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Histone deacetylase 7 (HD7) (EC 3.5.1.98) (Histone deacetylase 7A) (HD7a)

 HDAC7_HUMAN             Reviewed;         952 AA.
Q8WUI4; B3KY08; B4DWI0; B4E0Q5; Q6P1W9; Q6W9G7; Q7Z4K2; Q7Z5I1;
Q96K01; Q9BR73; Q9H7L0; Q9NW41; Q9NWA9; Q9NYK9; Q9UFU7;
16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
16-MAY-2003, sequence version 2.
25-OCT-2017, entry version 173.
RecName: Full=Histone deacetylase 7;
Short=HD7;
EC=3.5.1.98;
AltName: Full=Histone deacetylase 7A;
Short=HD7a;
Name=HDAC7; Synonyms=HDAC7A;
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).
TISSUE=Cervix carcinoma;
Li S., Fischle W., Verdin E., Walsh M.J.;
"A novel class II HDAC is associated with the transcriptional
homeodomain repressor CCAAT displacement protein.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
5).
Petrie K., Zelent A.;
"Genomic organization of the human histone deacetylase 7 gene.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Zhi Y., Su E.W.;
"Homo sapiens histone deacetylase 7A (HDAC7A), transcript variant 3.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5; 6; 8 AND 9),
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-952 (ISOFORM 3), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 651-952.
TISSUE=Embryo, Mammary gland, Placenta, Spleen, Teratocarcinoma, and
Thymus;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 242-952 (ISOFORM 1).
TISSUE=B-cell, Colon, and PNS;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-952 (ISOFORM 1).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH EDNRA.
PubMed=11262386; DOI=10.1074/jbc.C000909200;
Lee H.-J., Chun M., Kandror K.V.;
"Tip60 and HDAC7 interact with the endothelin receptor a and may be
involved in downstream signaling.";
J. Biol. Chem. 276:16597-16600(2001).
[11]
INTERACTION WITH HDAC3.
PubMed=11466315; DOI=10.1074/jbc.M104935200;
Fischle W., Dequiedt F., Fillion M., Hendzel M.J., Voelter W.,
Verdin E.;
"Human HDAC7 histone deacetylase activity is associated with HDAC3 in
vivo.";
J. Biol. Chem. 276:35826-35835(2001).
[12]
FUNCTION.
PubMed=12239305; DOI=10.1128/JVI.76.20.10290-10298.2002;
Bryant H., Farrell P.J.;
"Signal transduction and transcription factor modification during
reactivation of Epstein-Barr virus from latency.";
J. Virol. 76:10290-10298(2002).
[13]
INTERACTION WITH KAT5.
PubMed=12551922; DOI=10.1074/jbc.M210816200;
Xiao H., Chung J., Kao H.-Y., Yang Y.-C.;
"Tip60 is a co-repressor for STAT3.";
J. Biol. Chem. 278:11197-11204(2003).
[14]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-155 AND SER-181, AND
MUTAGENESIS OF LEU-150; SER-155; SER-181; SER-358 AND SER-486.
PubMed=16980613; DOI=10.1128/MCB.00231-06;
Dequiedt F., Martin M., Von Blume J., Vertommen D., Lecomte E.,
Mari N., Heinen M.F., Bachmann M., Twizere J.C., Huang M.C.,
Rider M.H., Piwnica-Worms H., Seufferlein T., Kettmann R.;
"New role for hPar-1 kinases EMK and C-TAK1 in regulating localization
and activity of class IIa histone deacetylases.";
Mol. Cell. Biol. 26:7086-7102(2006).
[15]
PHOSPHORYLATION AT SER-181.
PubMed=17962809; DOI=10.1038/sj.emboj.7601891;
von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A.,
Auer A., Van Lint J., Adler G., Seufferlein T.;
"Phosphorylation at Ser244 by CK1 determines nuclear localization and
substrate targeting of PKD2.";
EMBO J. 26:4619-4633(2007).
[16]
INTERACTION WITH KDM5B.
PubMed=17373667; DOI=10.1002/ijc.22673;
Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K.,
Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E.,
Freemont P., Taylor-Papadimitriou J.;
"Breast cancer associated transcriptional repressor PLU-1/JARID1B
interacts directly with histone deacetylases.";
Int. J. Cancer 121:265-275(2007).
[17]
FUNCTION, AND INTERACTION WITH FOXP3.
