB:5B8D}.
TURN 1176 1178 {ECO:0000244|PDB:5B8D}.
STRAND 1181 1183 {ECO:0000244|PDB:5B8D}.
TURN 1184 1187 {ECO:0000244|PDB:5B8D}.
STRAND 1188 1190 {ECO:0000244|PDB:5B8D}.
HELIX 1193 1195 {ECO:0000244|PDB:5B8D}.
HELIX 1196 1206 {ECO:0000244|PDB:5B8D}.
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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