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TNF receptor-associated factor 1 (Epstein-Barr virus-induced protein 6)

 TRAF1_HUMAN             Reviewed;         416 AA.
Q13077; B4DJ77; Q658U1; Q8NF13;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 173.
RecName: Full=TNF receptor-associated factor 1;
AltName: Full=Epstein-Barr virus-induced protein 6;
Name=TRAF1; Synonyms=EBI6;
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=Lymphoma;
PubMed=7859281; DOI=10.1016/0092-8674(95)90489-1;
Mosialos G., Birkenbach M., Yalamanchili R., VanArsdale T., Ware C.,
Kieff E.;
"The Epstein-Barr virus transforming protein LMP1 engages signaling
proteins for the tumor necrosis factor receptor family.";
Cell 80:389-399(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Spleen, and Substantia nigra;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Stomach;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH TRAF2 AND TNFRSF1B.
PubMed=8069916; DOI=10.1016/0092-8674(94)90532-0;
Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.;
"A novel family of putative signal transducers associated with the
cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.";
Cell 78:681-692(1994).
[9]
INTERACTION WITH TANK.
PubMed=8710854; DOI=10.1073/pnas.93.16.8241;
Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A.,
Goeddel D.V.;
"I-TRAF is a novel TRAF-interacting protein that regulates TRAF-
mediated signal transduction.";
Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996).
[10]
INTERACTION WITH TNFRSF8.
PubMed=8627180; DOI=10.1084/jem.183.2.669;
Lee S.Y., Park C.G., Choi Y.;
"T cell receptor-dependent cell death of T cell hybridomas mediated by
the CD30 cytoplasmic domain in association with tumor necrosis factor
receptor-associated factors.";
J. Exp. Med. 183:669-674(1996).
[11]
INTERACTION WITH TNFRSF5.
PubMed=9718306; DOI=10.1021/bi981067q;
Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J.,
Kehry M.R.;
"CD40-tumor necrosis factor receptor-associated factor (TRAF)
interactions: regulation of CD40 signaling through multiple TRAF
binding sites and TRAF hetero-oligomerization.";
Biochemistry 37:11836-11845(1998).
[12]
INTERACTION WITH RIPK2.
PubMed=9705938; DOI=10.1016/S0960-9822(07)00352-1;
Thome M., Hofmann K., Burns K., Martinon F., Bodmer J.-L.,
Mattmann C., Tschopp J.;
"Identification of CARDIAK, a RIP-like kinase that associates with
caspase-1.";
Curr. Biol. 8:885-888(1998).
[13]
INTERACTION WITH RIPK2.
PubMed=9642260; DOI=10.1074/jbc.273.27.16968;
McCarthy J.V., Ni J., Dixit V.M.;
"RIP2 is a novel NF-kappaB-activating and cell death-inducing
kinase.";
J. Biol. Chem. 273:16968-16975(1998).
[14]
INTERACTION WITH TNFRSF11A.
PubMed=9774460; DOI=10.1074/jbc.273.43.28355;
Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M.,
Choi Y.;
"The TRAF family of signal transducers mediates NF-kappaB activation
by the TRANCE receptor.";
J. Biol. Chem. 273:28355-28359(1998).
[15]
INTERACTION WITH TNFRSF9.
PubMed=9607925; DOI=10.1084/jem.187.11.1849;
Saoulli K., Lee S.Y., Cannons J.L., Yeh W.C., Santana A.,
Goldstein M.D., Bangia N., DeBenedette M.A., Mak T.W., Choi Y.,
Watts T.H.;
"CD28-independent, TRAF2-dependent costimulation of resting T cells by
4-1BB ligand.";
J. Exp. Med. 187:1849-1862(1998).
[16]
INTERACTION WITH TNFRSF4 AND TNFRSF9.
PubMed=9418902; DOI=10.1128/MCB.18.1.558;
Arch R.H., Thompson C.B.;
"4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve
growth factor receptor subfamily that bind TNF receptor-associated
factors and activate nuclear factor kappaB.";
Mol. Cell. Biol. 18:558-565(1998).
[17]
INTERACTION WITH TNFRSF18.
PubMed=10037686; DOI=10.1074/jbc.274.10.6056;
Kwon B., Yu K.-Y., Ni J., Yu G.-L., Jang I.-K., Kim Y.-J., Xing L.,
Liu D., Wang S.-X., Kwon B.S.;
"Identification of a novel activation-inducible protein of the tumor
necrosis factor receptor superfamily and its ligand.";
J. Biol. Chem. 274:6056-6061(1999).
[18]
FUNCTION, CLEAVAGE BY CASP8, MUTAGENESIS OF ASP-163, AND DOMAIN.
