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UniProtKB/Swiss-Prot entry Q12933


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRAF2_HUMAN
Primary accession number Q12933
Secondary accession number Q96NT2
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on September 19, 2002 (Sequence version 2)
Annotations were last modified on    April 29, 2008 (Entry version 105)
Name and origin of the protein
Protein name TNF receptor-associated factor 2
Synonym Tumor necrosis factor type 2 receptor-associated protein 3
Gene name
Name: TRAF2
Synonyms: TRAP3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7639698 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Cerebellum;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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 [GENOMIC DNA].
SeattleSNPs program for genomic applications;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, Fetal brain, Kidney, Leukocyte, Stomach, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 201-501, AND INTERACTION WITH TRAF1 AND TNFRSF1B.
DOI=10.1016/0092-8674(94)90532-0; PubMed=8069916 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
INTERACTION WITH TBK1.
TISSUE=Spleen;
DOI=10.1093/emboj/18.23.6694; PubMed=10581243 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
REVIEW.
DOI=10.1016/S0898-6568(01)00160-7; PubMed=11384837 [NCBI, ExPASy, EBI, Israel, Japan]
Wajant H., Henkler F., Scheurich P.;
"The TNF-receptor-associated factor family: scaffold molecules for cytokine receptors, kinases and their regulators.";
Cell. Signal. 13:389-400(2001).
[8]
REVIEW.
DOI=10.1038/sj.onc.1204788; PubMed=11607847 [NCBI, ExPASy, EBI, Israel, Japan]
Bradley J.R., Pober J.S.;
"Tumor necrosis factor receptor-associated factors (TRAFs).";
Oncogene 20:6482-6491(2001).
[9]
INTERACTION WITH TNFRSF8.
DOI=10.1084/jem.183.2.669; PubMed=8627180 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1073/pnas.93.16.8241; PubMed=8710854 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1074/jbc.272.21.13471; PubMed=9153189 [NCBI, ExPASy, EBI, Israel, Japan]
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]
INTERACTION WITH TRIP.
DOI=10.1084/jem.185.7.1275; PubMed=9104814 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1038/385540a0; PubMed=9020361 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1021/bi981067q; PubMed=9718306 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/S0960-9822(07)00352-1; PubMed=9705938 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1002/(SICI)1521-4141(199807)28:07<2208::AID-IMMU2208>3.0.CO;2-L; PubMed=9692890 [NCBI, ExPASy, EBI, Israel, Japan]
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 AND TNFRSF9.
PubMed=9418902 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
INTERACTION WITH TNFRSF4.
DOI=10.1074/jbc.273.10.5808; PubMed=9488716 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
INTERACTION WITH TNFRSF11A.
DOI=10.1074/jbc.273.43.28355; PubMed=9774460 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
INTERACTION WITH TNFRSF9.
DOI=10.1084/jem.187.11.1849; PubMed=9607925 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/S1097-2765(00)80283-X; PubMed=9774977 [NCBI, ExPASy, EBI, Israel, Japan]
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 IL15RA.
PubMed=10463949 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[23]
INTERACTION WITH TNFRSF18.
TISSUE=T-cell;
DOI=10.1074/jbc.274.10.6056; PubMed=10037686 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[24]
INTERACTION WITH TNFRSF16.
DOI=10.1074/jbc.274.42.30202; PubMed=10514511 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[25]
INTERACTION WITH TNIK.
DOI=10.1074/jbc.274.43.30729; PubMed=10521462 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[26]
INTERACTION WITH CDK9.
DOI=10.1002/(SICI)1097-4644(19981215)71:4<467::AID-JCB2>3.3.CO;2-7; PubMed=9827693 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[27]
INTERACTION WITH TNFRSF19.
DOI=10.1074/jbc.275.20.15336; PubMed=10809768 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[28]
INTERACTION WITH TNFRSF13B.
DOI=10.1084/jem.192.1.137; PubMed=10880535 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[29]
INTERACTION WITH MAP4K2.
PubMed=11784851 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[30]
INTERACTION WITH MAP3K1.
PubMed=10346818 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[31]
INTERACTION WITH TTRAP.
DOI=10.1074/jbc.M000531200; PubMed=10764746 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[32]
INTERACTION WITH SIAH2, AND DEGRADATION.
DOI=10.1093/emboj/cdf576; PubMed=12411493 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[33]
INTERACTION WITH CYLD.
DOI=10.1038/nature01802; PubMed=12917691 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[34]
INTERACTION WITH DAB2IP.
DOI=10.1074/jbc.M407617200; PubMed=15310755 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[35]
INTERACTION WITH MAVS.
DOI=10.1016/j.molcel.2005.08.014; PubMed=16153868 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[36]
INTERACTION WITH USP48.
DOI=10.1016/j.cellsig.2005.03.017; PubMed=16214042 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[37]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 310-501 IN COMPLEX WITH TNFRSF1B.
DOI=10.1038/19110; PubMed=10206649 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[38]
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.
DOI=10.1073/pnas.96.15.8408; PubMed=10411888 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[39]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 331-501 IN COMPLEX WITH TRADD.
DOI=10.1016/S0092-8674(00)80889-2; PubMed=10892748 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U12597; AAA87706.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK054686; BAB70792.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY623660; AAT27320.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032410; AAH32410.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033810; AAH33810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC043492; AAH43492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC064662; AAH64662.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S56163; S56163.
