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TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (Tumor necrosis factor type 2 receptor-associated protein 3)

 TRAF2_HUMAN             Reviewed;         501 AA.
Q12933; A8K107; B4DPJ7; Q7Z337; Q96NT2;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
25-OCT-2017, entry version 213.
RecName: Full=TNF receptor-associated factor 2;
EC=2.3.2.27;
AltName: Full=E3 ubiquitin-protein ligase TRAF2;
AltName: Full=RING-type E3 ubiquitin transferase TRAF2 {ECO:0000305};
AltName: Full=Tumor necrosis factor type 2 receptor-associated protein 3;
Name=TRAF2; Synonyms=TRAP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH
TNFRSF1B/TNFR2.
PubMed=7639698; DOI=10.1042/bj3090825;
Song H.Y., Donner D.B.;
"Association of a RING finger protein with the cytoplasmic domain of
the human type-2 tumour necrosis factor receptor.";
Biochem. J. 309:825-829(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain, Cerebellum, and Kidney;
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 4).
TISSUE=Endometrium;
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 [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAY-2004) 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=Colon, Fetal brain, Kidney, Leukocyte, Stomach, and Uterus;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 201-501, AND INTERACTION WITH TRAF1 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 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).
[10]
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).
[11]
INTERACTION WITH TNFRSF14.
PubMed=9153189; DOI=10.1074/jbc.272.21.13471;
Hsu H., Solovyev I., Colombero A., Elliott R., Kelley M., Boyle W.J.;
"ATAR, a novel tumor necrosis factor receptor family member, signals
through TRAF2 and TRAF5.";
J. Biol. Chem. 272:13471-13474(1997).
[12]
IDENTIFICATION IN A COMPLEX WITH TNFRSF8; TNFRSF1B, TRAF1 AND TRAIP,
AND INTERACTION WITH TRAIP.
PubMed=9104814; DOI=10.1084/jem.185.7.1275;
Lee S.Y., Lee S.Y., Choi Y.;
"TRAF-interacting protein (TRIP): a novel component of the tumor
necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes
that inhibits TRAF2-mediated NF-kappaB activation.";
J. Exp. Med. 185:1275-1285(1997).
[13]
INTERACTION WITH MAP3K14.
PubMed=9020361; DOI=10.1038/385540a0;
Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D.;
"MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and
IL-1.";
Nature 385:540-544(1997).
[14]
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).
[15]
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).
[16]
INTERACTION WITH CD27.
PubMed=9692890;
DOI=10.1002/(SICI)1521-4141(199807)28:07<2208::AID-IMMU2208>3.0.CO;2-L;
Gravestein L.A., Amsen D., Boes M., Calvo C.R., Kruisbeek A.M.,
Borst J.;
"The TNF receptor family member CD27 signals to Jun N-terminal kinase
via Traf-2.";
Eur. J. Immunol. 28:2208-2216(1998).
[17]
INTERACTION WITH TNFRSF4.
PubMed=9488716; DOI=10.1074/jbc.273.10.5808;
Kawamata S., Hori T., Imura A., Takaori-Kondo A., Uchiyama T.;
"Activation of OX40 signal transduction pathways leads to tumor
necrosis factor receptor-associated factor (TRAF) 2- and TRAF5-
mediated NF-kappaB activation.";
J. Biol. Chem. 273:5808-5814(1998).
[18]
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).
[19]
INTERACTION WITH CDK9.
PubMed=9827693;
DOI=10.1002/(SICI)1097-4644(19981215)71:4<467::AID-JCB2>3.0.CO;2-G;
MacLachlan T.K., Sang N., De Luca A., Puri P.L., Levrero M.,
Giordano A.;
"Binding of CDK9 to TRAF2.";
J. Cell. Biochem. 71:467-478(1998).
[20]
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).
[21]
INTERACTION WITH MAP3K5.
PubMed=9774977; DOI=10.1016/S1097-2765(00)80283-X;
Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M.,
Miyazono K., Ichijo H.;
"ASK1 is essential for JNK/SAPK activation by TRAF2.";
Mol. Cell 2:389-395(1998).
[22]
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).
[23]
IDENTIFICATION IN A COMPLEX WITH TBK1 AND TANK.
TISSUE=Spleen;
PubMed=10581243; DOI=10.1093/emboj/18.23.6694;
Pomerantz J.L., Baltimore D.;
"NF-kB activation by a signaling complex containing TRAF2, TANK, and
TBK1, a novel IKK-related kinase.";
EMBO J. 18:6694-6704(1999).
[24]
INTERACTION WITH IL15RA.
PubMed=10463949;
Bulfone-Paus S., Bulanova E., Pohl T., Budagian V., Duerkop H.,
Rueckert R., Kunzendorf U., Paus R., Krause H.;
"Death deflected: IL-15 inhibits TNF-alpha-mediated apoptosis in
fibroblasts by TRAF2 recruitment to the IL-15Ralpha chain.";
FASEB J. 13:1575-1585(1999).
[25]
INTERACTION WITH MAP3K1, AND FUNCTION.
PubMed=10346818; DOI=10.1101/gad.13.10.1297;
Baud V., Liu Z.-G., Bennett B., Suzuki N., Xia Y., Karin M.;
"Signaling by proinflammatory cytokines: oligomerization of TRAF2 and
TRAF6 is sufficient for JNK and IKK activation and target gene
induction via an amino-terminal effector domain.";
Genes Dev. 13:1297-1308(1999).
[26]
INTERACTION WITH TNFRSF18.
TISSUE=T-cell;
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).
[27]
INTERACTION WITH TNFRSF16.
PubMed=10514511; DOI=10.1074/jbc.274.42.30202;
Ye X., Mehlen P., Rabizadeh S., VanArsdale T., Zhang H., Shin H.,
Wang J.J.L., Leo E., Zapata J.M., Hauser C.A., Reed J.C.,
Bredesen D.E.;
"TRAF family proteins interact with the common neurotrophin receptor
and modulate apoptosis induction.";
J. Biol. Chem. 274:30202-30208(1999).
[28]
INTERACTION WITH TNIK.
PubMed=10521462; DOI=10.1074/jbc.274.43.30729;
Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.;
"TNIK, a novel member of the germinal center kinase family that
activates the c-Jun N-terminal kinase pathway and regulates the
cytoskeleton.";
J. Biol. Chem. 274:30729-30737(1999).
[29]
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).
[30]
INTERACTION WITH TDP2.
PubMed=10764746; DOI=10.1074/jbc.M000531200;
Pype S., Declercq W., Ibrahimi A., Michiels C.,
Van Rietschoten J.G.I., Dewulf N., de Boer M., Vandenabeele P.,
Huylebroeck D., Remacle J.E.;
"TTRAP, a novel protein that associates with CD40, tumor necrosis
factor (TNF) receptor-75 and TNF receptor-associated factors (TRAFs),
and that inhibits nuclear factor-kappa B activation.";
J. Biol. Chem. 275:18586-18593(2000).
[31]
INTERACTION WITH TNFRSF13B.
PubMed=10880535; DOI=10.1084/jem.192.1.137;
Xia X.-Z., Treanor J., Senaldi G., Khare S.D., Boone T., Kelley M.,
Theill L.E., Colombero A., Solovyev I., Lee F., McCabe S., Elliott R.,
Miner K., Hawkins N., Guo J., Stolina M., Yu G., Wang J., Delaney J.,
Meng S.-Y., Boyle W.J., Hsu H.;
"TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis
factor family member involved in B cell regulation.";
J. Exp. Med. 192:137-143(2000).
[32]
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).
