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Histone deacetylase 8 (HD8) (EC 3.5.1.98)

 HDAC8_HUMAN             Reviewed;         377 AA.
Q9BY41; A6ND12; A6ND61; A6NET3; A6NJR3; A8MQ62; B4DKN0; B4DV22;
Q86VC8; Q9NP76; Q9NYH4;
11-APR-2003, integrated into UniProtKB/Swiss-Prot.
11-APR-2003, sequence version 2.
25-OCT-2017, entry version 157.
RecName: Full=Histone deacetylase 8;
Short=HD8;
EC=3.5.1.98;
Name=HDAC8; Synonyms=HDACL1; ORFNames=CDA07;
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), CHARACTERIZATION, AND
FUNCTION.
TISSUE=Kidney;
PubMed=10748112; DOI=10.1074/jbc.M908988199;
Hu E., Chen Z., Fredrickson T., Zhu Y., Kirkpatrick R., Zhang G.-F.,
Johanson K., Sung C.-M., Liu R., Winkler J.;
"Cloning and characterization of a novel human class I histone
deacetylase that functions as a transcription repressor.";
J. Biol. Chem. 275:15254-15264(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION,
AND MUTAGENESIS OF 142-HIS-HIS-143.
TISSUE=Uterus;
PubMed=10926844; DOI=10.1042/bj3500199;
Buggy J.J., Sideris M.L., Mak P., Lorimer D.D., McIntosh B.,
Clark J.M.;
"Cloning and characterization of a novel human histone deacetylase,
HDAC8.";
Biochem. J. 350:199-205(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND
FUNCTION.
TISSUE=Heart;
PubMed=10922473; DOI=10.1016/S0014-5793(00)01813-5;
Van den Wyngaert I., de Vries W., Kremer A., Neefs J.-M.,
Verhasselt P., Luyten W.H.M.L., Kass S.U.;
"Cloning and characterization of human histone deacetylase 8.";
FEBS Lett. 478:77-83(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10756090; DOI=10.1006/geno.2000.6128;
McDonell N., Ramser J., Francis F., Vinet M.-C., Rider S., Sudbrak R.,
Riesselman L., Yaspo M.-L., Reinhardt R., Monaco A.P., Ross F.,
Kahn A., Kearney L., Buckle V., Chelly J.;
"Characterization of a highly complex region in Xq13 and mapping of
three isodicentric breakpoints associated with preleukemia.";
Genomics 64:221-229(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
PubMed=8889548; DOI=10.1101/gr.6.9.791;
Bonaldo M.F., Lennon G., Soares M.B.;
"Normalization and subtraction: two approaches to facilitate gene
discovery.";
Genome Res. 6:791-806(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Pheochromocytoma;
Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z.,
Han Z.;
"A novel gene expressed in human pheochromocytoma.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
TISSUE=Colon, and Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[10]
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).
[11]
INTERACTION WITH PEPB2-MYH11 FUSION PROTEIN.
PubMed=12509458; DOI=10.1128/MCB.23.2.607-619.2003;
Durst K.L., Lutterbach B., Kummalue T., Friedman A.D., Hiebert S.W.;
"The inv(16) fusion protein associates with corepressors via a smooth
muscle myosin heavy-chain domain.";
Mol. Cell. Biol. 23:607-619(2003).
[12]
PHOSPHORYLATION BY PKA, MUTAGENESIS OF SER-39, FUNCTION, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=14701748; DOI=10.1128/MCB.24.2.765-773.2004;
Lee H., Rezai-Zadeh N., Seto E.;
"Negative regulation of histone deacetylase 8 activity by cyclic AMP-
dependent protein kinase A.";
Mol. Cell. Biol. 24:765-773(2004).
[13]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15772115; DOI=10.1096/fj.04-2303fje;
Waltregny D., Glenisson W., Tran S.L., North B.J., Verdin E.,
Colige A., Castronovo V.;
"Histone deacetylase HDAC8 associates with smooth muscle alpha-actin
and is essential for smooth muscle cell contractility.";
FASEB J. 19:966-968(2005).