PubMed=10692572; DOI=10.1016/S0014-5793(00)01206-0;
Irmler M., Steiner V., Ruegg C., Wajant H., Tschopp J.;
"Caspase-induced inactivation of the anti-apoptotic TRAF1 during Fas
ligand-mediated apoptosis.";
FEBS Lett. 468:129-133(2000).
[19]
INTERACTION WITH TNFRSF19.
PubMed=10809768; DOI=10.1074/jbc.275.20.15336;
Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.;
"TAJ, a novel member of the tumor necrosis factor receptor family,
activates the c-Jun N-terminal kinase pathway and mediates caspase-
independent cell death.";
J. Biol. Chem. 275:15336-15342(2000).
[20]
INTERACTION WITH TNFRSF17.
PubMed=10903733; DOI=10.4049/jimmunol.165.3.1322;
Hatzoglou A., Roussel J., Bourgeade M.-F., Rogier E., Madry C.,
Inoue J., Devergne O., Tsapis A.;
"TNF receptor family member BCMA (B cell maturation) associates with
TNF receptor-associated factor (TRAF) 1, TRAF2, and TRAF3 and
activates NF-kappa B, elk-1, c-Jun N-terminal kinase, and p38 mitogen-
activated protein kinase.";
J. Immunol. 165:1322-1330(2000).
[21]
INTERACTION WITH TNFRSF19L.
PubMed=11313261; DOI=10.1182/blood.V97.9.2702;
Sica G.L., Zhu G., Tamada K., Liu D., Ni J., Chen L.;
"RELT, a new member of the tumor necrosis factor receptor superfamily,
is selectively expressed in hematopoietic tissues and activates
transcription factor NF-kappaB.";
Blood 97:2702-2707(2001).
[22]
INTERACTION WITH EDAR.
PubMed=11035039; DOI=10.1074/jbc.M008356200;
Kumar A., Eby M.T., Sinha S., Jasmin A., Chaudhary P.M.;
"The ectodermal dysplasia receptor activates the nuclear factor-
kappaB, JNK, and cell death pathways and binds to ectodysplasin A.";
J. Biol. Chem. 276:2668-2677(2001).
[23]
INTERACTION WITH BIRC2.
PubMed=11907583; DOI=10.1038/416345a;
Li X., Yang Y., Ashwell J.D.;
"TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2.";
Nature 416:345-347(2002).
[24]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=15383523; DOI=10.1074/jbc.M407284200;
He L., Grammer A.C., Wu X., Lipsky P.E.;
"TRAF3 forms heterotrimers with TRAF2 and modulates its ability to
mediate NF-{kappa}B activation.";
J. Biol. Chem. 279:55855-55865(2004).
[25]
UBIQUITINATION AT LYS-185 AND LYS-193, IDENTIFICATION BY MASS
SPECTROMETRY, AND MUTAGENESIS OF LYS-185 AND LYS-193.
PubMed=15468071; DOI=10.1002/pmic.200401000;
Lee J.S., Hong U.S., Lee T.H., Yoon S.K., Yoon J.B.;
"Mass spectrometric analysis of tumor necrosis factor receptor-
associated factor 1 ubiquitination mediated by cellular inhibitor of
apoptosis 2.";
Proteomics 4:3376-3382(2004).
[26]
FUNCTION, INTERACTION WITH TICAM1, CLEAVAGE BY CASP8, AND MUTAGENESIS
OF ASP-163.
PubMed=16323247; DOI=10.1002/eji.200535415;
Su X., Li S., Meng M., Qian W., Xie W., Chen D., Zhai Z., Shu H.B.;
"TNF receptor-associated factor-1 (TRAF1) negatively regulates
Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF)-
mediated signaling.";
Eur. J. Immunol. 36:199-206(2006).
[27]
FUNCTION, AND PHOSPHORYLATION.
PubMed=18429822; DOI=10.1111/j.1365-2443.2008.01182.x;
Kato T. Jr., Gotoh Y., Hoffmann A., Ono Y.;
"Negative regulation of constitutive NF-kappaB and JNK signaling by
PKN1-mediated phosphorylation of TRAF1.";
Genes Cells 13:509-520(2008).
