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Protein SET (HLA-DR-associated protein II) (Inhibitor of granzyme A-activated DNase) (IGAAD) (PHAPII) (Phosphatase 2A inhibitor I2PP2A) (I-2PP2A) (Template-activating factor I) (TAF-I)

 SET_HUMAN               Reviewed;         290 AA.
Q01105; A5A5H4; A6NGV1; B4DUE2; Q15541; Q5VXV1; Q5VXV2; Q6FHZ5;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 3.
12-SEP-2018, entry version 194.
RecName: Full=Protein SET;
AltName: Full=HLA-DR-associated protein II;
AltName: Full=Inhibitor of granzyme A-activated DNase;
Short=IGAAD;
AltName: Full=PHAPII;
AltName: Full=Phosphatase 2A inhibitor I2PP2A;
Short=I-2PP2A;
AltName: Full=Template-activating factor I;
Short=TAF-I;
Name=SET;
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 2).
PubMed=1630450;
von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A.,
Grosveld G.;
"Can, a putative oncogene associated with myeloid leukemogenesis, may
be activated by fusion of its 3' half to different genes:
characterization of the set gene.";
Mol. Cell. Biol. 12:3346-3355(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
PubMed=8192856; DOI=10.1515/bchm3.1994.375.2.113;
Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T.,
Zimmermann B., Kratzin H.D., Hilschmann N.;
"Purification and characterization of two putative HLA class II
associated proteins: PHAPI and PHAPII.";
Biol. Chem. Hoppe-Seyler 375:113-126(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
14-35; 40-60; 75-90 AND 155-167, AND ACTIVATION OF DNA REPLICATION.
TISSUE=Cervix carcinoma;
PubMed=7753797; DOI=10.1073/pnas.92.10.4279;
Nagata K., Kawase H., Handa H., Yano K., Yamasaki M., Ishimi Y.,
Okuda A., Kikuchi A., Matsumoto K.;
"Replication factor encoded by a putative oncogene, set, associated
with myeloid leukemogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 92:4279-4283(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=8626647; DOI=10.1074/jbc.271.19.11059;
Li M., Makkinje A., Damuni Z.;
"The myeloid leukemia-associated protein SET is a potent inhibitor of
protein phosphatase 2A.";
J. Biol. Chem. 271:11059-11062(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=15642345; DOI=10.1016/j.febslet.2004.11.097;
Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.;
"Inhibitors of protein phosphatase-2A from human brain structures,
immunocytological localization and activities towards
dephosphorylation of the Alzheimer type hyperphosphorylated tau.";
FEBS Lett. 579:363-372(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[11]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
PubMed=8294483;
Adachi Y., Pavlaki G.N., Copeland T.D.;
"Identification and characterization of SET, a nuclear phosphoprotein
encoded by the translocation break point in acute undifferentiated
leukemia.";
J. Biol. Chem. 269:2258-2262(1994).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-241 (ISOFORM 2).
Wang L.C., Chen Y.;
"A relative factor in human rectum carcinoma.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[13]
EXPRESSION IN THE KIDNEY.
PubMed=9773788;
Carlson S.G., Eng E., Kim E.-G., Perlman E.J., Copeland T.D.,
Ballermann B.J.;
"Expression of SET, an inhibitor of protein phosphatase 2A, in renal
development and Wilms' tumor.";
J. Am. Soc. Nephrol. 9:1873-1880(1998).
[14]
INHIBITION OF HISTONE ACETYLATION.
PubMed=11163245; DOI=10.1016/S0092-8674(01)00196-9;
Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.;
"Regulation of histone acetylation and transcription by INHAT, a human
cellular complex containing the Set oncoprotein.";
Cell 104:119-130(2001).
[15]
INTERACTION WITH SETBP1.
TISSUE=Cervix carcinoma;
PubMed=11231286; DOI=10.1046/j.1432-1327.2001.02000.x;
Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D.,
Ueda K., Adachi Y.;
"Identification and characterization of SEB, a novel protein that
binds to the acute undifferentiated leukemia-associated protein SET.";
Eur. J. Biochem. 268:1340-1351(2001).
[16]
FUNCTION, INTERACTION WITH AN32A, PROTEOLYTIC CLEAVAGE AT LYS-179 BY
GZMA (ISOFORM 2), AND SUBCELLULAR LOCATION.
