CD120b. TNF-RII (p75/p80)

MR2-1

Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Association to the receptor is also mediated by the interaction with TRADD. Mediates activation of NF-kappa-B and JNK and is involved in apoptosis. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. Seems to be involved in IL-15 signaling.

Cytoplasm.

The MATH/TRAF domain binds to receptor cytoplasmic domains.

Contains 1 MATH domain.

Contains 2 TRAF-type zinc fingers. Summary: The protein encoded by this gene is a member of the TNF receptor associated factor (TRAF) protein family. TRAF proteins associate with and mediate the signal transduction from members of the TNF receptor superfamily. This protein directly interacts with TNF receptors and forms a heterodimeric complex with TRAF1. This protein is required for TNF-alpha-mediated activation of MAPK8/JNK and NF-kappaB. The protein complex formed by this protein and TRAF1 interacts with the inhibitor-of-apoptosis proteins (IAPs) and functions as a mediator of the anti-apoptotic signals from TNF receptors. The interaction of this protein with TRADD a TNF receptor associated apoptotic signal transducer ensures the recruitment of IAPs for the direct inhibition of caspase activation. BIRC2/c-IAP1 an apoptosis inhibitor possessing ubiquitin ligase activity can unbiquitinate and induce the degradation of this protein and thus potentiate TNF-induced apoptosis. Multiple alternatively spliced transcript variants have been found for this gene but the biological validity of only one transcript has been determined. [1] Varfolomeev E. Wayson S. M. Dixit V. M. Fairbrother W. J. and Vucic D. The inhibitor of apoptosis protein fusion c-IAP2. MALT1 stimulates NF-kappaB activation independently of TRAF1 AND TRAF2[2] Wu Y. Fan Y. Xue B. Luo L. Shen J. Zhang S. Jiang Y. and Yin Z. Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals[3] Wang J. Li C. Liu Y. Mei W. Yu S. Liu C. Zhang L. Cao X. Kimberly R. P. Grizzle W. and Zhang H. G. JAB1 determines the response of rheumatoid arthritis synovial fibroblasts to tumor necrosis factor-alpha[4] Lim J. Hao T. Shaw C. Patel A. J. Szabo G. Rual J. F. Fisk C. J. Li N. Smolyar A. Hill D. E. Barabasi A. L. Vidal M. et al. A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration[5] Uemura N. Kajino T. Sanjo H. Sato S. Akira S. Matsumoto K. and Ninomiya-Tsuji J. TAK1 is a component of the Epstein-Barr virus LMP1 complex and is essential for activation of JNK but not of NF-kappaB[6] 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. [7] Ota T. Suzuki Y. Nishikawa T. Otsuki T. Sugiyama T. Irie R. Wakamatsu A. Hayashi K. Sato H. Nagai K. et al. Complete sequencing and characterization of 21 243 full-length human cDNAs. [8] Rieder M. J. Daniels R. L. da Ponte S. H. Hastings N. C. Ahearn M. O. Rajkumar N. Yi Q. Nickerson D. A. SeattleSNPs. NHLBI HL66682 program for genomic applications UW-FHCRC Seattle WA (URL: http://pga. gs. washington. edu). [9] 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. [10] Pomerantz J. L. Baltimore D. NF-kB activation by a signaling complex containing TRAF2 TANK and TBK1 a novel IKK-related kinase.