PubMed=17360565; DOI=10.1073/pnas.0700298104;
Li B., Samanta A., Song X., Iacono K.T., Bembas K., Tao R., Basu S.,
Riley J.L., Hancock W.W., Shen Y., Saouaf S.J., Greene M.I.;
"FOXP3 interactions with histone acetyltransferase and class II
histone deacetylases are required for repression.";
Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-283; THR-286
AND SER-486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
PHOSPHORYLATION.
PubMed=20188095; DOI=10.1016/j.febslet.2010.02.057;
Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,
McKinsey T.A.;
"Protein kinase C-related kinase targets nuclear localization signals
in a subset of class IIa histone deacetylases.";
FEBS Lett. 584:1103-1110(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-283 AND
THR-286, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-486, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
INTERACTION WITH PML.
PubMed=22155184; DOI=10.1053/j.gastro.2011.11.041;
Satow R., Shitashige M., Jigami T., Fukami K., Honda K.,
Kitabayashi I., Yamada T.;
"Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor
function in colorectal cancer cells.";
Gastroenterology 142:572-581(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-181; SER-405;
SER-486; SER-487; SER-507 AND SER-595, 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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-486, 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).
[27]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 482-903, ZINC-BINDING SITES,
AND MUTAGENESIS OF HIS-843.
PubMed=18285338; DOI=10.1074/jbc.M707362200;
Schuetz A., Min J., Allali-Hassani A., Schapira M., Shuen M.,
Loppnau P., Mazitschek R., Kwiatkowski N.P., Lewis T.A.,
Maglathin R.L., McLean T.H., Bochkarev A., Plotnikov A.N., Vedadi M.,
Arrowsmith C.H.;
"Human HDAC7 harbors a class IIa histone deacetylase-specific zinc
binding motif and cryptic deacetylase activity.";
J. Biol. Chem. 283:11355-11363(2008).
[28]
VARIANT [LARGE SCALE ANALYSIS] MET-43.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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. Involved in muscle
maturation by repressing transcription of myocyte enhancer factors
such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it
shuttles into the cytoplasm, allowing the expression of myocyte
enhancer factors (By similarity). May be involved in Epstein-Barr
virus (EBV) latency, possibly by repressing the viral BZLF1 gene.
Positively regulates the transcriptional repressor activity of
FOXP3 (PubMed:17360565). {ECO:0000250|UniProtKB:Q8C2B3,
ECO:0000269|PubMed:12239305, ECO:0000269|PubMed:17360565}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1,
NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3.
Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C
(By similarity). Interacts with KAT5 and EDNRA. Interacts with
KDM5B. Interacts with ZMYND15 (By similarity). Interacts with PML
(isoform PML-4). Interacts with FOXP3.
{ECO:0000250|UniProtKB:Q8C2B3, ECO:0000269|PubMed:11262386,
ECO:0000269|PubMed:11466315, ECO:0000269|PubMed:12551922,
ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17373667,
ECO:0000269|PubMed:22155184}.
-!- INTERACTION:
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-10276431, EBI-739580;
P00533:EGFR; NbExp=2; IntAct=EBI-1048378, EBI-297353;
Q9BZS1-1:FOXP3; NbExp=2; IntAct=EBI-1048378, EBI-9695448;
Q9BZS1-2:FOXP3; NbExp=2; IntAct=EBI-1048378, EBI-16338471;
P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-1048378, EBI-6148881;
Q8CFN5:Mef2c (xeno); NbExp=2; IntAct=EBI-1048378, EBI-643797;
Q9BQI9:NRIP2; NbExp=4; IntAct=EBI-12094670, EBI-3913975;
Q9BZL6:PRKD2; NbExp=6; IntAct=EBI-1048378, EBI-1384325;
Q04864:REL; NbExp=3; IntAct=EBI-10276431, EBI-307352;
Q0D2K3:RIPPLY1; NbExp=4; IntAct=EBI-12094670, EBI-10226430;
P31947:SFN; NbExp=3; IntAct=EBI-1048378, EBI-476295;
P63104:YWHAZ; NbExp=3; IntAct=EBI-1048378, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In the nucleus, it
associates with distinct subnuclear dot-like structures. Shuttles
between the nucleus and the cytoplasm. Treatment with EDN1 results
in shuttling from the nucleus to the perinuclear region. The
export to cytoplasm depends on the interaction with the 14-3-3
protein YWHAE and is due to its phosphorylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Name=1;
IsoId=Q8WUI4-1; Sequence=Displayed;
Name=2;
IsoId=Q8WUI4-2; Sequence=VSP_007429, VSP_007431;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8WUI4-3; Sequence=VSP_008772;
Name=4;
IsoId=Q8WUI4-4; Sequence=VSP_007430;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q8WUI4-5; Sequence=VSP_038104;
Name=6;
IsoId=Q8WUI4-6; Sequence=VSP_038105;
Name=7;
IsoId=Q8WUI4-7; Sequence=VSP_038104, VSP_008772;
Name=8;
IsoId=Q8WUI4-8; Sequence=VSP_038106, VSP_038107;
Name=9;
IsoId=Q8WUI4-9; Sequence=VSP_038102;
Name=10;
IsoId=Q8WUI4-10; Sequence=VSP_038103;
-!- DOMAIN: The nuclear export sequence mediates the shuttling between
the nucleus and the cytoplasm. {ECO:0000250}.