[14]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=16538051; DOI=10.1097/01.pas.0000188029.63706.31;
de Leval L., Waltregny D., Boniver J., Young R.H., Castronovo V.,
Oliva E.;
"Use of histone deacetylase 8 (HDAC8), a new marker of smooth muscle
differentiation, in the classification of mesenchymal tumors of the
uterus.";
Am. J. Surg. Pathol. 30:319-327(2006).
[15]
INTERACTION WITH SMG5.
PubMed=16809764; DOI=10.1128/MCB.01971-05;
Lee H., Sengupta N., Villagra A., Rezai-Zadeh N., Seto E.;
"Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B
(hEST1B) protein from ubiquitin-mediated degradation.";
Mol. Cell. Biol. 26:5259-5269(2006).
[16]
INVOLVEMENT IN WTS.
PubMed=22889856; DOI=10.1136/jmedgenet-2012-100921;
Harakalova M., van den Boogaard M.J., Sinke R., van Lieshout S.,
van Tuil M.C., Duran K., Renkens I., Terhal P.A., de Kovel C.,
Nijman I.J., van Haelst M., Knoers N.V., van Haaften G.,
Kloosterman W., Hennekam R.C., Cuppen E., Ploos van Amstel H.K.;
"X-exome sequencing identifies a HDAC8 variant in a large pedigree
with X-linked intellectual disability, truncal obesity, gynaecomastia,
hypogonadism and unusual face.";
J. Med. Genet. 49:539-543(2012).
[17]
FUNCTION, AND VARIANTS CDLS5 ARG-180; MET-311; ARG-320 AND ARG-334.
PubMed=22885700; DOI=10.1038/nature11316;
Deardorff M.A., Bando M., Nakato R., Watrin E., Itoh T., Minamino M.,
Saitoh K., Komata M., Katou Y., Clark D., Cole K.E., De Baere E.,
Decroos C., Di Donato N., Ernst S., Francey L.J., Gyftodimou Y.,
Hirashima K., Hullings M., Ishikawa Y., Jaulin C., Kaur M., Kiyono T.,
Lombardi P.M., Magnaghi-Jaulin L., Mortier G.R., Nozaki N.,
Petersen M.B., Seimiya H., Siu V.M., Suzuki Y., Takagaki K.,
Wilde J.J., Willems P.J., Prigent C., Gillessen-Kaesbach G.,
Christianson D.W., Kaiser F.J., Jackson L.G., Hirota T., Krantz I.D.,
Shirahige K.;
"HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin
acetylation cycle.";
Nature 489:313-317(2012).
[18]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH TSA; SAHA;
MS-344; CRA-A AND DIVALENT METAL CATION, ENZYME REGULATION, AND
PHOSPHORYLATION AT SER-39.
PubMed=15242608; DOI=10.1016/j.str.2004.04.012;
Somoza J.R., Skene R.J., Katz B.A., Mol C., Ho J.D., Jennings A.J.,
Luong C., Arvai A., Buggy J.J., Chi E., Tang J., Sang B.-C.,
Verner E., Wynands R., Leahy E.M., Dougan D.R., Snell G., Navre M.,
Knuth M.W., Swanson R.V., McRee D.E., Tari L.W.;
"Structural snapshots of human HDAC8 provide insights into the class I
histone deacetylases.";
Structure 12:1325-1334(2004).
[19]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH DIVALENT METAL
CATION, AND MUTAGENESIS OF ASP-101 AND TYR-306.
PubMed=17721440; DOI=10.1038/sj.embor.7401047;
Vannini A., Volpari C., Gallinari P., Jones P., Mattu M., Carfi A.,
De Francesco R., Steinkuehler C., Di Marco S.;
"Substrate binding to histone deacetylases as shown by the crystal
structure of the HDAC8-substrate complex.";
EMBO Rep. 8:879-884(2007).
[20]
X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEXES WITH PEPTIDE
SUBSTRATE; SAHA; TSA; M-344 AND APHA, ACTIVE SITE, AND MUTAGENESIS OF
ASP-101 AND HIS-143.