PubMed=11555662; DOI=10.1074/jbc.M108137200;
Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L.,
Jaju M., Lieberman J.;
"Granzyme A activates an endoplasmic reticulum-associated caspase-
independent nuclease to induce single-stranded DNA nicks.";
J. Biol. Chem. 276:43285-43293(2001).
[17]
INTERACTION WITH HMGB2, AND IDENTIFICATION IN THE SET COMPLEX.
PubMed=11909973; DOI=10.1128/MCB.22.8.2810-2820.2002;
Fan Z., Beresford P.J., Zhang D., Lieberman J.;
"HMG2 interacts with the nucleosome assembly protein SET and is a
target of the cytotoxic T-lymphocyte protease granzyme A.";
Mol. Cell. Biol. 22:2810-2820(2002).
[18]
FUNCTION IN NME1 INHIBITION, INTERACTION WITH NME1, SUBCELLULAR
LOCATION, DESCRIPTION OF THE SET COMPLEX, AND PROTEOLYTIC CLEAVAGE BY
GZMA.
PubMed=12628186; DOI=10.1016/S0092-8674(03)00150-8;
Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.;
"Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-
mediated apoptosis, and the nucleosome assembly protein SET is its
inhibitor.";
Cell 112:659-672(2003).
[19]
ERRATUM.
Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.;
Cell 115:241-241(2003).
[20]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 VP22 (MICROBIAL INFECTION).
PubMed=12917472; DOI=10.1099/vir.0.19326-0;
van Leeuwen H., Okuwaki M., Hong R., Chakravarti D., Nagata K.,
O'Hare P.;
"Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-
I proteins and inhibits nucleosome assembly but not regulation of
histone acetylation by INHAT.";
J. Gen. Virol. 84:2501-2510(2003).
[21]
SUBCELLULAR LOCATION.
PubMed=12524539; DOI=10.1038/ni885;
Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A.,
Pommier Y., Lieberman J.;
"Cleaving the oxidative repair protein Ape1 enhances cell death
mediated by granzyme A.";
Nat. Immunol. 4:145-153(2003).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[23]
INTERACTION WITH TREX1, IDENTIFICATION IN THE SET COMPLEX, PROTEOLYTIC
CLEAVAGE BY GZMA, AND SUBCELLULAR LOCATION.
PubMed=16818237; DOI=10.1016/j.molcel.2006.06.005;
Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B.,
Perrino F.W., Lieberman J.;
"The exonuclease TREX1 is in the SET complex and acts in concert with
NM23-H1 to degrade DNA during granzyme A-mediated cell death.";
Mol. Cell 23:133-142(2006).
[24]
INTERACTION WITH SGO1.
PubMed=16541025; DOI=10.1038/nature04663;
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
Kawashima S.A., Watanabe Y.;
"Shugoshin collaborates with protein phosphatase 2A to protect
cohesin.";
Nature 441:46-52(2006).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[26]
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).
[27]
INTERACTION WITH APBB1.
PubMed=19343227; DOI=10.1371/journal.pone.0005071;
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
"FE65 binds Teashirt, inhibiting expression of the primate-specific
caspase-4.";
PLoS ONE 4:E5071-E5071(2009).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150 AND LYS-172, ACETYLATION
[LARGE SCALE ANALYSIS] AT LYS-11 (ISOFORM 2), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM 2), 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).
[30]
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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM
2), 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).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-63, 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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, 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).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[35]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-238, DNA-BINDING, DOMAINS,
AND SUBUNIT.
PubMed=17360516; DOI=10.1073/pnas.0603762104;
Muto S., Senda M., Akai Y., Sato L., Suzuki T., Nagai R., Senda T.,
Horikoshi M.;
"Relationship between the structure of SET/TAF-Ibeta/INHAT and its
histone chaperone activity.";
Proc. Natl. Acad. Sci. U.S.A. 104:4285-4290(2007).
[36]
VARIANT 233-TYR--ASP-290 DEL.
PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C.,
Patry L., Massicotte C., Ambalavanan A., Spiegelman D., Diallo O.,
Henrion E., Dionne-Laporte A., Fougerat A., Pshezhetsky A.V.,
Venkateswaran S., Rouleau G.A., Michaud J.L.;
"De novo mutations in moderate or severe intellectual disability.";
PLoS Genet. 10:E1004772-E1004772(2014).
-!- FUNCTION: Multitasking protein, involved in apoptosis,
transcription, nucleosome assembly and histone chaperoning.