[33]
INTERACTION WITH ERN1 AND TAOK3.
PubMed=11278723; DOI=10.1074/jbc.M010677200;
Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T.,
Tohyama M.;
"Activation of caspase-12, an endoplastic reticulum (ER) resident
caspase, through tumor necrosis factor receptor-associated factor 2-
dependent mechanism in response to the ER stress.";
J. Biol. Chem. 276:13935-13940(2001).
[34]
INTERACTION WITH SIAH2, AND DEGRADATION.
PubMed=12411493; DOI=10.1093/emboj/cdf576;
Habelhah H., Frew I.J., Laine A., Janes P.W., Relaix F., Sassoon D.,
Bowtell D.D.L., Ronai Z.;
"Stress-induced decrease in TRAF2 stability is mediated by Siah2.";
EMBO J. 21:5756-5765(2002).
[35]
FUNCTION.
PubMed=11784851; DOI=10.1128/MCB.22.3.737-749.2002;
Chadee D.N., Yuasa T., Kyriakis J.M.;
"Direct activation of mitogen-activated protein kinase kinase kinase
MEKK1 by the Ste20p homologue GCK and the adapter protein TRAF2.";
Mol. Cell. Biol. 22:737-749(2002).
[36]
FUNCTION, INTERACTION WITH BIRC2 AND BIRC3, UBIQUITINATION BY BIRC2,
AND DEGRADATION.
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).
[37]
FUNCTION, UBIQUITINATION, AND DEUBIQUITINATION BY CYLD.
PubMed=12917689; DOI=10.1038/nature01803;
Trompouki E., Hatzivassiliou E., Tsichritzis T., Farmer H.,
Ashworth A., Mosialos G.;
"CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB
activation by TNFR family members.";
Nature 424:793-796(2003).
[38]
INTERACTION WITH CYLD, UBIQUITINATION, AND DEUBIQUITINATION BY CYLD.
PubMed=12917691; DOI=10.1038/nature01802;
Kovalenko A., Chable-Bessia C., Cantarella G., Israeel A., Wallach D.,
Courtois G.;
"The tumour suppressor CYLD negatively regulates NF-kappaB signalling
by deubiquitination.";
Nature 424:801-805(2003).
[39]
INTERACTION WITH DAB2IP.
PubMed=15310755; DOI=10.1074/jbc.M407617200;
Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.;
"AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-
induced ASK1-JNK activation.";
J. Biol. Chem. 279:44955-44965(2004).
[40]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TRAF3, 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).
[41]
FUNCTION, AND INTERACTION WITH EIF2AK2.
PubMed=15121867; DOI=10.1128/MCB.24.10.4502-4512.2004;
Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J.,
Nakano H., Alcami J., Esteban M.;
"TRAF family proteins link PKR with NF-kappa B activation.";
Mol. Cell. Biol. 24:4502-4512(2004).
[42]
INTERACTION WITH MAVS.
PubMed=16153868; DOI=10.1016/j.molcel.2005.08.014;
Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.;
"VISA is an adapter protein required for virus-triggered IFN-beta
Signaling.";
Mol. Cell 19:727-740(2005).
[43]
UBIQUITINATION, AND DEUBIQUITINATION BY CYLD.
PubMed=15870263; DOI=10.1128/MCB.25.10.3886-3895.2005;
Reiley W., Zhang M., Wu X., Granger E., Sun S.C.;
"Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase
gamma-dependent phosphorylation.";
Mol. Cell. Biol. 25:3886-3895(2005).
[44]
INTERACTION WITH PTPN2.
PubMed=15696169; DOI=10.1038/ni1169;
van Vliet C., Bukczynska P.E., Puryer M.A., Sadek C.M., Shields B.J.,
Tremblay M.L., Tiganis T.;
"Selective regulation of tumor necrosis factor-induced Erk signaling
by Src family kinases and the T cell protein tyrosine phosphatase.";
Nat. Immunol. 6:253-260(2005).
[45]
INTERACTION WITH USP48.
PubMed=16214042; DOI=10.1016/j.cellsig.2005.03.017;
Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G.,
Hatzivassiliou E.G.;
"Human ubiquitin specific protease 31 is a deubiquitinating enzyme
implicated in activation of nuclear factor-kappaB.";
Cell. Signal. 18:83-92(2006).
[46]
INTERACTION WITH DAB2IP.
PubMed=17389591; DOI=10.1074/jbc.M701148200;
Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.;
"RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is
critical for tumor necrosis factor-induced ASK1-JNK/p38 activation.";
J. Biol. Chem. 282:14788-14796(2007).
[47]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[48]
FUNCTION, AND INTERACTION WITH BIRC2.
PubMed=19506082; DOI=10.1074/jbc.M109.029983;
Csomos R.A., Brady G.F., Duckett C.S.;
"Enhanced cytoprotective effects of the inhibitor of apoptosis protein
cellular IAP1 through stabilization with TRAF2.";
J. Biol. Chem. 284:20531-20539(2009).
[49]
FUNCTION, INTERACTION WITH IKKA; IKKB; TAB2 AND TAB3, UBIQUITINATION
AT LYS-31, PHOSPHORYLATION AT THR-117, MUTAGENESIS OF THR-117,
UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=19150425; DOI=10.1016/j.molcel.2008.11.023;
Li S., Wang L., Dorf M.E.;
"PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and
K63-linked polyubiquitination.";
Mol. Cell 33:30-42(2009).
[50]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH TNFRSF1A; RIPK1 AND IKKB,
MUTAGENESIS OF SER-11, AND PHOSPHORYLATION AT SER-11.
PubMed=18981220; DOI=10.1128/MCB.00699-08;
Blackwell K., Zhang L., Thomas G.S., Sun S., Nakano H., Habelhah H.;
"TRAF2 phosphorylation modulates tumor necrosis factor alpha-induced
gene expression and cell resistance to apoptosis.";
Mol. Cell. Biol. 29:303-314(2009).
[51]
FUNCTION, AND INTERACTION WITH MAP3K11.
PubMed=19918265; DOI=10.1038/cr.2009.125;
Sondarva G., Kundu C.N., Mehrotra S., Mishra R., Rangasamy V.,
Sathyanarayana P., Ray R.S., Rana B., Rana A.;
"TRAF2-MLK3 interaction is essential for TNF-alpha-induced MLK3
activation.";
Cell Res. 20:89-98(2010).
[52]
INTERACTION WITH BIRC2, SUBUNIT, AND HOMOTRIMERIZATION.
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).
[53]
FUNCTION, AND DOMAIN.
PubMed=20064526; DOI=10.1016/j.jmb.2010.01.008;
Zhang L., Blackwell K., Shi Z., Habelhah H.;
"The RING domain of TRAF2 plays an essential role in the inhibition of
TNFalpha-induced cell death but not in the activation of NF-kappaB.";
J. Mol. Biol. 396:528-539(2010).
[54]
UBIQUITINATION, AND FUNCTION.
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).
[55]
INTERACTION WITH TICAM1, AND FUNCTION.
PubMed=20047764; DOI=10.1016/j.molimm.2009.12.002;
Sasai M., Tatematsu M., Oshiumi H., Funami K., Matsumoto M.,
Hatakeyama S., Seya T.;
"Direct binding of TRAF2 and TRAF6 to TICAM-1/TRIF adaptor
participates in activation of the Toll-like receptor 3/4 pathway.";
Mol. Immunol. 47:1283-1291(2010).