[28]
FUNCTION, AND INTERACTION WITH TNFRSF13C.
PubMed=19698991; DOI=10.1016/j.molimm.2009.07.029;
Lavorgna A., De Filippi R., Formisano S., Leonardi A.;
"TNF receptor-associated factor 1 is a positive regulator of the NF-
kappaB alternative pathway.";
Mol. Immunol. 46:3278-3282(2009).
[29]
FUNCTION, AND INTERACTION WITH TNFRSF1A; TNFRSF1B AND TRAF2.
PubMed=19287455; DOI=10.1038/onc.2009.29;
Wicovsky A., Henkler F., Salzmann S., Scheurich P., Kneitz C.,
Wajant H.;
"Tumor necrosis factor receptor-associated factor-1 enhances
proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2
cooperation.";
Oncogene 28:1769-1781(2009).
[30]
INTERACTION WITH BIRC2.
PubMed=20447407; DOI=10.1016/j.jmb.2010.04.055;
Mace P.D., Smits C., Vaux D.L., Silke J., Day C.L.;
"Asymmetric recruitment of cIAPs by TRAF2.";
J. Mol. Biol. 400:8-15(2010).
[31]
UBIQUITINATION.
PubMed=19937093; DOI=10.1007/s11010-009-0315-y;
Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X.,
Xie P., Xing G., He F., Zhang L.;
"Ubiquitin ligase Smurf1 targets TRAF family proteins for
ubiquitination and degradation.";
Mol. Cell. Biochem. 338:11-17(2010).
[32]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 181-244 IN COMPLEX WITH TRAF2
AND BIRC3, SUBUNIT, AND FUNCTION.
PubMed=20385093; DOI=10.1016/j.molcel.2010.03.009;
Zheng C., Kabaleeswaran V., Wang Y., Cheng G., Wu H.;
"Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2
complexes: affinity, specificity, and regulation.";
Mol. Cell 38:101-113(2010).
[33]
VARIANT [LARGE SCALE ANALYSIS] THR-139.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: Adapter molecule that regulates the activation of NF-
kappa-B and JNK. Plays a role in the regulation of cell survival
and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part
of a E3 ubiquitin-protein ligase complex that promotes
ubiquitination of target proteins, such as MAP3K14. The
TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-
ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.
{ECO:0000269|PubMed:10692572, ECO:0000269|PubMed:16323247,
ECO:0000269|PubMed:18429822, ECO:0000269|PubMed:19287455,
ECO:0000269|PubMed:19698991, ECO:0000269|PubMed:20385093}.
-!- SUBUNIT: Homotrimer. Heterotrimer with TRAF2. Interacts with
TNFRSF1A/TNFR1, TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40,
TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13C,
TNFRSF18/AITR, TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT,
XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1, TANK/ITRAF, TRAIP and
RIPK2. Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2
or BIRC3 molecule interacts with a heterotrimer formed by TRAF1
and TRAF2. Interacts with NFATC2IP, TRAFD1 and with HIVEP3 (By
similarity). Interacts with MAP3K14. {ECO:0000250,
ECO:0000269|PubMed:10037686, ECO:0000269|PubMed:10809768,
ECO:0000269|PubMed:10903733, ECO:0000269|PubMed:11035039,