Isoform 2 anti-apoptotic activity is mediated by inhibition of the
GZMA-activated DNase, NME1. In the course of cytotoxic T-
lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting
its binding to NME1 and releasing NME1 inhibition. Isoform 1 and
isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform
1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation
of histones (HAT) and nucleosomes, most probably by masking the
accessibility of lysines of histones to the acetylases. The
predominant target for inhibition is histone H4. HAT inhibition
leads to silencing of HAT-dependent transcription and prevents
active demethylation of DNA. Both isoforms stimulate DNA
replication of the adenovirus genome complexed with viral core
proteins; however, isoform 2 specific activity is higher.
{ECO:0000269|PubMed:11555662, ECO:0000269|PubMed:12628186}.
-!- SUBUNIT: Headphone-shaped homodimer. Isoforms 1 and 2 interact
directly with each other and with ANP32A within the tripartite
INHAT (inhibitor of acetyltransferases) complex. Isoform 1 and
isoform 2 interact also with histones. Isoform 2 is a component of
the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1,
SET and TREX1, but not NME2 or TREX2. Within this complex,
directly interacts with ANP32A, NME1, HMGB2 and TREX1; the
interaction with ANP32A is enhanced after cleavage. Interacts with
APBB1, CHTOP, SETBP1, SGO1. {ECO:0000269|PubMed:11231286,
ECO:0000269|PubMed:11555662, ECO:0000269|PubMed:11909973,
ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16541025,
ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:17360516,
ECO:0000269|PubMed:19343227}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
1 VP22. {ECO:0000269|PubMed:12917472}.
-!- INTERACTION:
Q6SJ93:FAM111B; NbExp=3; IntAct=EBI-1053182, EBI-6309082;
Q12778:FOXO1; NbExp=5; IntAct=EBI-1053182, EBI-1108782;
Q00987:MDM2; NbExp=2; IntAct=EBI-1053182, EBI-389668;
P50222:MEOX2; NbExp=3; IntAct=EBI-1053182, EBI-748397;
P10644:PRKAR1A; NbExp=2; IntAct=EBI-1053182, EBI-476431;
P63000:RAC1; NbExp=8; IntAct=EBI-1053182, EBI-413628;
O00560:SDCBP; NbExp=3; IntAct=EBI-1053182, EBI-727004;
Q15573:TAF1A; NbExp=2; IntAct=EBI-1053182, EBI-2510647;
Q53T94:TAF1B; NbExp=3; IntAct=EBI-1053182, EBI-1560239;
Q15572:TAF1C; NbExp=4; IntAct=EBI-1053182, EBI-2510659;
P20226:TBP; NbExp=4; IntAct=EBI-1053182, EBI-355371;
Q9BT49:THAP7; NbExp=6; IntAct=EBI-1053182, EBI-741350;
P17480:UBTF; NbExp=4; IntAct=EBI-1053182, EBI-396235;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum.
Nucleus, nucleoplasm. Note=In the cytoplasm, found both in the
cytosol and associated with the endoplasmic reticulum. The SET
complex is associated with the endoplasmic reticulum. Following
CTL attack and cleavage by GZMA, moves rapidly to the nucleus,
where it is found in the nucleoplasm, avoiding the nucleolus.
Similar translocation to the nucleus is also observed for
lymphocyte-activated killer cells after the addition of calcium.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=TAF-I alpha;
IsoId=Q01105-1; Sequence=Displayed;
Name=2; Synonyms=TAF-I beta;
IsoId=Q01105-2; Sequence=VSP_009868;
Note=Variant in position: 4:P->Q (in dbSNP:rs1141138). Contains
a N6-acetyllysine at position 11. Contains a phosphoserine at
position 15. Contains a phosphoserine at position 24.
{ECO:0000244|PubMed:19608861, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692};
Name=3;
IsoId=Q01105-3; Sequence=VSP_045175;
Name=4;
IsoId=Q01105-4; Sequence=VSP_046741;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Widely expressed. Low levels in quiescent
cells during serum starvation, contact inhibition or
differentiation. Highly expressed in Wilms' tumor.
-!- DOMAIN: A long alpha helix in the N-terminus mediates
dimerization, while the earmuff domain is responsible for core
histone and dsDNA binding. The C-terminal acidic domain mediates
the inhibition of histone acetyltransferases and is required for
the DNA replication stimulatory activity.
{ECO:0000269|PubMed:17360516}.
-!- PTM: Isoform 2 is phosphorylated on Ser-15 and Ser-24.
-!- PTM: Isoform 2 is acetylated on Lys-11.