[56]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, UBIQUITINATION,
INTERACTION WITH SPHK1, AND SPHINGOLIPID BINDING.
PubMed=20577214; DOI=10.1038/nature09128;
Alvarez S.E., Harikumar K.B., Hait N.C., Allegood J., Strub G.M.,
Kim E.Y., Maceyka M., Jiang H., Luo C., Kordula T., Milstien S.,
Spiegel S.;
"Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin
ligase TRAF2.";
Nature 465:1084-1088(2010).
[57]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[58]
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).
[59]
IDENTIFICATION IN APOPTOTIC COMPLEX I, AND INTERACTION WITH UXT.
PubMed=21307340; DOI=10.1091/mbc.E10-10-0827;
Huang Y., Chen L., Zhou Y., Liu H., Yang J., Liu Z., Wang C.;
"UXT-V1 protects cells against TNF-induced apoptosis through
modulating complex II formation.";
Mol. Biol. Cell 22:1389-1397(2011).
[60]
INTERACTION WITH CARD14.
PubMed=21302310; DOI=10.1002/jcp.22667;
Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P.,
Stilo R.;
"Alternative splicing of CARMA2/CARD14 transcripts generates protein
variants with differential effect on NF-kappaB activation and
endoplasmic reticulum stress-induced cell death.";
J. Cell. Physiol. 226:3121-3131(2011).
[61]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT THR-7; SER-11 AND THR-22, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[62]
FUNCTION IN IKBKE UBIQUITINATION.
PubMed=23453969; DOI=10.1016/j.celrep.2013.01.031;
Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.;
"IKKepsilon-mediated tumorigenesis requires K63-linked
polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase
complex.";
Cell Rep. 3:724-733(2013).
[63]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; THR-7 AND SER-11, 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).
[64]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 310-501 IN COMPLEX WITH
TNFRSF1B.
PubMed=10206649; DOI=10.1038/19110;
Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.;
"Structural basis for self-association and receptor recognition of
human TRAF2.";
Nature 398:533-538(1999).
[65]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 334-501 IN COMPLEX WITH EBV
BNFL1, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 315-501 IN COMPLEX
WITH TNFRSF5, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 334-501 IN
COMPLEX WITH TNFRSF4, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF
334-501 IN COMPLEX WITH TNFRSF9.
PubMed=10411888; DOI=10.1073/pnas.96.15.8408;
McWhirter S.M., Pullen S.S., Holton J.M., Crute J.J., Kehry M.R.,
Alber T.;
"Crystallographic analysis of CD40 recognition and signaling by human
TRAF2.";
Proc. Natl. Acad. Sci. U.S.A. 96:8408-8413(1999).
[66]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 331-501 IN COMPLEX WITH
TRADD.
PubMed=10892748; DOI=10.1016/S0092-8674(00)80889-2;
Park Y.C., Ye H., Hsia C., Segal D., Rich R.L., Liou H.C.,
Myszka D.G., Wu H.;
"A novel mechanism of TRAF signaling revealed by structural and
functional analyses of the TRADD-TRAF2 interaction.";
Cell 101:777-787(2000).
[67]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-133, FUNCTION, AND SUBUNIT.
PubMed=19810754; DOI=10.1021/bi901462e;
Yin Q., Lamothe B., Darnay B.G., Wu H.;
"Structural basis for the lack of E2 interaction in the RING domain of
TRAF2.";
Biochemistry 48:10558-10567(2009).
[68]
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 266-330 IN COMPLEXES WITH
TRAF1 AND BIRC3, FUNCTION, SUBUNIT, COILED-COIL DOMAIN, AND
MUTAGENESIS OF ILE-285; VAL-288 AND GLU-292.
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).
-!- FUNCTION: Regulates activation of NF-kappa-B and JNK and plays a
central role in the regulation of cell survival and apoptosis.
Required for normal antibody isotype switching from IgM to IgG.
Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-
linked ubiquitination of target proteins, such as BIRC3, RIPK1 and
TICAM1. Is an essential constituent of several E3 ubiquitin-
protein ligase complexes, where it promotes the ubiquitination of
target proteins by bringing them into contact with other E3
ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by
inhibiting their autoubiquitination and subsequent degradation;
this does not depend on the TRAF2 RING-type zinc finger domain.
Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR.
In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.
{ECO:0000269|PubMed:10346818, ECO:0000269|PubMed:11784851,
ECO:0000269|PubMed:11907583, ECO:0000269|PubMed:12917689,
ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15383523,
ECO:0000269|PubMed:18981220, ECO:0000269|PubMed:19150425,
ECO:0000269|PubMed:19506082, ECO:0000269|PubMed:19810754,
ECO:0000269|PubMed:19918265, ECO:0000269|PubMed:19937093,
ECO:0000269|PubMed:20047764, ECO:0000269|PubMed:20064526,
ECO:0000269|PubMed:20385093, ECO:0000269|PubMed:20577214,
ECO:0000269|PubMed:23453969}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- ENZYME REGULATION: Has very low E3 ubiquitin ligase activity in
the absence of sphingosine-1-phosphate. E3 ubiquitin ligase
activity is strongly activated by cytoplasmic sphingosine-1-
phosphate. {ECO:0000269|PubMed:20577214}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homotrimer (PubMed:8069916). Heterotrimer with TRAF1
(PubMed:8069916). Heterotrimer with TRAF3 (via TRAF domain)
(PubMed:15383523, PubMed:20447407). The domain containing the
RING-type and the first TRAF-type zinc finger can also form
homodimers (in vitro) (PubMed:19810754). Interacts with
TNFRSF1B/TNFR2 (PubMed:7639698, PubMed:8069916, PubMed:10206649).
Interacts with TNFRSF5/CD40 (PubMed:9718306). Interacts with
TNFRSF4, TNFRSF7/CD27, TNFRSF8/CD30, TNFRSF9/CD137,
TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR,
TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT, EDAR
and IL15RA (PubMed:8627180, PubMed:9153189, PubMed:9692890,
PubMed:9488716, PubMed:9774460, PubMed:9607925, PubMed:9418902,
PubMed:10463949, PubMed:10037686, PubMed:10514511,
PubMed:10809768, PubMed:10880535, PubMed:11035039,
PubMed:10411888). Stimulation of TNF-alpha receptor TNFRSF1A leads
to the formation of two distinct signaling complexes. Plasma
membrane-bound complex I is composed of TNFRSF1A, TRADD, RIPK1,
TRAF2 and BIRC2/c-IAP1 or BIRC3 which interacts with CHUCK/IKK-
alpha, IKBKB/IKK-beta and IKBKG/IKK-gamma promoting cell survival
(PubMed:21307340, PubMed:18981220). Subsequently, TRADD, RIPK1 and
TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II
with FADD and caspase CASP8 promoting cell apoptosis
(PubMed:21307340). Interacts with TRADD (PubMed:10892748).
Identified in a complex with TNFRSF1A, RIPK1 and IKBKB/IKK-beta
(PubMed:18981220). Interacts with RIPK2 (PubMed:9705938).
Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3
molecule interacts with a heterotrimer formed by TRAF1 and TRAF2,
or a TRAF2 homotrimer (PubMed:11907583, PubMed:19506082,
PubMed:20447407, PubMed:20385093). Identified in a complex
composed of TRAF2, TRAF3, BIRC2 and BIRC3 (By similarity).