ECO:0000269|PubMed:11313261, ECO:0000269|PubMed:11907583,
ECO:0000269|PubMed:15383523, ECO:0000269|PubMed:16323247,
ECO:0000269|PubMed:19287455, ECO:0000269|PubMed:19698991,
ECO:0000269|PubMed:20385093, ECO:0000269|PubMed:20447407,
ECO:0000269|PubMed:8069916, ECO:0000269|PubMed:8627180,
ECO:0000269|PubMed:8710854, ECO:0000269|PubMed:9418902,
ECO:0000269|PubMed:9607925, ECO:0000269|PubMed:9642260,
ECO:0000269|PubMed:9705938, ECO:0000269|PubMed:9718306,
ECO:0000269|PubMed:9774460}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-359224, EBI-359224;
B2R8Y4:-; NbExp=3; IntAct=EBI-359224, EBI-10175581;
Q5W150:-; NbExp=3; IntAct=EBI-359224, EBI-10248148;
Q96EJ4:-; NbExp=4; IntAct=EBI-359224, EBI-750454;
Q9NWL9:-; NbExp=3; IntAct=EBI-359224, EBI-10315054;
Q9NQ94:A1CF; NbExp=5; IntAct=EBI-359224, EBI-2809489;
Q08117:AES; NbExp=3; IntAct=EBI-359224, EBI-717810;
Q08117-2:AES; NbExp=5; IntAct=EBI-359224, EBI-11741437;
Q02040-3:AKAP17A; NbExp=3; IntAct=EBI-359224, EBI-10222656;
P29972:AQP1; NbExp=3; IntAct=EBI-359224, EBI-745213;
Q8N5N6:ARSJ; NbExp=3; IntAct=EBI-359224, EBI-10266832;
A0AVN2:BARD1; NbExp=3; IntAct=EBI-359224, EBI-9977322;
P41182:BCL6; NbExp=5; IntAct=EBI-359224, EBI-765407;
Q9BXY8:BEX2; NbExp=3; IntAct=EBI-359224, EBI-745073;
Q13489:BIRC3; NbExp=2; IntAct=EBI-359224, EBI-517709;
Q9NVL8:C14orf105; NbExp=3; IntAct=EBI-359224, EBI-10238351;
Q9NX04:C1orf109; NbExp=5; IntAct=EBI-359224, EBI-8643161;
Q8TAB5:C1orf216; NbExp=5; IntAct=EBI-359224, EBI-747505;
Q53TS8:C2CD6; NbExp=3; IntAct=EBI-359224, EBI-739879;
Q96GV9:C5orf30; NbExp=3; IntAct=EBI-359224, EBI-2350695;
Q9Y2V2:CARHSP1; NbExp=3; IntAct=EBI-359224, EBI-718719;
Q8IYX3:CCDC116; NbExp=3; IntAct=EBI-359224, EBI-744311;
Q96HB5-4:CCDC120; NbExp=3; IntAct=EBI-359224, EBI-10185348;
Q8IYE0-2:CCDC146; NbExp=3; IntAct=EBI-359224, EBI-10247802;
Q8TD31-3:CCHCR1; NbExp=5; IntAct=EBI-359224, EBI-10175300;
Q99618:CDCA3; NbExp=5; IntAct=EBI-359224, EBI-739534;
P38936:CDKN1A; NbExp=3; IntAct=EBI-359224, EBI-375077;
P42772:CDKN2B; NbExp=5; IntAct=EBI-359224, EBI-711280;
O15519:CFLAR; NbExp=5; IntAct=EBI-359224, EBI-514941;
Q9NX63:CHCHD3; NbExp=3; IntAct=EBI-359224, EBI-743375;
P10606:COX5B; NbExp=3; IntAct=EBI-359224, EBI-1053725;
Q24JT5:CRYGA; NbExp=3; IntAct=EBI-359224, EBI-10239205;
Q6BCY4:CYB5R2; NbExp=3; IntAct=EBI-359224, EBI-744761;
Q8TB45:DEPTOR; NbExp=3; IntAct=EBI-359224, EBI-2359040;
Q9NQL9:DMRT3; NbExp=3; IntAct=EBI-359224, EBI-9679045;
Q7L591:DOK3; NbExp=3; IntAct=EBI-359224, EBI-2834978;
Q7L591-3:DOK3; NbExp=4; IntAct=EBI-359224, EBI-10694655;
Q9HAK2:EBF2; NbExp=4; IntAct=EBI-359224, EBI-12267154;
Q13011:ECH1; NbExp=3; IntAct=EBI-359224, EBI-711968;
Q08426:EHHADH; NbExp=3; IntAct=EBI-359224, EBI-2339219;
Q01844:EWSR1; NbExp=3; IntAct=EBI-359224, EBI-739737;
Q3B820:FAM161A; NbExp=5; IntAct=EBI-359224, EBI-719941;