-!- PTM: Some glutamate residues are glycylated by TTLL8. This
modification occurs exclusively on glutamate residues and results
in a glycine chain on the gamma-carboxyl group (By similarity).
{ECO:0000250}.
-!- PTM: N-terminus of isoform 1 is methylated by METTL11A/NTM1.
Mainly trimethylated (By similarity). {ECO:0000250}.
-!- PTM: Isoform 2: Cleaved after Lys-176 by GZMA. The cleavage
inhibits its nucleosome assembly activity and disrupts the
inhibition on NME1. {ECO:0000269|PubMed:11555662,
ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237}.
-!- DISEASE: Note=A chromosomal aberration involving SET is found in
some cases of acute undifferentiated leukemia (AUL). Translocation
t(6;9)(q21;q34.1) with NUP214/CAN.
-!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP)
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SETID42272ch9q34.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M93651; AAA60318.1; -; mRNA.
EMBL; X75091; CAA52982.1; -; mRNA.
EMBL; D45198; BAA08139.1; -; mRNA.
EMBL; U51924; AAC50460.1; -; mRNA.
EMBL; AY349172; AAQ79833.1; -; mRNA.
EMBL; CR536543; CAG38780.1; -; mRNA.
EMBL; CR542050; CAG46847.1; -; mRNA.
EMBL; AK223556; BAD97276.1; -; mRNA.
EMBL; AK300609; BAG62304.1; -; mRNA.
EMBL; AL356481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032749; AAH32749.1; -; mRNA.
EMBL; EF534308; ABP96841.1; -; mRNA.
CCDS; CCDS48037.1; -. [Q01105-1]
CCDS; CCDS59149.1; -. [Q01105-4]
CCDS; CCDS6907.1; -. [Q01105-2]
PIR; A57984; A45018.
PIR; I59377; I59377.
RefSeq; NP_001116293.1; NM_001122821.1. [Q01105-1]
RefSeq; NP_001234929.1; NM_001248000.1. [Q01105-4]
RefSeq; NP_001234930.1; NM_001248001.1.
RefSeq; NP_003002.2; NM_003011.3. [Q01105-2]
UniGene; Hs.436687; -.
PDB; 2E50; X-ray; 2.30 A; A/B/P/Q=38-238.
PDBsum; 2E50; -.
ProteinModelPortal; Q01105; -.
SMR; Q01105; -.
BioGrid; 112316; 130.
CORUM; Q01105; -.
DIP; DIP-33561N; -.
IntAct; Q01105; 107.
MINT; Q01105; -.
STRING; 9606.ENSP00000361777; -.
iPTMnet; Q01105; -.
PhosphoSitePlus; Q01105; -.
SwissPalm; Q01105; -.
BioMuta; SET; -.
DMDM; 46397790; -.
EPD; Q01105; -.
PaxDb; Q01105; -.
PeptideAtlas; Q01105; -.
PRIDE; Q01105; -.
ProteomicsDB; 57917; -.
ProteomicsDB; 57918; -. [Q01105-2]
TopDownProteomics; Q01105-1; -. [Q01105-1]
TopDownProteomics; Q01105-2; -. [Q01105-2]
DNASU; 6418; -.
Ensembl; ENST00000322030; ENSP00000318012; ENSG00000119335. [Q01105-2]
Ensembl; ENST00000372686; ENSP00000361771; ENSG00000119335. [Q01105-3]
Ensembl; ENST00000372692; ENSP00000361777; ENSG00000119335. [Q01105-1]
Ensembl; ENST00000409104; ENSP00000387321; ENSG00000119335. [Q01105-4]
GeneID; 6418; -.
KEGG; hsa:6418; -.
UCSC; uc004bvu.5; human. [Q01105-1]
CTD; 6418; -.
DisGeNET; 6418; -.
EuPathDB; HostDB:ENSG00000119335.16; -.
GeneCards; SET; -.
HGNC; HGNC:10760; SET.
HPA; CAB005232; -.
HPA; HPA063683; -.
MIM; 600960; gene.
neXtProt; NX_Q01105; -.
OpenTargets; ENSG00000119335; -.
PharmGKB; PA35678; -.
eggNOG; KOG1508; Eukaryota.
eggNOG; ENOG410XQRX; LUCA.
GeneTree; ENSGT00530000062882; -.
HOGENOM; HOG000232096; -.
HOVERGEN; HBG014779; -.
InParanoid; Q01105; -.
KO; K11290; -.
OMA; PVALMNH; -.
OrthoDB; EOG091G00YT; -.
PhylomeDB; Q01105; -.