Interacts with BIRC2; the interaction promotes BIRC2 stability
(PubMed:19506082). Interaction with BIRC2 and/or BIRC3 is
essential for ubiquitination of IKBKE, degradation of NFKBIA and
activation of NF-kappa-B (By similarity). Within complex I,
phosphorylated TRAF2 interacts (via 'Lys-63'-linked polyubiquitin
chains) with CHUCK/IKK-alpha, IKBKB/IKK-beta, IKBKG/IKK-gamma
TAB2, TAB3 and TAK1 in response to TNF-alpha stimulation
(PubMed:19150425). Within complex I, interacts with UXT isoform 1
(via TPQE motif); the interaction prevents the recruitment of FADD
and CASP8/caspase 8 to complex I (PubMed:21307340). Forms a
complex composed of TNFRSF8/CD30 or TNFRSF1B/TNFR2, and TRAF1,
TRAF2 and E3 ligase TRAIP (PubMed:9104814). Within the complex,
interacts with TRAIP; the interaction inhibits TRAF2-mediated NF-
kappa B activation (PubMed:9104814). Component of a complex
composed of TANK and TBK1 (PubMed:10581243). Interacts with
TRPC4AP (By similarity). Interacts with MAP3K1/MEKK1, MAP3K5/ASK1
and MAP3K11/MLK3 in response to TNF-alpha stimulation; the
interaction leads to JNK activation (PubMed:10346818,
PubMed:19918265, PubMed:9774977). Component of a complex composed
of MAP3K14/NIK BIRC3 and TRAF3; the interaction leads to BIRC2/3-
mediated ubiquitination of TRAF3 upon CD40 engagement in a TRAF2-
dependent manner (By similarity). Interacts with MAP3K14/NIK in
response to TNF-alpha stimulation; the interaction leads to NF-
kappa B activation (PubMed:9020361). Interacts with PEG3; the
interaction may promote TRAF2-mediated NF-kappa B activation (By
similarity). Interacts with HIVEP3; the interaction may inhibit
TNF-alpha-TRAF2-mediated NF-kappa B and JNK activation (By
similarity). Interacts with TANK/ITRAF; the interaction prevents
interaction between TNFRSF1B/TNFR2 and TRAF2 (PubMed:8710854).
Interacts with deubiquitinating enzyme CYLD; the interaction
results in the deubiquitination and inactivation of TRAF2
(PubMed:12917691). Interacts with SIAH2; the interaction leads to
TRAF2 ubiquitination and degradation (PubMed:12411493). Interacts
with E2 conjugating enzyme UBE2N/Ubc13, E3 ligase ITCH and RNF11
in response to TNF-alpha stimulation (By similarity). Interacts
with ubiquitin-editing enzyme TNFAIP3/A20 in response to TNF-alpha
stimulation; the interaction promotes TRAF2 dissociation from
UBE2N/Ubc13, ITCH, RNF11 and TAX1BP1 and prevents prolonged TRAF-2
ubiquitination (By similarity). Interacts with TAX1BP1 in response
to TNF-alpha stimulation; the interaction promotes TRAF2
dissociation from UBE2N/Ubc13 and TNFAIP3/A20, and prevents
prolonged TRAF-2 ubiquitination (By similarity). Interacts (via C-
terminus) with EIF2AK2/PKR (via the kinase catalytic domain)
(PubMed:15121867). Interacts with deubiquitinating enzyme USP48
(PubMed:16214042). Interacts with PTPN2; probably involved in TNF-
mediated signaling (PubMed:15696169). Interacts with Toll-like
receptor TLR4/3 adapter TICAM1/TRIF; the interaction may promotes
TICAM1 ubiquitination (PubMed:20047764). Interacts with
kinase/endoribonuclease ERN1/IRE1 and DAB2IP in response to ER
stress; the interaction requires DAB2IP (By similarity). Interacts
with ERN1/IRE1 and TAOK3 in response to ER stress; the interaction
may promote TRAF2 phosphorylation (PubMed:11278723). Interacts
(via zinc fingers) with DAB2IP (via C-terminus PER domain)in
response to TNF-alpha stimulation (PubMed:15310755,
PubMed:17389591). Interacts with CASP8AP2/FLASH (By similarity).
Interacts with NFATC2IP; the interaction may repress IL-4
production in T cells (By similarity). Interacts with kinase CDK9
(PubMed:9827693). Interacts with sphingosine kinase 1 SPHK1
(PubMed:20577214). Interacts with kinase TNIK (PubMed:10521462).
Interacts with TRAFD1 (By similarity). Interacts with DNA
phosphodiesterase TDP2 (PubMed:10764746). Interacts with MAVS/IPS1
(PubMed:16153868). Interacts with CARD14 (PubMed:21302310).
Interacts with Epstein-Barr virus LMP1/BNFL1 (PubMed:10411888).
{ECO:0000250|UniProtKB:P39429, ECO:0000269|PubMed:10037686,
ECO:0000269|PubMed:10206649, ECO:0000269|PubMed:10346818,
ECO:0000269|PubMed:10411888, ECO:0000269|PubMed:10463949,
ECO:0000269|PubMed:10514511, ECO:0000269|PubMed:10521462,
ECO:0000269|PubMed:10581243, ECO:0000269|PubMed:10764746,
ECO:0000269|PubMed:10809768, ECO:0000269|PubMed:10880535,
ECO:0000269|PubMed:10892748, ECO:0000269|PubMed:11035039,
ECO:0000269|PubMed:11278723, ECO:0000269|PubMed:11907583,
ECO:0000269|PubMed:12411493, ECO:0000269|PubMed:12917691,
ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15310755,
ECO:0000269|PubMed:15383523, ECO:0000269|PubMed:15696169,
ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:16214042,
ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:18981220,
ECO:0000269|PubMed:19150425, ECO:0000269|PubMed:19506082,
ECO:0000269|PubMed:19810754, ECO:0000269|PubMed:19918265,
ECO:0000269|PubMed:20047764, ECO:0000269|PubMed:20385093,
ECO:0000269|PubMed:20447407, ECO:0000269|PubMed:20577214,
ECO:0000269|PubMed:21302310, ECO:0000269|PubMed:21307340,
ECO:0000269|PubMed:7639698, ECO:0000269|PubMed:8069916,
ECO:0000269|PubMed:8627180, ECO:0000269|PubMed:8710854,
ECO:0000269|PubMed:9020361, ECO:0000269|PubMed:9104814,