PubMed=19053282; DOI=10.1021/bi801610c;
Dowling D.P., Gantt S.L., Gattis S.G., Fierke C.A., Christianson D.W.;
"Structural studies of human histone deacetylase 8 and its site-
specific variants complexed with substrate and inhibitors.";
Biochemistry 47:13554-13563(2008).
-!- 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. Also involved in
the deacetylation of cohesin complex protein SMC3 regulating
release of cohesin complexes from chromatin. May play a role in
smooth muscle cell contractility. {ECO:0000269|PubMed:10748112,
ECO:0000269|PubMed:10922473, ECO:0000269|PubMed:10926844,
ECO:0000269|PubMed:14701748, ECO:0000269|PubMed:22885700}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Note=Binds 1 divalent metal cation per subunit.;
-!- ENZYME REGULATION: Its activity is inhibited by trichostatin A
(TSA), suberoylanilide hydroxamic acid (SAHA), 3-(1-methyl-4-
phenylacetyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide (APHA), 4-
dimethylamino-N-(6-hydroxycarbamoyethyl)benzamide-N-hydroxy-7-(4-
dimethylaminobenzoyl)aminoheptanamide (MS-344), 5-(4-methyl-
benzoylamino)-biphenyl-3,4'-dicarboxylic acid 3-dimethylamide 4'-
hydroxyamide (CRA-A) and butyrate. {ECO:0000269|PubMed:15242608}.
-!- SUBUNIT: Interacts with PEPB2-MYH11, a fusion protein consisting
of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail
region of MYH11 produced by the inversion Inv(16)(p13q22), a
translocation associated with acute myeloid leukemia of M4EO
subtype. The PEPB2-MYH1 fusion protein also interacts with RUNX1,
a well known transcriptional regulator, suggesting that the
interaction with HDAC8 may participate in the conversion of RUNX1
into a constitutive transcriptional repressor. Interacts with
CBFA2T3. Interacts with phosphorylated SMG5/EST1B; this
interaction protects SMG5 from ubiquitin-mediated degradation.
Associates with alpha-SMA (smooth muscle alpha-actin).
{ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:12509458,
ECO:0000269|PubMed:16809764, ECO:0000269|PubMed:17721440}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Excluded from the
nucleoli. Found in the cytoplasm of cells showing smooth muscle
differentiation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1;
IsoId=Q9BY41-1; Sequence=Displayed;
Name=2;
IsoId=Q9BY41-2; Sequence=VSP_007176, VSP_007177;
Note=Derived from EST data.;
Name=3;
IsoId=Q9BY41-3; Sequence=VSP_007174, VSP_007175;
Name=4;
IsoId=Q9BY41-4; Sequence=VSP_043426;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9BY41-5; Sequence=VSP_043427, VSP_007177;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q9BY41-6; Sequence=VSP_043426, VSP_046834, VSP_046835,
VSP_046836;
Note=Gene prediction based on EST data.;
Name=7;
IsoId=Q9BY41-7; Sequence=VSP_046832, VSP_046833;
Note=Gene prediction based on EST data.;
Name=8;
IsoId=Q9BY41-8; Sequence=VSP_047502;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Weakly expressed in most tissues. Expressed at
higher level in heart, brain, kidney and pancreas and also in
liver, lung, placenta, prostate and kidney.
{ECO:0000269|PubMed:10926844, ECO:0000269|PubMed:14701748,
ECO:0000269|PubMed:15772115, ECO:0000269|PubMed:16538051}.
-!- PTM: Phosphorylated by PKA on serine 39. Phosphorylation reduces
deacetylase activity observed preferentially on histones H3 and
H4. {ECO:0000269|PubMed:14701748, ECO:0000269|PubMed:15242608}.
-!- DISEASE: Cornelia de Lange syndrome 5 (CDLS5) [MIM:300882]: A form
of Cornelia de Lange syndrome, a clinically heterogeneous
developmental disorder associated with malformations affecting
multiple systems. It is characterized by facial dysmorphisms,
abnormal hands and feet, growth delay, cognitive retardation,
hirsutism, gastroesophageal dysfunction and cardiac,
ophthalmologic and genitourinary anomalies.