TreeFam; TF313386; -.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
SIGNOR; Q01105; -.
ChiTaRS; SET; human.
EvolutionaryTrace; Q01105; -.
GeneWiki; Protein_SET; -.
GenomeRNAi; 6418; -.
PRO; PR:Q01105; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000119335; Expressed in 234 organ(s), highest expression level in substantia nigra.
CleanEx; HS_SET; -.
ExpressionAtlas; Q01105; baseline and differential.
Genevisible; Q01105; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005811; C:lipid droplet; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042393; F:histone binding; TAS:UniProtKB.
GO; GO:0004864; F:protein phosphatase inhibitor activity; TAS:ProtInc.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:ProtInc.
GO; GO:0035067; P:negative regulation of histone acetylation; TAS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; TAS:ProtInc.
GO; GO:0006337; P:nucleosome disassembly; TAS:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR037231; NAP-like_sf.
InterPro; IPR002164; NAP_family.
PANTHER; PTHR11875; PTHR11875; 1.
Pfam; PF00956; NAP; 1.
SUPFAM; SSF143113; SSF143113; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chaperone;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; DNA-binding;
Endoplasmic reticulum; Host-virus interaction; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9EQU5}.
CHAIN 2 290 Protein SET.
/FTId=PRO_0000185662.
REGION 31 78 Dimerization.
REGION 79 225 Earmuff domain.
COMPBIAS 239 290 Asp/Glu-rich (highly acidic).
SITE 283 284 Breakpoint for translocation to form SET-
CAN oncogene.
MOD_RES 2 2 N,N,N-trimethylalanine.
{ECO:0000250|UniProtKB:Q9EQU5}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 68 68 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9EQU5}.
MOD_RES 146 146 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9EQU5}.
MOD_RES 150 150 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 1 37 MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG ->
MSAPAAKVSKKELNSNHDGADETS (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15642345,
ECO:0000303|PubMed:1630450,
ECO:0000303|PubMed:7753797,
ECO:0000303|PubMed:8192856,
ECO:0000303|PubMed:8626647,
ECO:0000303|Ref.12, ECO:0000303|Ref.6,
ECO:0000303|Ref.7}.
/FTId=VSP_009868.
VAR_SEQ 1 37 MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG ->
MPRSHQPPPPPH (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045175.
VAR_SEQ 1 37 MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG ->
MGCRDLLPSLKPTLL (in isoform 4).
{ECO:0000305}.
/FTId=VSP_046741.
VARIANT 233 290 Missing (probable disease-associated
mutation found in a patient with
congenital microcephaly and moderate
intellecutal disability).
{ECO:0000269|PubMed:25356899}.
/FTId=VAR_078653.
HELIX 37 88 {ECO:0000244|PDB:2E50}.
HELIX 94 100 {ECO:0000244|PDB:2E50}.
HELIX 103 106 {ECO:0000244|PDB:2E50}.
HELIX 111 116 {ECO:0000244|PDB:2E50}.
HELIX 117 119 {ECO:0000244|PDB:2E50}.
STRAND 120 127 {ECO:0000244|PDB:2E50}.
STRAND 135 141 {ECO:0000244|PDB:2E50}.
STRAND 145 148 {ECO:0000244|PDB:2E50}.
STRAND 150 156 {ECO:0000244|PDB:2E50}.
STRAND 166 168 {ECO:0000244|PDB:2E50}.
HELIX 203 206 {ECO:0000244|PDB:2E50}.
HELIX 215 223 {ECO:0000244|PDB:2E50}.
TURN 224 227 {ECO:0000244|PDB:2E50}.
HELIX 230 233 {ECO:0000244|PDB:2E50}.
SEQUENCE 290 AA; 33489 MW; F4664118171EF230 CRC64;
MAPKRQSPLP PQKKKPRPPP ALGPEETSAS AGLPKKGEKE QQEAIEHIDE VQNEIDRLNE
QASEEILKVE QKYNKLRQPF FQKRSELIAK IPNFWVTTFV NHPQVSALLG EEDEEALHYL
TRVEVTEFED IKSGYRIDFY FDENPYFENK VLSKEFHLNE SGDPSSKSTE IKWKSGKDLT
KRSSQTQNKA SRKRQHEEPE SFFTWFTDHS DAGADELGEV IKDDIWPNPL QYYLVPDMDD
EEGEGEEDDD DDEEEEGLED IDEEGDEDEG EEDEDDDEGE EGEEDEGEDD


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