ECO:0000269|PubMed:9153189, ECO:0000269|PubMed:9418902,
ECO:0000269|PubMed:9488716, ECO:0000269|PubMed:9607925,
ECO:0000269|PubMed:9692890, ECO:0000269|PubMed:9705938,
ECO:0000269|PubMed:9718306, ECO:0000269|PubMed:9774460,
ECO:0000269|PubMed:9774977, ECO:0000269|PubMed:9827693}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-355744, EBI-355744;
B2R8Y4:-; NbExp=3; IntAct=EBI-355744, EBI-10175581;
G2XKQ0:-; NbExp=3; IntAct=EBI-355744, EBI-10175576;
P88961:- (xeno); NbExp=3; IntAct=EBI-355744, EBI-7907665;
Q9NRN7:AASDHPPT; NbExp=6; IntAct=EBI-355744, EBI-740884;
Q08117:AES; NbExp=3; IntAct=EBI-355744, EBI-717810;
Q9UHB7:AFF4; NbExp=3; IntAct=EBI-355744, EBI-395282;
Q9UHB7-2:AFF4; NbExp=3; IntAct=EBI-355744, EBI-10261324;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-355744, EBI-10187270;
Q96IX9:ANKRD36BP1; NbExp=6; IntAct=EBI-355744, EBI-744859;
Q9UKG1:APPL1; NbExp=2; IntAct=EBI-355744, EBI-741243;
P29972:AQP1; NbExp=3; IntAct=EBI-355744, EBI-745213;
Q8N5N6:ARSJ; NbExp=3; IntAct=EBI-355744, EBI-10266832;
Q8N9N2:ASCC1; NbExp=3; IntAct=EBI-355744, EBI-10268317;
P54253:ATXN1; NbExp=7; IntAct=EBI-355744, EBI-930964;
Q8TBE0:BAHD1; NbExp=3; IntAct=EBI-355744, EBI-742750;
Q8N9N5:BANP; NbExp=4; IntAct=EBI-355744, EBI-744695;
O95999:BCL10; NbExp=8; IntAct=EBI-355744, EBI-958922;
Q9BXY8:BEX2; NbExp=5; IntAct=EBI-355744, EBI-745073;
Q13490:BIRC2; NbExp=14; IntAct=EBI-355744, EBI-514538;
Q13489:BIRC3; NbExp=7; IntAct=EBI-355744, EBI-517709;
Q9NVL8:C14orf105; NbExp=5; IntAct=EBI-355744, EBI-10238351;
Q86X59:C17orf82; NbExp=5; IntAct=EBI-355744, EBI-8465536;
O75808:CAPN15; NbExp=4; IntAct=EBI-355744, EBI-6149008;
O08736:Casp12 (xeno); NbExp=6; IntAct=EBI-355744, EBI-6140033;
Q8NEC5:CATSPER1; NbExp=3; IntAct=EBI-355744, EBI-744545;
Q9HC52:CBX8; NbExp=5; IntAct=EBI-355744, EBI-712912;
Q8TD31-3:CCHCR1; NbExp=5; IntAct=EBI-355744, EBI-10175300;
F6RF56:CCNJL; NbExp=3; IntAct=EBI-355744, EBI-10177725;
P25942:CD40; NbExp=9; IntAct=EBI-355744, EBI-525714;
Q86Y33:CDC20B; NbExp=3; IntAct=EBI-355744, EBI-10260504;
Q99618:CDCA3; NbExp=6; IntAct=EBI-355744, EBI-739534;
P46527:CDKN1B; NbExp=5; IntAct=EBI-355744, EBI-519280;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-355744, EBI-10181988;
Q02930-3:CREB5; NbExp=5; IntAct=EBI-355744, EBI-10192698;
Q6BCY4:CYB5R2; NbExp=3; IntAct=EBI-355744, EBI-744761;
O60941:DTNB; NbExp=4; IntAct=EBI-355744, EBI-740402;
Q8WWZ3:EDARADD; NbExp=5; IntAct=EBI-355744, EBI-2949647;
Q12805:EFEMP1; NbExp=8; IntAct=EBI-355744, EBI-536772;
Q5JVL4:EFHC1; NbExp=5; IntAct=EBI-355744, EBI-743105;
P00533:EGFR; NbExp=3; IntAct=EBI-355744, EBI-297353;
Q9H0I2:ENKD1; NbExp=6; IntAct=EBI-355744, EBI-744099;
O75460:ERN1; NbExp=3; IntAct=EBI-355744, EBI-371750;
Q01844:EWSR1; NbExp=3; IntAct=EBI-355744, EBI-739737;
Q8N2X6:EXOC3-AS1; NbExp=8; IntAct=EBI-355744, EBI-749333;
O95990-4:FAM107A; NbExp=4; IntAct=EBI-355744, EBI-11977223;
Q96EK7:FAM120B; NbExp=3; IntAct=EBI-355744, EBI-739883;
Q3B820:FAM161A; NbExp=4; IntAct=EBI-355744, EBI-719941;
Q9GZU8:FAM192A; NbExp=3; IntAct=EBI-355744, EBI-2371956;
Q86YD7:FAM90A1; NbExp=5; IntAct=EBI-355744, EBI-6658203;
Q9NVF7:FBXO28; NbExp=5; IntAct=EBI-355744, EBI-740282;
Q9BRP7:FDXACB1; NbExp=5; IntAct=EBI-355744, EBI-10297077;
Q53EP0-3:FNDC3B; NbExp=3; IntAct=EBI-355744, EBI-10242151;
Q06547:GABPB1; NbExp=6; IntAct=EBI-355744, EBI-618165;
Q9H8Y8:GORASP2; NbExp=6; IntAct=EBI-355744, EBI-739467;
Q92917:GPKOW; NbExp=5; IntAct=EBI-355744, EBI-746309;
Q2KHT4:GSG1; NbExp=3; IntAct=EBI-355744, EBI-10239244;
P09211:GSTP1; NbExp=5; IntAct=EBI-355744, EBI-353467;
Q5T8I9:HENMT1; NbExp=3; IntAct=EBI-355744, EBI-9675710;
P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-355744, EBI-3957603;
Q8NA54:IQUB; NbExp=3; IntAct=EBI-355744, EBI-10220600;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-355744, EBI-2125614;
P57682:KLF3; NbExp=5; IntAct=EBI-355744, EBI-8472267;
Q8TBB1:LNX1; NbExp=5; IntAct=EBI-355744, EBI-739832;
Q13233:MAP3K1; NbExp=2; IntAct=EBI-355744, EBI-49776;
Q62925:Map3k1 (xeno); NbExp=2; IntAct=EBI-355744, EBI-636664;
Q99558:MAP3K14; NbExp=7; IntAct=EBI-355744, EBI-358011;
Q99683:MAP3K5; NbExp=4; IntAct=EBI-355744, EBI-476263;
Q7Z434:MAVS; NbExp=3; IntAct=EBI-355744, EBI-995373;
Q8N6R0:METTL13; NbExp=4; IntAct=EBI-355744, EBI-1053295;
Q8IVT2:MISP; NbExp=4; IntAct=EBI-355744, EBI-2555085;
Q6PF18:MORN3; NbExp=5; IntAct=EBI-355744, EBI-9675802;
Q8N6N6:NATD1; NbExp=3; IntAct=EBI-355744, EBI-8656665;
O76041:NEBL; NbExp=5; IntAct=EBI-355744, EBI-2880203;
Q16649:NFIL3; NbExp=3; IntAct=EBI-355744, EBI-3951858;
P07174:Ngfr (xeno); NbExp=3; IntAct=EBI-355744, EBI-1038810;
Q9GZQ4:NMUR2; NbExp=3; IntAct=EBI-355744, EBI-10303844;
Q16656:NRF1; NbExp=3; IntAct=EBI-355744, EBI-2547810;
P89055:NSP1 (xeno); NbExp=3; IntAct=EBI-355744, EBI-9522973;
Q9BRJ7:NUDT16L1; NbExp=5; IntAct=EBI-355744, EBI-2949792;
Q86SE9:PCGF5; NbExp=3; IntAct=EBI-355744, EBI-2827999;
Q96JS3:PGBD1; NbExp=6; IntAct=EBI-355744, EBI-10290053;
Q13526:PIN1; NbExp=6; IntAct=EBI-355744, EBI-714158;
O60437:PPL; NbExp=7; IntAct=EBI-355744, EBI-368321;
Q6NYC8:PPP1R18; NbExp=5; IntAct=EBI-355744, EBI-2557469;
O43741:PRKAB2; NbExp=8; IntAct=EBI-355744, EBI-1053424;