{ECO:0000269|PubMed:22885700}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Wilson-Turner X-linked mental retardation syndrome (WTS)
[MIM:309585]: A neurologic disorder characterized by severe
intellectual disability, dysmorphic facial features, hypogonadism,
short stature, and truncal obesity. Affected females have a milder
phenotype than affected males. {ECO:0000269|PubMed:22889856}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
subfamily. {ECO:0000305}.
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EMBL; AF230097; AAF73076.1; -; mRNA.
EMBL; AF245664; AAF73428.1; -; mRNA.
EMBL; AJ277724; CAB90213.1; -; mRNA.
EMBL; BQ189619; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK296641; BAG59242.1; -; mRNA.
EMBL; AK300895; BAG62534.1; -; mRNA.
EMBL; AA376331; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AI159768; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; T99283; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF212246; AAK14930.1; -; mRNA.
EMBL; AL133500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX295542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050433; AAH50433.1; -; mRNA.
CCDS; CCDS14420.1; -. [Q9BY41-1]
CCDS; CCDS55448.1; -. [Q9BY41-6]
CCDS; CCDS55449.1; -. [Q9BY41-4]
CCDS; CCDS55450.1; -. [Q9BY41-8]
CCDS; CCDS55451.1; -. [Q9BY41-5]
CCDS; CCDS55452.1; -. [Q9BY41-7]
RefSeq; NP_001159890.1; NM_001166418.1. [Q9BY41-4]
RefSeq; NP_001159891.1; NM_001166419.1. [Q9BY41-5]
RefSeq; NP_001159892.1; NM_001166420.1. [Q9BY41-8]
RefSeq; NP_001159894.1; NM_001166422.1. [Q9BY41-7]
RefSeq; NP_001159920.1; NM_001166448.1. [Q9BY41-6]
RefSeq; NP_060956.1; NM_018486.2. [Q9BY41-1]
UniGene; Hs.310536; -.
PDB; 1T64; X-ray; 1.90 A; A/B=1-377.
PDB; 1T67; X-ray; 2.31 A; A=1-377.
PDB; 1T69; X-ray; 2.91 A; A=1-377.
PDB; 1VKG; X-ray; 2.20 A; A/B=1-377.
PDB; 1W22; X-ray; 2.50 A; A/B=1-377.
PDB; 2V5W; X-ray; 2.00 A; A/B=1-377.
PDB; 2V5X; X-ray; 2.25 A; A/B=1-377.
PDB; 3EW8; X-ray; 1.80 A; A=1-377.
PDB; 3EWF; X-ray; 2.50 A; A/B/C/D=1-377.
PDB; 3EZP; X-ray; 2.65 A; A/B=1-377.
PDB; 3EZT; X-ray; 2.85 A; A/B=1-377.
PDB; 3F06; X-ray; 2.55 A; A/B=1-377.
PDB; 3F07; X-ray; 3.30 A; A/B/C=1-377.
PDB; 3F0R; X-ray; 2.54 A; A/B/C=1-377.
PDB; 3MZ3; X-ray; 3.20 A; A/B=1-377.
PDB; 3MZ4; X-ray; 1.84 A; A/B=1-377.
PDB; 3MZ6; X-ray; 2.00 A; A=1-377.
PDB; 3MZ7; X-ray; 1.90 A; A=1-377.
PDB; 3RQD; X-ray; 2.14 A; A/B=1-377.
PDB; 3SFF; X-ray; 2.00 A; A=1-377.
PDB; 3SFH; X-ray; 2.70 A; A=1-377.
PDB; 4QA0; X-ray; 2.24 A; A/B=1-377.
PDB; 4QA1; X-ray; 1.92 A; A/B/C/D=1-377.
PDB; 4QA2; X-ray; 2.38 A; A/B=1-377.
PDB; 4QA3; X-ray; 2.88 A; A/B=1-377.
PDB; 4QA4; X-ray; 1.98 A; A=1-377.