Q9NVL1:FAM86C1; NbExp=3; IntAct=EBI-359224, EBI-751617;
Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-359224, EBI-10244131;
Q96D16:FBXL18; NbExp=3; IntAct=EBI-359224, EBI-744419;
P15408:FOSL2; NbExp=5; IntAct=EBI-359224, EBI-3893419;
P15976-2:GATA1; NbExp=3; IntAct=EBI-359224, EBI-9090198;
P23769:GATA2; NbExp=3; IntAct=EBI-359224, EBI-2806671;
Q8WXI9:GATAD2B; NbExp=3; IntAct=EBI-359224, EBI-923440;
P55040:GEM; NbExp=5; IntAct=EBI-359224, EBI-744104;
Q14161:GIT2; NbExp=2; IntAct=EBI-359224, EBI-1046878;
O76003:GLRX3; NbExp=5; IntAct=EBI-359224, EBI-374781;
Q8NEA9:GMCL1P1; NbExp=3; IntAct=EBI-359224, EBI-745707;
P63218:GNG5; NbExp=3; IntAct=EBI-359224, EBI-10220734;
Q9H8Y8:GORASP2; NbExp=7; IntAct=EBI-359224, EBI-739467;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-359224, EBI-2514791;
Q9UBP5:HEY2; NbExp=5; IntAct=EBI-359224, EBI-750630;
P49639:HOXA1; NbExp=3; IntAct=EBI-359224, EBI-740785;
P09022:Hoxa1 (xeno); NbExp=4; IntAct=EBI-359224, EBI-3957603;
P35452:HOXD12; NbExp=3; IntAct=EBI-359224, EBI-10206752;
Q15040:JOSD1; NbExp=3; IntAct=EBI-359224, EBI-2510602;
Q5T5P2-6:KIAA1217; NbExp=3; IntAct=EBI-359224, EBI-10188326;
Q2WGJ6:KLHL38; NbExp=3; IntAct=EBI-359224, EBI-6426443;
Q6PJG3:LATS1; NbExp=3; IntAct=EBI-359224, EBI-10253976;
Q96JN0:LCOR; NbExp=3; IntAct=EBI-359224, EBI-746045;
Q96JN0-2:LCOR; NbExp=4; IntAct=EBI-359224, EBI-10961483;
Q8TBB1:LNX1; NbExp=6; IntAct=EBI-359224, EBI-739832;
A0A090N7T1:LOC401431; NbExp=4; IntAct=EBI-359224, EBI-12083408;
Q15555:MAPRE2; NbExp=7; IntAct=EBI-359224, EBI-739717;
P43243:MATR3; NbExp=4; IntAct=EBI-359224, EBI-352602;
Q9H7H0:METTL17; NbExp=3; IntAct=EBI-359224, EBI-749353;
Q6PF18:MORN3; NbExp=9; IntAct=EBI-359224, EBI-9675802;
P00540:MOS; NbExp=5; IntAct=EBI-359224, EBI-1757866;
Q9P2K5-2:MYEF2; NbExp=3; IntAct=EBI-359224, EBI-10318831;
O76041:NEBL; NbExp=3; IntAct=EBI-359224, EBI-2880203;
Q7Z417:NUFIP2; NbExp=3; IntAct=EBI-359224, EBI-1210753;
Q9BVL2:NUP58; NbExp=9; IntAct=EBI-359224, EBI-2811583;
Q7RTU3:OLIG3; NbExp=5; IntAct=EBI-359224, EBI-10225049;
Q9HBE1-4:PATZ1; NbExp=4; IntAct=EBI-359224, EBI-11022007;
Q5JS98:PBX3; NbExp=3; IntAct=EBI-359224, EBI-10244393;
Q08499:PDE4D; NbExp=3; IntAct=EBI-359224, EBI-1642831;
Q96BD5:PHF21A; NbExp=3; IntAct=EBI-359224, EBI-745085;
Q13526:PIN1; NbExp=3; IntAct=EBI-359224, EBI-714158;
Q16512:PKN1; NbExp=4; IntAct=EBI-359224, EBI-602382;
Q494U1:PLEKHN1; NbExp=3; IntAct=EBI-359224, EBI-10241513;
Q3SYA9:POM121L1P; NbExp=5; IntAct=EBI-359224, EBI-10241319;
Q969H6:POP5; NbExp=5; IntAct=EBI-359224, EBI-366525;
Q96KQ4:PPP1R13B; NbExp=3; IntAct=EBI-359224, EBI-1105153;
Q9NQW5:PRDM7; NbExp=3; IntAct=EBI-359224, EBI-10312471;
P25786:PSMA1; NbExp=3; IntAct=EBI-359224, EBI-359352;
P20618:PSMB1; NbExp=5; IntAct=EBI-359224, EBI-372273;
Q2TAL8:QRICH1; NbExp=5; IntAct=EBI-359224, EBI-2798044;