Q9H875:PRKRIP1; NbExp=3; IntAct=EBI-355744, EBI-744488;
P54725:RAD23A; NbExp=6; IntAct=EBI-355744, EBI-746453;
Q8WWW0:RASSF5; NbExp=3; IntAct=EBI-355744, EBI-367390;
Q96IZ5:RBM41; NbExp=5; IntAct=EBI-355744, EBI-740773;
Q9P2K3:RCOR3; NbExp=4; IntAct=EBI-355744, EBI-743428;
P48380:RFX3; NbExp=3; IntAct=EBI-355744, EBI-742557;
Q13546:RIPK1; NbExp=6; IntAct=EBI-355744, EBI-358507;
Q0D2K3:RIPPLY1; NbExp=5; IntAct=EBI-355744, EBI-10226430;
P57055:RIPPLY3; NbExp=4; IntAct=EBI-355744, EBI-12092053;
Q9NTX7:RNF146; NbExp=3; IntAct=EBI-355744, EBI-722397;
Q9H788:SH2D4A; NbExp=5; IntAct=EBI-355744, EBI-747035;
Q9H0W8:SMG9; NbExp=5; IntAct=EBI-355744, EBI-2872322;
Q9BV90:SNRNP25; NbExp=3; IntAct=EBI-355744, EBI-9675976;
Q9NZD8:SPG21; NbExp=6; IntAct=EBI-355744, EBI-742688;
Q9BSW7:SYT17; NbExp=5; IntAct=EBI-355744, EBI-745392;
Q92844:TANK; NbExp=4; IntAct=EBI-355744, EBI-356349;
Q9H2K8:TAOK3; NbExp=2; IntAct=EBI-355744, EBI-1384100;
Q9UHD2:TBK1; NbExp=3; IntAct=EBI-355744, EBI-356402;
Q15560:TCEA2; NbExp=6; IntAct=EBI-355744, EBI-710310;
Q9BXF9:TEKT3; NbExp=5; IntAct=EBI-355744, EBI-8644516;
Q9BT49:THAP7; NbExp=8; IntAct=EBI-355744, EBI-741350;
Q96CV8:THOP1; NbExp=3; IntAct=EBI-355744, EBI-6137619;
Q96CG3:TIFA; NbExp=7; IntAct=EBI-355744, EBI-740711;
P21580:TNFAIP3; NbExp=5; IntAct=EBI-355744, EBI-527670;
Q9NP84:TNFRSF12A; NbExp=3; IntAct=EBI-355744, EBI-2851995;
Q92956:TNFRSF14; NbExp=4; IntAct=EBI-355760, EBI-1056653;
P19438:TNFRSF1A; NbExp=4; IntAct=EBI-355744, EBI-299451;
P20333:TNFRSF1B; NbExp=3; IntAct=EBI-355744, EBI-358983;
Q9UKE5:TNIK; NbExp=2; IntAct=EBI-355744, EBI-1051794;
Q15628:TRADD; NbExp=8; IntAct=EBI-355744, EBI-359215;
Q13077:TRAF1; NbExp=6; IntAct=EBI-355744, EBI-359224;
P70191:Traf5 (xeno); NbExp=2; IntAct=EBI-355744, EBI-523899;
Q9Y4K3:TRAF6; NbExp=12; IntAct=EBI-355744, EBI-359276;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-355744, EBI-5235829;
Q12815:TROAP; NbExp=3; IntAct=EBI-355744, EBI-2349743;
Q63HK5:TSHZ3; NbExp=3; IntAct=EBI-355744, EBI-9053916;
Q9Y5U2:TSSC4; NbExp=3; IntAct=EBI-355744, EBI-717229;
Q5T124:UBXN11; NbExp=5; IntAct=EBI-355744, EBI-746004;
P22415:USF1; NbExp=3; IntAct=EBI-355744, EBI-1054489;
O75604:USP2; NbExp=6; IntAct=EBI-355744, EBI-743272;
Q70EK8:USP53; NbExp=3; IntAct=EBI-355744, EBI-742050;
Q5GFL6:VWA2; NbExp=3; IntAct=EBI-355744, EBI-10243723;
P07947:YES1; NbExp=3; IntAct=EBI-355744, EBI-515331;
Q05516:ZBTB16; NbExp=4; IntAct=EBI-355744, EBI-711925;
P24278:ZBTB25; NbExp=4; IntAct=EBI-355744, EBI-739899;
Q53FD0:ZC2HC1C; NbExp=3; IntAct=EBI-355744, EBI-740767;
Q6FIF0:ZFAND6; NbExp=6; IntAct=EBI-355744, EBI-724630;
Q96NC0:ZMAT2; NbExp=5; IntAct=EBI-355744, EBI-2682299;
Q86VK4:ZNF410; NbExp=3; IntAct=EBI-355744, EBI-720304;
Q86VK4-3:ZNF410; NbExp=4; IntAct=EBI-355744, EBI-11741890;
Q96MN9:ZNF488; NbExp=3; IntAct=EBI-355744, EBI-948288;
Q32MK9:ZNF509; NbExp=3; IntAct=EBI-355744, EBI-10239929;
Q6NX49:ZNF544; NbExp=3; IntAct=EBI-355744, EBI-2841978;
Q7Z3I7:ZNF572; NbExp=4; IntAct=EBI-355744, EBI-10172590;
Q8N720:ZNF655; NbExp=3; IntAct=EBI-355744, EBI-625509;
Q6ZS27-3:ZNF662; NbExp=3; IntAct=EBI-355744, EBI-10255155;
Q3MJ62:ZSCAN23; NbExp=4; IntAct=EBI-355744, EBI-5667532;
I3L3J2:ZSCAN32; NbExp=3; IntAct=EBI-355744, EBI-10178206;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15383523,
ECO:0000269|PubMed:19150425}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q12933-1; Sequence=Displayed;
Name=2;
IsoId=Q12933-2; Sequence=VSP_007401;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q12933-3; Sequence=VSP_039687;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q12933-4; Sequence=VSP_039688;
Note=No experimental confirmation available.;
-!- DOMAIN: The coiled coil domain mediates homo- and hetero-
oligomerization. {ECO:0000269|PubMed:20064526}.
-!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic
domains. {ECO:0000269|PubMed:20064526}.
-!- DOMAIN: The RING-type zinc finger domain is essential for E3
ubiquitin-protein ligase activity. It is not essential for the
stabilization of BIRC2, or for the ubiquitination of RIPK1 in
response to TNFR1 signaling. {ECO:0000269|PubMed:20064526}.
-!- PTM: Phosphorylated at several serine residues within the first
128 amino acid residues. Phosphorylated at Thr-117 in response to
signaling via TNF and TNFRSF1A. Phosphorylation at Thr-117 is
required for 'Lys-63'-linked polyubiquitination, but not for 'Lys-
48'-linked polyubiquitination. Phosphorylation at Thr-117 is
important for interaction with IKKA and IKKB, activation of IKK
and subsequent activation of NF-kappa-B.
{ECO:0000269|PubMed:19150425}.
-!- PTM: Undergoes both 'Lys-48'-linked and 'Lys-63'-linked
polyubiquitination. Polyubiquitinated via 'Lys-63'-linked
ubiquitin in response to TNF signaling; this requires prior
phosphorylation at Thr-117. 'Lys-63'-linked polyubiquitination
promotes TRAF2-mediated activation of NF-kappa-B. Can be
polyubiquitinated at several Lys residues via 'Lys-48'-linked
ubiquitin chains in response to TNF signaling, leading to
proteasomal degradation. Autoubiquitinated, leading to its
subsequent proteasomal degradation. Polyubiquitinated by BIRC2 and
SIAH2, leading to its subsequent proteasomal degradation.