PDB; 4QA5; X-ray; 1.76 A; A/B=1-377.
PDB; 4QA6; X-ray; 2.05 A; A/B=1-377.
PDB; 4QA7; X-ray; 2.31 A; A=1-377.
PDB; 4RN0; X-ray; 1.76 A; A/B=1-377.
PDB; 4RN1; X-ray; 2.18 A; A/B=1-377.
PDB; 4RN2; X-ray; 2.39 A; A/B=1-377.
PDB; 5BWZ; X-ray; 1.59 A; A/B=1-377.
PDB; 5D1B; X-ray; 2.90 A; A/B=1-377.
PDB; 5D1C; X-ray; 1.42 A; A/B=1-377.
PDB; 5D1D; X-ray; 2.01 A; A/B=1-377.
PDB; 5DC5; X-ray; 1.94 A; A/B=1-377.
PDB; 5DC6; X-ray; 1.55 A; A/B=1-377.
PDB; 5DC7; X-ray; 2.30 A; A/B=1-377.
PDB; 5DC8; X-ray; 1.30 A; A/B=1-377.
PDB; 5FCW; X-ray; 1.98 A; A/B=1-377.
PDB; 5THS; X-ray; 1.90 A; A/B=1-377.
PDB; 5THT; X-ray; 2.41 A; A/B/C/D=1-377.
PDB; 5THU; X-ray; 1.95 A; A/B=1-377.
PDB; 5THV; X-ray; 1.87 A; A/B=1-377.
PDB; 5VI6; X-ray; 1.24 A; A=8-377.
PDBsum; 1T64; -.
PDBsum; 1T67; -.
PDBsum; 1T69; -.
PDBsum; 1VKG; -.
PDBsum; 1W22; -.
PDBsum; 2V5W; -.
PDBsum; 2V5X; -.
PDBsum; 3EW8; -.
PDBsum; 3EWF; -.
PDBsum; 3EZP; -.
PDBsum; 3EZT; -.
PDBsum; 3F06; -.
PDBsum; 3F07; -.
PDBsum; 3F0R; -.
PDBsum; 3MZ3; -.
PDBsum; 3MZ4; -.
PDBsum; 3MZ6; -.
PDBsum; 3MZ7; -.
PDBsum; 3RQD; -.
PDBsum; 3SFF; -.
PDBsum; 3SFH; -.
PDBsum; 4QA0; -.
PDBsum; 4QA1; -.
PDBsum; 4QA2; -.
PDBsum; 4QA3; -.
PDBsum; 4QA4; -.
PDBsum; 4QA5; -.
PDBsum; 4QA6; -.
PDBsum; 4QA7; -.
PDBsum; 4RN0; -.
PDBsum; 4RN1; -.
PDBsum; 4RN2; -.
PDBsum; 5BWZ; -.
PDBsum; 5D1B; -.
PDBsum; 5D1C; -.
PDBsum; 5D1D; -.
PDBsum; 5DC5; -.
PDBsum; 5DC6; -.
PDBsum; 5DC7; -.
PDBsum; 5DC8; -.
PDBsum; 5FCW; -.
PDBsum; 5THS; -.
PDBsum; 5THT; -.
PDBsum; 5THU; -.
PDBsum; 5THV; -.
PDBsum; 5VI6; -.
ProteinModelPortal; Q9BY41; -.
SMR; Q9BY41; -.
BioGrid; 120968; 36.
ELM; Q9BY41; -.
IntAct; Q9BY41; 17.
MINT; MINT-5207407; -.
STRING; 9606.ENSP00000362674; -.
BindingDB; Q9BY41; -.
ChEMBL; CHEMBL3192; -.
DrugBank; DB07350; (2E)-N-hydroxy-3-[1-methyl-4-(phenylacetyl)-1H-pyrrol-2-yl]prop-2-enamide.
DrugBank; DB02565; 4-Dimethylamino-N-(6-Hydroxycarbamoyethyl)Benzamide-N-Hydroxy-7-(4-Dimethyla Minobenzoyl)Aminoheptanamide.