-!- PTM: May be phosphorylated by CaMK1. Phosphorylated by the PKC
kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation
at Ser-155 by MARK2, MARK3 and PRKD1 promotes interaction with 14-
3-3 proteins and export from the nucleus. Phosphorylation at Ser-
155 is a prerequisite for phosphorylation at Ser-181.
{ECO:0000269|PubMed:16980613, ECO:0000269|PubMed:17962809,
ECO:0000269|PubMed:20188095}.
-!- MISCELLANEOUS: Its activity is inhibited by Trichostatin A (TSA),
a known histone deacetylase inhibitor. {ECO:0000250}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF63491.1; Type=Frameshift; Positions=877; Evidence={ECO:0000305};
Sequence=BAA91474.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA91545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB15759.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB55363.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC56929.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF239243; AAF63491.1; ALT_FRAME; mRNA.
EMBL; AY302468; AAQ18232.1; -; mRNA.
EMBL; AY321367; AAP84704.1; -; mRNA.
EMBL; BT009771; AAP88773.1; -; mRNA.
EMBL; AK001032; BAA91474.1; ALT_INIT; mRNA.
EMBL; AK001190; BAA91545.1; ALT_INIT; mRNA.
EMBL; AK024469; BAB15759.1; ALT_INIT; mRNA.
EMBL; AK027781; BAB55363.1; ALT_INIT; mRNA.
EMBL; AK122588; BAC56929.1; ALT_SEQ; mRNA.
EMBL; AK128383; BAG54670.1; -; mRNA.
EMBL; AK299292; BAG61307.1; -; mRNA.
EMBL; AK301545; BAG63042.1; -; mRNA.
EMBL; AK303481; BAG64517.1; -; mRNA.
EMBL; AC004466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW57957.1; -; Genomic_DNA.
EMBL; BC006453; AAH06453.2; -; mRNA.
EMBL; BC020505; AAH20505.2; -; mRNA.
EMBL; BC064840; AAH64840.1; -; mRNA.
EMBL; AL117455; CAB55935.1; -; mRNA.
CCDS; CCDS41776.1; -. [Q8WUI4-7]
CCDS; CCDS81685.1; -. [Q8WUI4-6]
CCDS; CCDS8756.2; -. [Q8WUI4-5]
PIR; T17245; T17245.
RefSeq; NP_001091886.1; NM_001098416.3. [Q8WUI4-7]
RefSeq; NP_001295019.1; NM_001308090.1. [Q8WUI4-6]
RefSeq; NP_056216.2; NM_015401.4. [Q8WUI4-5]
RefSeq; XP_011536783.1; XM_011538481.1. [Q8WUI4-1]
RefSeq; XP_011536784.1; XM_011538482.1. [Q8WUI4-1]
UniGene; Hs.200063; -.
PDB; 3C0Y; X-ray; 2.10 A; A/B/C=482-903.
PDB; 3C0Z; X-ray; 2.10 A; A/B/C=482-903.
PDB; 3C10; X-ray; 2.00 A; A/B/C=482-903.
PDB; 3ZNR; X-ray; 2.40 A; A/B/C=482-903.
PDB; 3ZNS; X-ray; 2.45 A; A/B/C=482-903.
PDBsum; 3C0Y; -.
PDBsum; 3C0Z; -.
PDBsum; 3C10; -.
PDBsum; 3ZNR; -.
PDBsum; 3ZNS; -.
ProteinModelPortal; Q8WUI4; -.
SMR; Q8WUI4; -.
BioGrid; 119613; 94.
CORUM; Q8WUI4; -.
DIP; DIP-29860N; -.
IntAct; Q8WUI4; 37.
MINT; MINT-3089050; -.
STRING; 9606.ENSP00000080059; -.