RefSeq NP_066961.2; -.
UniGene Hs.522506
3D structure databases
PDB
1CA4; X-ray; 2.20 A; A/B/C/D/E/F=334-501.[ExPASy / RCSB / EBI]
1CA9; X-ray; 2.30 A; A/B/C/D/E/F=310-501.[ExPASy / RCSB / EBI]
1CZY; X-ray; 2.00 A; A/B/C=334-501.[ExPASy / RCSB / EBI]
1CZZ; X-ray; 2.70 A; A/B/C=315-501.[ExPASy / RCSB / EBI]
1D00; X-ray; 2.00 A; A/B/C/D/E/F/G/H=334-501.[ExPASy / RCSB / EBI]
1D01; X-ray; 2.00 A; A/B/C/D/E/F=334-501.[ExPASy / RCSB / EBI]
1D0A; X-ray; 2.00 A; A/B/C/D/E/F=334-501.[ExPASy / RCSB / EBI]
1D0J; X-ray; 2.50 A; A/B/C/D/E/F=334-501.[ExPASy / RCSB / EBI]
1F3V; X-ray; 2.00 A; B=331-501.[ExPASy / RCSB / EBI]
1QSC; X-ray; 2.40 A; A/B/C=311-501.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CA4; -.
1CA9; -.
1CZY; -.
1CZZ; -.
1D00; -.
1D01; -.
1D0A; -.
1D0J; -.
1F3V; -.
1QSC; -.
ModBase Q12933.
Protein-protein interaction databases
DIP DIP:6223N; -.
IntAct Q12933; -.
PTM databases
PhosphoSite Q12933; -.
Enzyme and pathway databases
Reactome REACT_578; Apoptosis.
Organism-specific databases
H-InvDB HIX0008562; -.
HGNC HGNC:12032; TRAF2.
GeneLynx TRAF2; Homo sapiens.
GenAtlas TRAF2.
HPA CAB004603; -.
HPA009972; -.
HPA010634; -.
MIM 601895; gene. [NCBI / EBI]
PharmGKB PA36709; -.
GeneCards Q12933.
Gene expression databases
ArrayExpress Q12933; -.
CleanEx HS_TRAF2; -.
GermOnline ENSG00000127191; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004871; Molecular function: signal transducer activity (non-traceable author statement from ProtInc).
GO:0007250; Biological process: activation of NF-kappaB-inducing kinase activity (inferred from mutant phenotype from UniProtKB).
GO:0032743; Biological process: positive regulation of interleukin-2 production (inferred from mutant phenotype from UniProtKB).
GO:0050870; Biological process: positive regulation of T cell activation (inferred by curator from UniProtKB).
GO:0002726; Biological process: positive regulation of T cell cytokine production (inferred from mutant phenotype from UniProtKB).
GO:0006461; Biological process: protein complex assembly (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002083; MATH.
IPR012227; TNF_recpt_TRAF.
IPR013322; TRAF-type.
IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
IPR001293; Znf_TRAF.
Graphical view of domain structure.
Gene3D G3DSA:2.60.210.10; TRAF-type; 1.
G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
Pfam PF00917; MATH; 1.
PF00097; zf-C3HC4; 1.
PF02176; zf-TRAF; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF015614; TRAF; 1.
SMART SM00061; MATH; 1.
SM00184; RING; 1.
SMART graphical view of domain structure.
PROSITE PS50144; MATH; 1.
PS00518; ZF_RING_1; 1.
PS50089; ZF_RING_2; 1.
PS50145; ZF_TRAF; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q12933.
Genome annotation databases
Ensembl ENSG00000127191; Homo sapiens. [Contig view]
GeneID 7186; -.
KEGG hsa:7186; -.
Other
SOURCE TRAF2; Homo sapiens.
ProtoNet Q12933.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm; Metal-binding; Repeat; Ubl conjugation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   501  501     TNF receptor-associated factor 2. PRO_0000056399
DOMAIN   351   496  146     MATH. 
ZN_FING   34    73  40     RING-type. 
ZN_FING   124   180  57     TRAF-type 1. 
ZN_FING   177   233  57     TRAF-type 2. 
COILED   299   348  50     Potential. 
VAR_SEQ   122   122        E -> EVKMPACGMVTEAPAVGSRPRSPSSYDLVLHVPLTGAEAC LMSVEEETELLLR (in isoform 2). VSP_007401
CONFLICT   205   310        Missing (in Ref. 2). 
CONFLICT   343   365        LEMEASTYDGVFIWKISDFARKR -> RPFQAQCGHRYCSFCLASILRKL (in Ref. 1; AAA87706). 
HELIX   315   318  4      
HELIX   335   347  13      
STRAND   350   360  11      
HELIX   361   369  9      
STRAND   381   384  4      
STRAND   389   395  7      
HELIX   400   402  3      
TURN   403   405  3      
STRAND   406   414  9      
HELIX   419   421  3      
STRAND   430   434  5      
STRAND   443   447  5      
HELIX   454   456  3      
STRAND   460   463  4      
STRAND   467   474  8      
TURN   475   480  6      
TURN   482   484  3      
STRAND   489   496