Q9UJF2:RASAL2; NbExp=3; IntAct=EBI-359224, EBI-359444;
Q8WWW0:RASSF5; NbExp=3; IntAct=EBI-359224, EBI-367390;
Q96IZ5:RBM41; NbExp=3; IntAct=EBI-359224, EBI-740773;
Q8IUH3:RBM45; NbExp=3; IntAct=EBI-359224, EBI-2512147;
Q13546:RIPK1; NbExp=5; IntAct=EBI-359224, EBI-358507;
Q14D33:RTP5; NbExp=3; IntAct=EBI-359224, EBI-10217913;
Q9NUL5:RYDEN; NbExp=3; IntAct=EBI-359224, EBI-10313866;
Q9BWG6:SCNM1; NbExp=7; IntAct=EBI-359224, EBI-748391;
Q9Y2K2-3:SIK3; NbExp=3; IntAct=EBI-359224, EBI-10326390;
Q6ZT89:SLC25A48; NbExp=3; IntAct=EBI-359224, EBI-10255185;
P12236:SLC25A6; NbExp=3; IntAct=EBI-359224, EBI-356254;
Q13573:SNW1; NbExp=3; IntAct=EBI-359224, EBI-632715;
Q9NZD8:SPG21; NbExp=5; IntAct=EBI-359224, EBI-742688;
A1L4H1:SSC5D; NbExp=3; IntAct=EBI-359224, EBI-10172867;
Q13188:STK3; NbExp=5; IntAct=EBI-359224, EBI-992580;
Q8N0S2:SYCE1; NbExp=3; IntAct=EBI-359224, EBI-6872807;
P56279:TCL1A; NbExp=7; IntAct=EBI-359224, EBI-749995;
D3DUQ6:TEAD4; NbExp=3; IntAct=EBI-359224, EBI-10176734;
Q01664:TFAP4; NbExp=3; IntAct=EBI-359224, EBI-2514218;
A0A024R4Q5:TFPT; NbExp=4; IntAct=EBI-359224, EBI-11527449;
Q9BT49:THAP7; NbExp=5; IntAct=EBI-359224, EBI-741350;
Q12933:TRAF2; NbExp=6; IntAct=EBI-359224, EBI-355744;
Q9Y4K3:TRAF6; NbExp=13; IntAct=EBI-359224, EBI-359276;
P36406:TRIM23; NbExp=3; IntAct=EBI-359224, EBI-740098;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-359224, EBI-5235829;
Q9Y260:TRPV6; NbExp=5; IntAct=EBI-359224, EBI-750052;
Q9Y5U2:TSSC4; NbExp=3; IntAct=EBI-359224, EBI-717229;
Q5TAP6:UTP14C; NbExp=4; IntAct=EBI-359224, EBI-11737646;
Q9BTA9:WAC; NbExp=3; IntAct=EBI-359224, EBI-749118;
Q05516:ZBTB16; NbExp=4; IntAct=EBI-359224, EBI-711925;
Q53FD0:ZC2HC1C; NbExp=3; IntAct=EBI-359224, EBI-740767;
Q9BQ24:ZFYVE21; NbExp=3; IntAct=EBI-359224, EBI-2849569;
Q68DK2-5:ZFYVE26; NbExp=3; IntAct=EBI-359224, EBI-8656416;
Q15973:ZNF124; NbExp=5; IntAct=EBI-359224, EBI-2555767;
P17024:ZNF20; NbExp=5; IntAct=EBI-359224, EBI-717634;
Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-359224, EBI-740727;
Q8IYI8:ZNF440; NbExp=8; IntAct=EBI-359224, EBI-726439;
Q8TBZ5:ZNF502; NbExp=5; IntAct=EBI-359224, EBI-10273699;
Q96KM6:ZNF512B; NbExp=5; IntAct=EBI-359224, EBI-1049952;
Q8TBZ8:ZNF564; NbExp=5; IntAct=EBI-359224, EBI-10273713;
Q7Z3I7:ZNF572; NbExp=6; IntAct=EBI-359224, EBI-10172590;
Q9P0T4:ZNF581; NbExp=3; IntAct=EBI-359224, EBI-745520;
Q96SQ5:ZNF587; NbExp=5; IntAct=EBI-359224, EBI-6427977;
Q6ZS27-3:ZNF662; NbExp=3; IntAct=EBI-359224, EBI-10255155;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13077-1; Sequence=Displayed;
Name=2;
IsoId=Q13077-2; Sequence=VSP_043092;
Note=No experimental confirmation available.;
-!- DOMAIN: The coiled coil domain mediates homo- and hetero-
oligomerization. {ECO:0000269|PubMed:10692572}.
-!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic
domains. {ECO:0000269|PubMed:10692572}.