DrugBank; DB08168; 7-AMINO-4-METHYL-CHROMEN-2-ONE.
DrugBank; DB05015; Belinostat.
DrugBank; DB02917; N-Hydroxy-4-(Methyl{[5-(2-Pyridinyl)-2-Thienyl]Sulfonyl}Amino)Benzamide.
DrugBank; DB06603; Panobinostat.
DrugBank; DB02546; Vorinostat.
GuidetoPHARMACOLOGY; 2619; -.
iPTMnet; Q9BY41; -.
PhosphoSitePlus; Q9BY41; -.
BioMuta; HDAC8; -.
DMDM; 29839394; -.
EPD; Q9BY41; -.
MaxQB; Q9BY41; -.
PaxDb; Q9BY41; -.
PeptideAtlas; Q9BY41; -.
PRIDE; Q9BY41; -.
DNASU; 55869; -.
Ensembl; ENST00000373554; ENSP00000362655; ENSG00000147099. [Q9BY41-8]
Ensembl; ENST00000373556; ENSP00000362657; ENSG00000147099. [Q9BY41-7]
Ensembl; ENST00000373559; ENSP00000362660; ENSG00000147099. [Q9BY41-6]
Ensembl; ENST00000373573; ENSP00000362674; ENSG00000147099. [Q9BY41-1]
Ensembl; ENST00000373589; ENSP00000362691; ENSG00000147099. [Q9BY41-4]
Ensembl; ENST00000439122; ENSP00000414486; ENSG00000147099. [Q9BY41-5]
GeneID; 55869; -.
KEGG; hsa:55869; -.
UCSC; uc004eau.3; human. [Q9BY41-1]
CTD; 55869; -.
DisGeNET; 55869; -.
EuPathDB; HostDB:ENSG00000147099.19; -.
GeneCards; HDAC8; -.
GeneReviews; HDAC8; -.
HGNC; HGNC:13315; HDAC8.
HPA; HPA048560; -.
MalaCards; HDAC8; -.
MIM; 300269; gene.
MIM; 300882; phenotype.
MIM; 309585; phenotype.
neXtProt; NX_Q9BY41; -.
OpenTargets; ENSG00000147099; -.
Orphanet; 199; Cornelia de Lange syndrome.
Orphanet; 3459; Wilson-Turner syndrome.
PharmGKB; PA37766; -.
eggNOG; KOG1342; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00900000140987; -.
HOGENOM; HOG000225180; -.
HOVERGEN; HBG057112; -.
InParanoid; Q9BY41; -.
KO; K11405; -.
OMA; CGYDANA; -.
OrthoDB; EOG091G0A9R; -.
PhylomeDB; Q9BY41; -.
TreeFam; TF106175; -.
BRENDA; 3.5.1.98; 2681.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
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-3214815; HDACs deacetylate histones.
SABIO-RK; Q9BY41; -.
SIGNOR; Q9BY41; -.
ChiTaRS; HDAC8; human.
EvolutionaryTrace; Q9BY41; -.
GeneWiki; HDAC8; -.
GenomeRNAi; 55869; -.
PRO; PR:Q9BY41; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000147099; -.
CleanEx; HS_HDAC8; -.
ExpressionAtlas; Q9BY41; baseline and differential.
Genevisible; Q9BY41; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IPI:BHF-UCL.
GO; GO:0051879; F:Hsp90 protein binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; IEA:Ensembl.
GO; GO:0035984; P:cellular response to trichostatin A; IEA:Ensembl.
GO; GO:0006333; P:chromatin assembly or disassembly; TAS:ProtInc.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IEA:Ensembl.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0071922; P:regulation of cohesin loading; IMP:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
GO; GO:0032204; P:regulation of telomere maintenance; IMP:BHF-UCL.
GO; GO:0007062; P:sister chromatid cohesion; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR003084; His_deacetylse_1.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR023696; Ureohydrolase_domain.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037913; His_deacetylse_1; 1.
PRINTS; PR01270; HDASUPER.