Deubiquitinated by CYLD, a protease that specifically cleaves
'Lys-63'-linked polyubiquitin chains.
{ECO:0000269|PubMed:19150425}.
-!- SIMILARITY: Belongs to the TNF receptor-associated factor family.
A subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/traf2/";
-----------------------------------------------------------------------
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EMBL; U12597; AAA87706.1; -; mRNA.
EMBL; AK054686; BAB70792.1; -; mRNA.
EMBL; AK289722; BAF82411.1; -; mRNA.
EMBL; AK298370; BAG60609.1; -; mRNA.
EMBL; BX538160; CAD98040.1; -; mRNA.
EMBL; AY623660; AAT27320.1; -; Genomic_DNA.
EMBL; AL355987; CAI12703.1; -; Genomic_DNA.
EMBL; AL449425; CAI12703.1; JOINED; Genomic_DNA.
EMBL; AL449425; CAI15106.1; -; Genomic_DNA.
EMBL; AL355987; CAI15106.1; JOINED; Genomic_DNA.
EMBL; CH471090; EAW88299.1; -; Genomic_DNA.
EMBL; BC032410; AAH32410.1; -; mRNA.
EMBL; BC033810; AAH33810.1; -; mRNA.
EMBL; BC043492; AAH43492.1; -; mRNA.
EMBL; BC064662; AAH64662.1; -; mRNA.
CCDS; CCDS7013.1; -. [Q12933-1]
PIR; S56163; S56163.
RefSeq; NP_066961.2; NM_021138.3. [Q12933-1]
RefSeq; XP_011517276.1; XM_011518974.2. [Q12933-1]
RefSeq; XP_011517277.1; XM_011518975.2. [Q12933-1]
RefSeq; XP_011517278.1; XM_011518976.2. [Q12933-1]
RefSeq; XP_011517279.1; XM_011518977.2. [Q12933-1]
RefSeq; XP_011517280.1; XM_011518978.2. [Q12933-1]
RefSeq; XP_016870584.1; XM_017015095.1. [Q12933-1]
UniGene; Hs.522506; -.
PDB; 1CA4; X-ray; 2.20 A; A/B/C/D/E/F=334-501.
PDB; 1CA9; X-ray; 2.30 A; A/B/C/D/E/F=310-501.
PDB; 1CZY; X-ray; 2.00 A; A/B/C=334-501.
PDB; 1CZZ; X-ray; 2.70 A; A/B/C=315-501.
PDB; 1D00; X-ray; 2.00 A; A/B/C/D/E/F/G/H=334-501.
PDB; 1D01; X-ray; 2.00 A; A/B/C/D/E/F=334-501.
PDB; 1D0A; X-ray; 2.00 A; A/B/C/D/E/F=334-501.
PDB; 1D0J; X-ray; 2.50 A; A/B/C/D/E/F=334-501.
PDB; 1F3V; X-ray; 2.00 A; B=331-501.
PDB; 1QSC; X-ray; 2.40 A; A/B/C=311-501.
PDB; 3KNV; X-ray; 1.90 A; A=1-133.
PDB; 3M06; X-ray; 2.67 A; A/B/C/D/E/F=266-329.
PDB; 3M0A; X-ray; 2.61 A; A/B/C=266-329.
PDB; 3M0D; X-ray; 2.80 A; A/B=266-329.
PDBsum; 1CA4; -.
PDBsum; 1CA9; -.
PDBsum; 1CZY; -.
PDBsum; 1CZZ; -.
PDBsum; 1D00; -.
PDBsum; 1D01; -.
PDBsum; 1D0A; -.
PDBsum; 1D0J; -.
PDBsum; 1F3V; -.
PDBsum; 1QSC; -.
PDBsum; 3KNV; -.
PDBsum; 3M06; -.
PDBsum; 3M0A; -.
PDBsum; 3M0D; -.
ProteinModelPortal; Q12933; -.
SMR; Q12933; -.
BioGrid; 113038; 355.
CORUM; Q12933; -.
DIP; DIP-6223N; -.
ELM; Q12933; -.
IntAct; Q12933; 349.
MINT; MINT-107429; -.
STRING; 9606.ENSP00000247668; -.
iPTMnet; Q12933; -.
PhosphoSitePlus; Q12933; -.
BioMuta; TRAF2; -.
DMDM; 23503103; -.
EPD; Q12933; -.
MaxQB; Q12933; -.
PaxDb; Q12933; -.
PeptideAtlas; Q12933; -.
PRIDE; Q12933; -.
DNASU; 7186; -.
Ensembl; ENST00000247668; ENSP00000247668; ENSG00000127191. [Q12933-1]
GeneID; 7186; -.
KEGG; hsa:7186; -.
UCSC; uc004cjv.4; human. [Q12933-1]
CTD; 7186; -.
DisGeNET; 7186; -.
EuPathDB; HostDB:ENSG00000127191.17; -.
GeneCards; TRAF2; -.
H-InvDB; HIX0169360; -.
HGNC; HGNC:12032; TRAF2.
HPA; CAB004603; -.
HPA; HPA009972; -.
HPA; HPA010634; -.
MIM; 601895; gene.
neXtProt; NX_Q12933; -.
OpenTargets; ENSG00000127191; -.
PharmGKB; PA164742666; -.
eggNOG; ENOG410ISDM; Eukaryota.
eggNOG; ENOG4111M70; LUCA.
GeneTree; ENSGT00550000074359; -.
HOGENOM; HOG000231558; -.
HOVERGEN; HBG058222; -.
InParanoid; Q12933; -.
KO; K03173; -.
OMA; SACRNVL; -.
OrthoDB; EOG091G0GHD; -.
PhylomeDB; Q12933; -.
TreeFam; TF321154; -.
Reactome; R-HSA-140534; Ligand-dependent caspase activation.
Reactome; R-HSA-3371378; Regulation by c-FLIP.
Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-HSA-5218900; CASP8 activity is inhibited.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-69416; Dimerization of procaspase-8.
Reactome; R-HSA-75893; TNF signaling.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
SignaLink; Q12933; -.
SIGNOR; Q12933; -.
UniPathway; UPA00143; -.
ChiTaRS; TRAF2; human.
EvolutionaryTrace; Q12933; -.
GeneWiki; TRAF2; -.
GenomeRNAi; 7186; -.
PRO; PR:Q12933; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000127191; -.
CleanEx; HS_TRAF2; -.
ExpressionAtlas; Q12933; baseline and differential.
Genevisible; Q12933; HS.
GO; GO:1990597; C:AIP1-IRE1 complex; IEA:Ensembl.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0097057; C:TRAF2-GSTP1 complex; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IPI:ParkinsonsUK-UCL.
GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
GO; GO:0005174; F:CD40 receptor binding; ISS:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004871; F:signal transducer activity; NAS:ProtInc.
GO; GO:0046625; F:sphingolipid binding; IDA:UniProtKB.
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:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IMP:UniProtKB.
GO; GO:0043623; P:cellular protein complex assembly; ISS:BHF-UCL.
GO; GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl.
GO; GO:0071550; P:death-inducing signaling complex assembly; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; TAS:ParkinsonsUK-UCL.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IEA:Ensembl.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0090073; P:positive regulation of protein homodimerization activity; IMP:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0050870; P:positive regulation of T cell activation; IC:UniProtKB.