-!- DOMAIN: Cleavage by CASP8 liberates a C-terminal fragment that
promotes apoptosis and inhibits the activation of NF-kappa-B in
response to TNF signaling. {ECO:0000269|PubMed:10692572}.
-!- PTM: Polyubiquitinated by BIRC2 and/or BIRC3, leading to its
subsequent proteasomal degradation. {ECO:0000269|PubMed:15468071,
ECO:0000269|PubMed:19937093}.
-!- CAUTION: Lacks a RING domain and has therefore no E3 ubiquitin-
protein ligase activity by itself. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC03449.1; Type=Frameshift; Positions=111; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U19261; AAA62309.1; -; mRNA.
EMBL; AK090468; BAC03449.1; ALT_FRAME; mRNA.
EMBL; AK295959; BAG58739.1; -; mRNA.
EMBL; AK315476; BAG37860.1; -; mRNA.
EMBL; AL832989; CAH56343.1; -; mRNA.
EMBL; BT019408; AAV38215.1; -; mRNA.
EMBL; AC006430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87479.1; -; Genomic_DNA.
EMBL; BC024145; AAH24145.1; -; mRNA.
CCDS; CCDS55335.1; -. [Q13077-2]
CCDS; CCDS6825.1; -. [Q13077-1]
PIR; B55649; B55649.
RefSeq; NP_001177874.1; NM_001190945.1. [Q13077-1]
RefSeq; NP_001177876.1; NM_001190947.1. [Q13077-2]
RefSeq; NP_005649.1; NM_005658.4. [Q13077-1]
UniGene; Hs.531251; -.
PDB; 3M0D; X-ray; 2.80 A; C=181-244.
PDB; 5E1T; X-ray; 2.80 A; A/B/C=220-416.
PDB; 5H10; X-ray; 3.21 A; A/B/C=220-416.
PDBsum; 3M0D; -.
PDBsum; 5E1T; -.
PDBsum; 5H10; -.
ProteinModelPortal; Q13077; -.
SMR; Q13077; -.
BioGrid; 113037; 219.
DIP; DIP-27514N; -.
IntAct; Q13077; 228.
MINT; MINT-1131534; -.
STRING; 9606.ENSP00000362994; -.
iPTMnet; Q13077; -.
PhosphoSitePlus; Q13077; -.
BioMuta; TRAF1; -.
DMDM; 6707734; -.
MaxQB; Q13077; -.
PaxDb; Q13077; -.
PeptideAtlas; Q13077; -.
PRIDE; Q13077; -.
DNASU; 7185; -.
Ensembl; ENST00000373887; ENSP00000362994; ENSG00000056558. [Q13077-1]
Ensembl; ENST00000540010; ENSP00000443183; ENSG00000056558. [Q13077-1]
Ensembl; ENST00000546084; ENSP00000438583; ENSG00000056558. [Q13077-2]
GeneID; 7185; -.
KEGG; hsa:7185; -.
UCSC; uc004bku.3; human. [Q13077-1]
CTD; 7185; -.
DisGeNET; 7185; -.
EuPathDB; HostDB:ENSG00000056558.10; -.
GeneCards; TRAF1; -.
HGNC; HGNC:12031; TRAF1.
HPA; CAB009593; -.
HPA; HPA001852; -.
MIM; 601711; gene.
neXtProt; NX_Q13077; -.
OpenTargets; ENSG00000056558; -.
PharmGKB; PA36708; -.
eggNOG; ENOG410ISDN; Eukaryota.
eggNOG; ENOG410YE68; LUCA.
GeneTree; ENSGT00550000074359; -.
HOGENOM; HOG000231558; -.
HOVERGEN; HBG058222; -.
InParanoid; Q13077; -.
KO; K03172; -.
OMA; IHQSQLD; -.
OrthoDB; EOG091G0GHD; -.
PhylomeDB; Q13077; -.
TreeFam; TF321154; -.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
SignaLink; Q13077; -.
SIGNOR; Q13077; -.
EvolutionaryTrace; Q13077; -.
GeneWiki; TRAF1; -.
GenomeRNAi; 7185; -.
PMAP-CutDB; Q13077; -.
PRO; PR:Q13077; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000056558; -.
CleanEx; HS_TRAF1; -.
Genevisible; Q13077; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 2.60.210.10; -; 1.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR012227; TNF_rcpt--assoc_TRAF.
InterPro; IPR008974; TRAF-like.