BindingDB; Q8WUI4; -.
ChEMBL; CHEMBL2716; -.
DrugBank; DB05015; Belinostat.
DrugBank; DB06603; Panobinostat.
GuidetoPHARMACOLOGY; 2661; -.
iPTMnet; Q8WUI4; -.
PhosphoSitePlus; Q8WUI4; -.
BioMuta; HDAC7; -.
DMDM; 30913097; -.
EPD; Q8WUI4; -.
MaxQB; Q8WUI4; -.
PaxDb; Q8WUI4; -.
PeptideAtlas; Q8WUI4; -.
PRIDE; Q8WUI4; -.
DNASU; 51564; -.
Ensembl; ENST00000080059; ENSP00000080059; ENSG00000061273. [Q8WUI4-5]
Ensembl; ENST00000354334; ENSP00000351326; ENSG00000061273. [Q8WUI4-7]
Ensembl; ENST00000427332; ENSP00000404394; ENSG00000061273. [Q8WUI4-1]
Ensembl; ENST00000552960; ENSP00000448532; ENSG00000061273. [Q8WUI4-6]
GeneID; 51564; -.
KEGG; hsa:51564; -.
UCSC; uc001rqj.5; human. [Q8WUI4-1]
CTD; 51564; -.
DisGeNET; 51564; -.
EuPathDB; HostDB:ENSG00000061273.17; -.
GeneCards; HDAC7; -.
H-InvDB; HIX0129669; -.
HGNC; HGNC:14067; HDAC7.
HPA; HPA004775; -.
MIM; 606542; gene.
neXtProt; NX_Q8WUI4; -.
OpenTargets; ENSG00000061273; -.
PharmGKB; PA162390579; -.
eggNOG; KOG1343; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062809; -.
HOVERGEN; HBG057100; -.
InParanoid; Q8WUI4; -.
KO; K11408; -.
PhylomeDB; Q8WUI4; -.
TreeFam; TF106174; -.
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-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SIGNOR; Q8WUI4; -.
ChiTaRS; HDAC7; human.
EvolutionaryTrace; Q8WUI4; -.
GeneWiki; HDAC7; -.
GenomeRNAi; 51564; -.
PMAP-CutDB; Q8WUI4; -.
PRO; PR:Q8WUI4; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000061273; -.
CleanEx; HS_HDAC7; -.
ExpressionAtlas; Q8WUI4; baseline and differential.
Genevisible; Q8WUI4; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000118; C:histone deacetylase complex; IEA:InterPro.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
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:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0019789; F:SUMO transferase activity; TAS:Reactome.
GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
GO; GO:0007043; P:cell-cell junction assembly; IEA:Ensembl.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:BHF-UCL.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR017320; Histone_deAcase_II_euk.
InterPro; IPR023696; Ureohydrolase_domain.
PANTHER; PTHR10625; PTHR10625; 4.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037911; HDAC_II_euk; 1.
PRINTS; PR01270; HDASUPER.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Zinc.
CHAIN 1 952 Histone deacetylase 7.
/FTId=PRO_0000114705.
REGION 1 268 Transcription repression 1.
{ECO:0000250}.
REGION 1 98 Interaction with MEF2C. {ECO:0000250}.
REGION 49 149 Interaction with MEF2A. {ECO:0000250}.
REGION 218 546 Transcription repression 2.
{ECO:0000250}.
REGION 518 865 Histone deacetylase.
REGION 877 952 Interaction with SIN3A. {ECO:0000250}.
MOTIF 918 952 Nuclear export signal. {ECO:0000250}.
COMPBIAS 197 203 Poly-Ser.
COMPBIAS 368 373 Poly-Pro.
ACT_SITE 670 670 {ECO:0000250}.
METAL 533 533 Zinc.
METAL 535 535 Zinc.
METAL 541 541 Zinc.
METAL 618 618 Zinc.
SITE 843 843 Contributes to catalysis.
MOD_RES 109 109 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 155 155 Phosphoserine; by MARK2, MARK3 and
PKD/PRKD1. {ECO:0000305|PubMed:16980613}.
MOD_RES 181 181 Phosphoserine; by PKD/PRKD2.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16980613,
ECO:0000269|PubMed:17962809}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 286 286 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 358 358 Phosphoserine; by PKD/PRKD1.
{ECO:0000250|UniProtKB:Q8C2B3}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 487 487 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 595 595 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 527 Missing (in isoform 9).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038102.
VAR_SEQ 1 472 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_007429.