PRINTS; PR01271; HISDACETLASE.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Cytoplasm; Disease mutation; Hydrolase;
Mental retardation; Metal-binding; Nucleus; Obesity; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 377 Histone deacetylase 8.
/FTId=PRO_0000114708.
REGION 14 324 Histone deacetylase.
ACT_SITE 143 143 Proton acceptor.
{ECO:0000269|PubMed:19053282}.
METAL 178 178 Divalent metal cation.
{ECO:0000269|PubMed:17721440}.
METAL 180 180 Divalent metal cation.
{ECO:0000269|PubMed:17721440}.
METAL 267 267 Divalent metal cation.
{ECO:0000269|PubMed:17721440}.
BINDING 101 101 Substrate.
BINDING 151 151 Substrate; via carbonyl oxygen.
BINDING 306 306 Substrate.
MOD_RES 39 39 Phosphoserine.
{ECO:0000269|PubMed:15242608}.
VAR_SEQ 56 146 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043426.
VAR_SEQ 147 377 Missing (in isoform 8).
{ECO:0000303|PubMed:8889548}.
/FTId=VSP_047502.
VAR_SEQ 147 163 DEASGFCYLNDAVLGIL -> RDVCVCGTLQGILKKSK
(in isoform 3). {ECO:0000303|Ref.6}.
/FTId=VSP_007174.
VAR_SEQ 147 158 DEASGFCYLNDA -> ETCVYVALYKAF (in isoform
7). {ECO:0000305}.
/FTId=VSP_046832.
VAR_SEQ 159 377 Missing (in isoform 7). {ECO:0000305}.
/FTId=VSP_046833.
VAR_SEQ 164 377 Missing (in isoform 3).
{ECO:0000303|Ref.6}.
/FTId=VSP_007175.
VAR_SEQ 185 210 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_046834.
VAR_SEQ 246 272 SVLKEVYQAFNPKAVVLQLGADTIAGD -> RYEPPAPNPG
L (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043427.
VAR_SEQ 246 256 SVLKEVYQAFN -> RYEPPAPNPGL (in isoform
6). {ECO:0000305}.
/FTId=VSP_046835.
VAR_SEQ 248 272 LKEVYQAFNPKAVVLQLGADTIAGD -> RTSCPKSRPVEA
AAAACLPHLHSLV (in isoform 2).
{ECO:0000303|PubMed:10756090}.
/FTId=VSP_007176.
VAR_SEQ 257 377 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_046836.
VAR_SEQ 273 377 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:10756090,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_007177.
VARIANT 180 180 H -> R (in CDLS5; dbSNP:rs397515416).
{ECO:0000269|PubMed:22885700}.
/FTId=VAR_069140.
VARIANT 311 311 T -> M (in CDLS5; dbSNP:rs397515417).
{ECO:0000269|PubMed:22885700}.
/FTId=VAR_069141.
VARIANT 320 320 G -> R (in CDLS5; dbSNP:rs398122909).
{ECO:0000269|PubMed:22885700}.
/FTId=VAR_069142.
VARIANT 334 334 H -> R (in CDLS5; dbSNP:rs397515418).
{ECO:0000269|PubMed:22885700}.
/FTId=VAR_069143.
MUTAGEN 39 39 S->A: Enhances the deacetylase activity.
{ECO:0000269|PubMed:14701748}.
MUTAGEN 39 39 S->E: Decreases the deacetylase activity.
{ECO:0000269|PubMed:14701748}.
MUTAGEN 101 101 D->A: Complete loss of catalytical
activity. Complete loss of catalytical
activity; when associated with F-306.
{ECO:0000269|PubMed:17721440,
ECO:0000269|PubMed:19053282}.
MUTAGEN 101 101 D->E: Partial loss of catalytical
activity. {ECO:0000269|PubMed:17721440,
ECO:0000269|PubMed:19053282}.
MUTAGEN 101 101 D->L: Complete loss of catalytical
activity. {ECO:0000269|PubMed:17721440,
ECO:0000269|PubMed:19053282}.
MUTAGEN 101 101 D->N: Almost complete loss of catalytical
activity. {ECO:0000269|PubMed:17721440,
ECO:0000269|PubMed:19053282}.