GO; GO:0002726; P:positive regulation of T cell cytokine production; IMP:UniProtKB.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
GO; GO:0097300; P:programmed necrotic cell death; IEA:Ensembl.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0070207; P:protein homotrimerization; IPI:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0060544; P:regulation of necroptotic process; TAS:Reactome.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0034976; P:response to endoplasmic reticulum stress; NAS:ParkinsonsUK-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
Gene3D; 2.60.210.10; -; 1.
Gene3D; 3.30.40.10; -; 4.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR012227; TNF_rcpt--assoc_TRAF.
InterPro; IPR008974; TRAF-like.
InterPro; IPR027133; TRAF2.
InterPro; IPR032070; TRAF_BIRC3-bd.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
InterPro; IPR001293; Znf_TRAF.
PANTHER; PTHR10131:SF21; PTHR10131:SF21; 1.
Pfam; PF16673; TRAF_BIRC3_bd; 1.
Pfam; PF00097; zf-C3HC4; 1.
Pfam; PF02176; zf-TRAF; 1.
PIRSF; PIRSF015614; TRAF; 1.
SMART; SM00061; MATH; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF49599; SSF49599; 1.
PROSITE; PS50144; MATH; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
PROSITE; PS50145; ZF_TRAF; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Coiled coil; Complete proteome; Cytoplasm; Isopeptide bond;
Lipid-binding; Metal-binding; Phosphoprotein; Reference proteome;
Repeat; Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CHAIN 2 501 TNF receptor-associated factor 2.
/FTId=PRO_0000056399.
DOMAIN 351 496 MATH. {ECO:0000255|PROSITE-
ProRule:PRU00129}.
ZN_FING 34 73 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 124 180 TRAF-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00207}.
ZN_FING 177 233 TRAF-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00207}.
REGION 283 293 Important for interaction with BIRC2 and
BIRC3. {ECO:0000250}.
COILED 299 348 {ECO:0000269|PubMed:20385093}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 7 7 Phosphothreonine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18981220}.
MOD_RES 22 22 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 117 117 Phosphothreonine; by PKC.
{ECO:0000269|PubMed:19150425}.
CROSSLNK 31 31 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19150425}.
VAR_SEQ 53 63 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039687.
VAR_SEQ 122 122 E -> EVKMPACGMVTEAPAVGSRPRSPSSYDLVLHVPLTG
AEACLMSVEEETELLLR (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_007401.
VAR_SEQ 176 200 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_039688.
MUTAGEN 11 11 S->A: Reduces global phosphorylation.
Partial reduction of TNF-dependent
activation of NF-kappa-B and activation
of JNK. {ECO:0000269|PubMed:18981220}.
MUTAGEN 11 11 S->D: Slight increase of TNF-dependent
activation of NF-kappa-B and activation
of JNK. {ECO:0000269|PubMed:18981220}.
MUTAGEN 31 31 K->R: Abolishes 'Lys-63'-linked
polyubiquitination.
MUTAGEN 117 117 T->A: Loss of phosphorylation site.
Abolishes activation of NF-kappa-B.
{ECO:0000269|PubMed:19150425}.
MUTAGEN 285 285 I->A: Strongly reduced interaction with
BIRC3. {ECO:0000269|PubMed:20385093}.
MUTAGEN 288 288 V->A: Strongly reduced interaction with
BIRC3. {ECO:0000269|PubMed:20385093}.
MUTAGEN 292 292 E->A: Strongly reduced interaction with
BIRC3. {ECO:0000269|PubMed:20385093}.
CONFLICT 205 310 Missing (in Ref. 2; BAB70792).
{ECO:0000305}.
CONFLICT 343 365 LEMEASTYDGVFIWKISDFARKR -> RPFQAQCGHRYCSF
CLASILRKL (in Ref. 1; AAA87706).
{ECO:0000305}.
HELIX 21 23 {ECO:0000244|PDB:3KNV}.
HELIX 25 27 {ECO:0000244|PDB:3KNV}.
HELIX 30 32 {ECO:0000244|PDB:3KNV}.
TURN 35 37 {ECO:0000244|PDB:3KNV}.
STRAND 42 46 {ECO:0000244|PDB:3KNV}.
STRAND 52 54 {ECO:0000244|PDB:3KNV}.
HELIX 55 61 {ECO:0000244|PDB:3KNV}.
HELIX 62 64 {ECO:0000244|PDB:3KNV}.
HELIX 70 74 {ECO:0000244|PDB:3KNV}.
TURN 80 83 {ECO:0000244|PDB:3KNV}.
HELIX 87 89 {ECO:0000244|PDB:3KNV}.
HELIX 94 101 {ECO:0000244|PDB:3KNV}.
STRAND 103 106 {ECO:0000244|PDB:3KNV}.
STRAND 115 117 {ECO:0000244|PDB:3KNV}.
HELIX 118 124 {ECO:0000244|PDB:3KNV}.
TURN 125 127 {ECO:0000244|PDB:3KNV}.
HELIX 130 133 {ECO:0000244|PDB:3KNV}.
HELIX 315 318 {ECO:0000244|PDB:1CA9}.
HELIX 335 347 {ECO:0000244|PDB:1CZY}.
STRAND 350 358 {ECO:0000244|PDB:1CZY}.
HELIX 361 369 {ECO:0000244|PDB:1CZY}.
STRAND 375 377 {ECO:0000244|PDB:1D0J}.
STRAND 381 384 {ECO:0000244|PDB:1CZY}.
STRAND 389 395 {ECO:0000244|PDB:1CZY}.
HELIX 400 402 {ECO:0000244|PDB:1CZY}.
TURN 403 405 {ECO:0000244|PDB:1CZY}.
STRAND 406 414 {ECO:0000244|PDB:1CZY}.
HELIX 419 421 {ECO:0000244|PDB:1CZY}.
STRAND 430 434 {ECO:0000244|PDB:1CZY}.
STRAND 443 447 {ECO:0000244|PDB:1CZY}.
HELIX 454 456 {ECO:0000244|PDB:1CZY}.
STRAND 460 463 {ECO:0000244|PDB:1CZY}.
STRAND 467 474 {ECO:0000244|PDB:1CZY}.
HELIX 476 480 {ECO:0000244|PDB:1CZY}.
TURN 482 484 {ECO:0000244|PDB:1CZY}.
STRAND 490 496 {ECO:0000244|PDB:1CZY}.
SEQUENCE 501 AA; 55859 MW; C508BE185B783B20 CRC64;
MAAASVTPPG SLELLQPGFS KTLLGTKLEA KYLCSACRNV LRRPFQAQCG HRYCSFCLAS
ILSSGPQNCA ACVHEGIYEE GISILESSSA FPDNAARREV ESLPAVCPSD GCTWKGTLKE
YESCHEGRCP LMLTECPACK GLVRLGEKER HLEHECPERS LSCRHCRAPC CGADVKAHHE
VCPKFPLTCD GCGKKKIPRE KFQDHVKTCG KCRVPCRFHA IGCLETVEGE KQQEHEVQWL
REHLAMLLSS VLEAKPLLGD QSHAGSELLQ RCESLEKKTA TFENIVCVLN REVERVAMTA
EACSRQHRLD QDKIEALSSK VQQLERSIGL KDLAMADLEQ KVLEMEASTY DGVFIWKISD
FARKRQEAVA GRIPAIFSPA FYTSRYGYKM CLRIYLNGDG TGRGTHLSLF FVVMKGPNDA
LLRWPFNQKV TLMLLDQNNR EHVIDAFRPD VTSSSFQRPV NDMNIASGCP LFCPVSKMEA
KNSYVRDDAI FIKAIVDLTG L


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