InterPro; IPR027136; TRAF1.
InterPro; IPR032070; TRAF_BIRC3-bd.
PANTHER; PTHR10131:SF91; PTHR10131:SF91; 1.
Pfam; PF16673; TRAF_BIRC3_bd; 1.
PIRSF; PIRSF015614; TRAF; 1.
SMART; SM00061; MATH; 1.
SUPFAM; SSF49599; SSF49599; 1.
PROSITE; PS50144; MATH; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Coiled coil;
Complete proteome; Isopeptide bond; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 416 TNF receptor-associated factor 1.
/FTId=PRO_0000056397.
DOMAIN 266 412 MATH. {ECO:0000255|PROSITE-
ProRule:PRU00129}.
COILED 182 264
SITE 163 164 Cleavage; by CASP8.
MOD_RES 146 146 Phosphoserine.
{ECO:0000250|UniProtKB:P39428}.
CROSSLNK 185 185 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:15468071}.
CROSSLNK 193 193 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:15468071}.
VAR_SEQ 1 122 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043092.
VARIANT 139 139 M -> T (in dbSNP:rs113495277).
{ECO:0000269|PubMed:18987736}.
/FTId=VAR_054161.
MUTAGEN 163 163 D->A: Abolishes CASP8-mediated cleavage.
{ECO:0000269|PubMed:10692572,
ECO:0000269|PubMed:16323247}.
MUTAGEN 185 185 K->R: Nearly abolished ubiquitination;
when associated with R-193.
{ECO:0000269|PubMed:15468071}.
MUTAGEN 193 193 K->R: Nearly abolished ubiquitination;
when associated with R-185.
{ECO:0000269|PubMed:15468071}.
HELIX 183 241 {ECO:0000244|PDB:3M0D}.
STRAND 265 274 {ECO:0000244|PDB:5E1T}.
HELIX 276 283 {ECO:0000244|PDB:5E1T}.
TURN 284 286 {ECO:0000244|PDB:5E1T}.
STRAND 290 292 {ECO:0000244|PDB:5E1T}.
STRAND 296 299 {ECO:0000244|PDB:5E1T}.
STRAND 304 310 {ECO:0000244|PDB:5E1T}.
HELIX 315 317 {ECO:0000244|PDB:5E1T}.
TURN 318 320 {ECO:0000244|PDB:5E1T}.
STRAND 321 329 {ECO:0000244|PDB:5E1T}.
HELIX 334 336 {ECO:0000244|PDB:5E1T}.
STRAND 345 350 {ECO:0000244|PDB:5E1T}.
STRAND 352 355 {ECO:0000244|PDB:5E1T}.
STRAND 358 362 {ECO:0000244|PDB:5E1T}.
STRAND 375 378 {ECO:0000244|PDB:5E1T}.
STRAND 382 389 {ECO:0000244|PDB:5E1T}.
HELIX 390 392 {ECO:0000244|PDB:5E1T}.
STRAND 400 402 {ECO:0000244|PDB:5E1T}.
STRAND 405 412 {ECO:0000244|PDB:5E1T}.
SEQUENCE 416 AA; 46164 MW; A956A123A40D284A CRC64;
MASSSGSSPR PAPDENEFPF GCPPTVCQDP KEPRALCCAG CLSENPRNGE DQICPKCRGE
DLQSISPGSR LRTQEKAHPE VAEAGIGCPF AGVGCSFKGS PQSVQEHEVT SQTSHLNLLL
GFMKQWKARL GCGLESGPMA LEQNLSDLQL QAAVEVAGDL EVDCYRAPCS ESQEELALQH
FMKEKLLAEL EGKLRVFENI VAVLNKEVEA SHLALATSIH QSQLDRERIL SLEQRVVELQ
QTLAQKDQAL GKLEQSLRLM EEASFDGTFL WKITNVTRRC HESACGRTVS LFSPAFYTAK
YGYKLCLRLY LNGDGTGKRT HLSLFIVIMR GEYDALLPWP FRNKVTFMLL DQNNREHAID
AFRPDLSSAS FQRPQSETNV ASGCPLFFPL SKLQSPKHAY VKDDTMFLKC IVETST


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P93206Hu01 Epstein Barr Virus Induced Protein 3 (EBI3) Organism: Homo sapiens (Human) Source: Escherichia coli 100ug
cyt-621 Recombinant Mouse Epstein Barr Virus Induced 3 1mg


 

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