MUTAGEN 142 143 HH->AA: Strongly reduces histone
deacetylase activity.
{ECO:0000269|PubMed:10926844}.
MUTAGEN 143 143 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:19053282}.
MUTAGEN 306 306 Y->F: Loss of catalytic activity.
Complete loss of catalytic activity; when
associated with A-101.
{ECO:0000269|PubMed:17721440}.
CONFLICT 31 31 L -> P (in Ref. 9; AAH50433).
{ECO:0000305}.
CONFLICT 179 179 L -> V (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 223 223 R -> W (in Ref. 2; AAF73428).
{ECO:0000305}.
STRAND 17 19 {ECO:0000244|PDB:5DC8}.
HELIX 22 28 {ECO:0000244|PDB:5DC8}.
TURN 29 31 {ECO:0000244|PDB:4RN0}.
STRAND 32 34 {ECO:0000244|PDB:3EZP}.
HELIX 37 47 {ECO:0000244|PDB:5DC8}.
HELIX 50 53 {ECO:0000244|PDB:5DC8}.
STRAND 54 57 {ECO:0000244|PDB:5DC8}.
HELIX 64 67 {ECO:0000244|PDB:5DC8}.
TURN 68 70 {ECO:0000244|PDB:5DC8}.
HELIX 73 83 {ECO:0000244|PDB:5DC8}.
TURN 84 86 {ECO:0000244|PDB:5DC8}.
STRAND 87 89 {ECO:0000244|PDB:3F0R}.
TURN 91 97 {ECO:0000244|PDB:5DC8}.
STRAND 99 102 {ECO:0000244|PDB:5DC8}.
HELIX 108 127 {ECO:0000244|PDB:5DC8}.
STRAND 128 130 {ECO:0000244|PDB:1W22}.
STRAND 132 136 {ECO:0000244|PDB:5DC8}.
STRAND 153 155 {ECO:0000244|PDB:5DC8}.
HELIX 157 165 {ECO:0000244|PDB:5DC8}.
TURN 166 168 {ECO:0000244|PDB:5DC8}.
STRAND 172 176 {ECO:0000244|PDB:5DC8}.
STRAND 178 180 {ECO:0000244|PDB:5DC8}.
HELIX 183 188 {ECO:0000244|PDB:5DC8}.
TURN 189 191 {ECO:0000244|PDB:5DC8}.
STRAND 193 202 {ECO:0000244|PDB:5DC8}.
STRAND 207 209 {ECO:0000244|PDB:1VKG}.
HELIX 220 222 {ECO:0000244|PDB:5DC8}.
STRAND 225 231 {ECO:0000244|PDB:5DC8}.
HELIX 237 255 {ECO:0000244|PDB:5DC8}.
STRAND 258 263 {ECO:0000244|PDB:5DC8}.
HELIX 266 268 {ECO:0000244|PDB:5DC8}.
HELIX 281 292 {ECO:0000244|PDB:5DC8}.
STRAND 297 301 {ECO:0000244|PDB:5DC8}.
HELIX 308 323 {ECO:0000244|PDB:5DC8}.
HELIX 337 340 {ECO:0000244|PDB:5DC8}.
TURN 341 343 {ECO:0000244|PDB:5DC8}.
HELIX 359 373 {ECO:0000244|PDB:5DC8}.
TURN 374 376 {ECO:0000244|PDB:5D1C}.
SEQUENCE 377 AA; 41758 MW; CAA1B91894FB5013 CRC64;
MEEPEEPADS GQSLVPVYIY SPEYVSMCDS LAKIPKRASM VHSLIEAYAL HKQMRIVKPK
VASMEEMATF HTDAYLQHLQ KVSQEGDDDH PDSIEYGLGY DCPATEGIFD YAAAIGGATI
TAAQCLIDGM CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFE RILYVDLDLH
HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDGIQDEKY
YQICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWQLATLI
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH
RIQQILNYIK GNLKHVV


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Genprice Inc, Invoices and accounting
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