VAR_SEQ 1 338 Missing (in isoform 10).
{ECO:0000303|Ref.4}.
/FTId=VSP_038103.
VAR_SEQ 1 1 M -> MHSPGADGTQVSPGAHYCSPTGAGCPRPCADTPGPQ
PQPM (in isoform 5 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_038104.
VAR_SEQ 1 1 M -> MHSPGAGCPRPCADTPGPQPQPM (in isoform
6). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_038105.
VAR_SEQ 1 1 M -> MSDLRKRELGALFTSRGTGGVEWDGTQVSPGAHYCS
PTGAGCPRPCADTPGPQPQPM (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038106.
VAR_SEQ 227 263 Missing (in isoform 3 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_008772.
VAR_SEQ 227 256 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_007430.
VAR_SEQ 473 520 LAQGGHRPLSRAQSSPAAPASLSAPEPASQARVLSSSETPA
RTLPFTT -> MQACVGVRGVYPPGSMWVPAVAVLACSLQP
RPWGVRTPWVPALTLAPA (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_007431.
VAR_SEQ 892 952 SKYWGCMQRLASCPDSWVPRVPGADKEEVEAVTALASLSVG
ILAEDRPSEQLVEEEEPMNL -> MGALTLSQIPGHGSSQQ
QAGGAFSRPGHPCRAAVVMVNTGAACSAWPPVQTPGCLECQ
GLTKKKWRQ (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038107.
VARIANT 43 43 V -> M (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036043.
MUTAGEN 150 150 L->A: Abolishes phosphorylation at S-155.
{ECO:0000269|PubMed:16980613}.
MUTAGEN 155 155 S->A: Abolishes nuclear export; when
associated with A-181; A-358 and A-486.
Abolishes phosphorylation by MARK2 and
MARK3, interaction with 14-3-3 and
localization to the cytoplasm.
{ECO:0000269|PubMed:16980613}.
MUTAGEN 181 181 S->A: Abolishes nuclear export; when
associated with A-155; A-358 and A-486.
{ECO:0000269|PubMed:16980613}.
MUTAGEN 358 358 S->A: Abolishes nuclear export; when
associated with A-192; A-1118 and A-486.
{ECO:0000269|PubMed:16980613}.
MUTAGEN 486 486 S->A: Abolishes nuclear export; when
associated with A-192; A-1118 and A-358.
{ECO:0000269|PubMed:16980613}.
MUTAGEN 843 843 H->A: Enhanced deacetylase activity.
{ECO:0000269|PubMed:18285338}.
MUTAGEN 843 843 H->F: Enhanced deacetylase activity.
{ECO:0000269|PubMed:18285338}.
MUTAGEN 843 843 H->Y: 6000 fold increase in deacetylase
activity. {ECO:0000269|PubMed:18285338}.
CONFLICT 50 50 M -> T (in Ref. 5; BAG64517).
{ECO:0000305}.
CONFLICT 225 264 Missing (in Ref. 1; AAF63491).
{ECO:0000305}.
CONFLICT 276 276 P -> L (in Ref. 5; BAA91545).
{ECO:0000305}.
CONFLICT 561 561 R -> L (in Ref. 5; BAA91545).
{ECO:0000305}.
CONFLICT 614 614 V -> E (in Ref. 1; AAF63491).
{ECO:0000305}.
CONFLICT 644 644 S -> R (in Ref. 5; BAB15759).
{ECO:0000305}.
CONFLICT 665 665 R -> W (in Ref. 5; BAA91474).
{ECO:0000305}.
CONFLICT 700 700 K -> KASK (in Ref. 1; AAF63491).
{ECO:0000305}.
CONFLICT 750 750 G -> S (in Ref. 5; BAA91545).
{ECO:0000305}.
CONFLICT 777 777 A -> T (in Ref. 5; BAB55363).
{ECO:0000305}.
CONFLICT 825 825 Q -> H (in Ref. 5; BAA91474).
{ECO:0000305}.
STRAND 520 523 {ECO:0000244|PDB:3C10}.
HELIX 526 530 {ECO:0000244|PDB:3C10}.
HELIX 538 540 {ECO:0000244|PDB:3C10}.
HELIX 546 557 {ECO:0000244|PDB:3C10}.
HELIX 561 563 {ECO:0000244|PDB:3C10}.
STRAND 564 567 {ECO:0000244|PDB:3C10}.
HELIX 574 577 {ECO:0000244|PDB:3C10}.
TURN 578 580 {ECO:0000244|PDB:3C10}.
HELIX 583 590 {ECO:0000244|PDB:3C10}.
HELIX 601 609 {ECO:0000244|PDB:3C10}.
STRAND 621 626 {ECO:0000244|PDB:3C10}.
TURN 631 633 {ECO:0000244|PDB:3C10}.
HELIX 634 653 {ECO:0000244|PDB:3C10}.
STRAND 656 662 {ECO:0000244|PDB:3C10}.
STRAND 680 682 {ECO:0000244|PDB:3C10}.
HELIX 684 695 {ECO:0000244|PDB:3C10}.
STRAND 701 705 {ECO:0000244|PDB:3C10}.
STRAND 707 709 {ECO:0000244|PDB:3C10}.
HELIX 712 718 {ECO:0000244|PDB:3C10}.
STRAND 724 731 {ECO:0000244|PDB:3C10}.
TURN 733 736 {ECO:0000244|PDB:3C10}.
HELIX 750 752 {ECO:0000244|PDB:3C10}.
STRAND 756 761 {ECO:0000244|PDB:3C10}.
STRAND 765 767 {ECO:0000244|PDB:3C10}.
HELIX 771 780 {ECO:0000244|PDB:3C10}.
HELIX 782 789 {ECO:0000244|PDB:3C10}.
STRAND 792 798 {ECO:0000244|PDB:3C10}.
HELIX 808 810 {ECO:0000244|PDB:3C10}.
HELIX 817 827 {ECO:0000244|PDB:3C10}.
HELIX 831 833 {ECO:0000244|PDB:3C10}.
STRAND 835 839 {ECO:0000244|PDB:3C10}.
HELIX 845 860 {ECO:0000244|PDB:3C10}.
HELIX 866 868 {ECO:0000244|PDB:3C10}.
HELIX 871 873 {ECO:0000244|PDB:3C10}.
HELIX 878 891 {ECO:0000244|PDB:3C10}.
TURN 892 894 {ECO:0000244|PDB:3C10}.
HELIX 896 898 {ECO:0000244|PDB:3C10}.
SEQUENCE 952 AA; 102927 MW; 786785B084667731 CRC64;
MDLRVGQRPP VEPPPEPTLL ALQRPQRLHH HLFLAGLQQQ RSVEPMRLSM DTPMPELQVG
PQEQELRQLL HKDKSKRSAV ASSVVKQKLA EVILKKQQAA LERTVHPNSP GIPYRTLEPL
ETEGATRSML SSFLPPVPSL PSDPPEHFPL RKTVSEPNLK LRYKPKKSLE RRKNPLLRKE
SAPPSLRRRP AETLGDSSPS SSSTPASGCS SPNDSEHGPN PILGSEALLG QRLRLQETSV
APFALPTVSL LPAITLGLPA PARADSDRRT HPTLGPRGPI LGSPHTPLFL PHGLEPEAGG
TLPSRLQPIL LLDPSGSHAP LLTVPGLGPL PFHFAQSLMT TERLSGSGLH WPLSRTRSEP
LPPSATAPPP PGPMQPRLEQ LKTHVQVIKR SAKPSEKPRL RQIPSAEDLE TDGGGPGQVV
DDGLEHRELG HGQPEARGPA PLQQHPQVLL WEQQRLAGRL PRGSTGDTVL LPLAQGGHRP
LSRAQSSPAA PASLSAPEPA SQARVLSSSE TPARTLPFTT GLIYDSVMLK HQCSCGDNSR
HPEHAGRIQS IWSRLQERGL RSQCECLRGR KASLEELQSV HSERHVLLYG TNPLSRLKLD
NGKLAGLLAQ RMFVMLPCGG VGVDTDTIWN ELHSSNAARW AAGSVTDLAF KVASRELKNG
FAVVRPPGHH ADHSTAMGFC FFNSVAIACR QLQQQSKASK ILIVDWDVHH GNGTQQTFYQ
DPSVLYISLH RHDDGNFFPG SGAVDEVGAG SGEGFNVNVA WAGGLDPPMG DPEYLAAFRI
VVMPIAREFS PDLVLVSAGF DAAEGHPAPL GGYHVSAKCF GYMTQQLMNL AGGAVVLALE
GGHDLTAICD ASEACVAALL GNRVDPLSEE GWKQKPNLNA IRSLEAVIRV HSKYWGCMQR
LASCPDSWVP RVPGADKEEV EAVTALASLS VGILAEDRPS EQLVEEEEPM NL


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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