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Tumor necrosis factor receptor superfamily, member 1B
Symbols TNFRSF1B; p75; CD120b; TBPII; TNF-R-II; TNF-R75; TNFBR; TNFR2; TNFR80; p75TNFR
External IDs OMIM191191 MGI1314883 HomoloGene829 GeneCards: TNFRSF1B Gene
RNA expression pattern
PBB GE TNFRSF1B 203508 at tn.png
More reference expression data
Species Human Mouse
Entrez 7133 21938
Ensembl ENSG00000028137 ENSMUSG00000028599
UniProt P20333 Q3U2A9
RefSeq (mRNA) NM_001066 NM_011610
RefSeq (protein) NP_001057 NP_035740
Location (UCSC) Chr 1:
12.15 - 12.19 Mb
Chr 4:
144.48 - 144.51 Mb
PubMed search [1] [2]

Tumor necrosis factor receptor superfamily member 1B is a protein that in humans is encoded by the TNFRSF1B gene.[1][2] The protein encoded by this gene is a member of the Tumor necrosis factor receptor superfamily, which also contains TNFRSF1A. The protein encoded by this gene is a member of the TNF-receptor superfamily. This protein and TNF-receptor 1 form a heterocomplex that mediates the recruitment of two anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. The function of IAPs in TNF-receptor signalling is unknown, however, c-IAP1 is thought to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Knockout studies in mice also suggest a role of this protein in protecting neurons from apoptosis by stimulating antioxidative pathways.[3]



TNFRSF1B has been shown to interact with TTRAP[4] and TRAF2.[5][6][7][8][9][10][11]


  1. ^ Schall TJ, Lewis M, Koller KJ, Lee A, Rice GC, Wong GH, Gatanaga T, Granger GA, Lentz R, Raab H, et al. (Jun 1990). "Molecular cloning and expression of a receptor for human tumor necrosis factor". Cell 61 (2): 361–70. PMID 2158863.  
  2. ^ Santee SM, Owen-Schaub LB (Oct 1996). "Human tumor necrosis factor receptor p75/80 (CD120b) gene structure and promoter characterization". J Biol Chem 271 (35): 21151–9. PMID 8702885.  
  3. ^ 7133 "Entrez Gene: TNFRSF1B tumor necrosis factor receptor superfamily, member 1B". 7133.  
  4. ^ Pype, S; Declercq W, Ibrahimi A, Michiels C, Van Rietschoten J G, Dewulf N, de Boer M, Vandenabeele P, Huylebroeck D, Remacle J E (Jun. 2000). "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. (UNITED STATES) 275 (24): 18586–93. doi:10.1074/jbc.M000531200. ISSN 0021-9258. PMID 10764746.  
  5. ^ Bouwmeester, Tewis; Bauch Angela, Ruffner Heinz, Angrand Pierre-Olivier, Bergamini Giovanna, Croughton Karen, Cruciat Cristina, Eberhard Dirk, Gagneur Julien, Ghidelli Sonja, Hopf Carsten, Huhse Bettina, Mangano Raffaella, Michon Anne-Marie, Schirle Markus, Schlegl Judith, Schwab Markus, Stein Martin A, Bauer Andreas, Casari Georg, Drewes Gerard, Gavin Anne-Claude, Jackson David B, Joberty Gerard, Neubauer Gitte, Rick Jens, Kuster Bernhard, Superti-Furga Giulio (Feb. 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. (England) 6 (2): 97–105. doi:10.1038/ncb1086. ISSN 1465-7392. PMID 14755267.  
  6. ^ Song, H Y; Donner D B (Aug. 1995). "Association of a RING finger protein with the cytoplasmic domain of the human type-2 tumour necrosis factor receptor". Biochem. J. (ENGLAND) 309 ( Pt 3): 825–9. ISSN 0264-6021. PMID 7639698.  
  7. ^ Takeuchi, M; Rothe M, Goeddel D V (Aug. 1996). "Anatomy of TRAF2. Distinct domains for nuclear factor-kappaB activation and association with tumor necrosis factor signaling proteins". J. Biol. Chem. (UNITED STATES) 271 (33): 19935–42. ISSN 0021-9258. PMID 8702708.  
  8. ^ Hostager, Bruce S; Bishop Gail A (Apr. 2002). "Role of TNF receptor-associated factor 2 in the activation of IgM secretion by CD40 and CD120b". J. Immunol. (United States) 168 (7): 3318–22. ISSN 0022-1767. PMID 11907088.  
  9. ^ Rothe, M; Xiong J, Shu H B, Williamson K, Goddard A, Goeddel D V (Aug. 1996). "I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 93 (16): 8241–6. ISSN 0027-8424. PMID 8710854.  
  10. ^ Marsters, S A; Ayres T M, Skubatch M, Gray C L, Rothe M, Ashkenazi A (May. 1997). "Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1". J. Biol. Chem. (UNITED STATES) 272 (22): 14029–32. ISSN 0021-9258. PMID 9162022.  
  11. ^ Carpentier, Isabelle; Coornaert Beatrice, Beyaert Rudi (Oct. 2008). "Smurf2 is a TRAF2 binding protein that triggers TNF-R2 ubiquitination and TNF-R2-induced JNK activation". Biochem. Biophys. Res. Commun. (United States) 374 (4): 752–7. doi:10.1016/j.bbrc.2008.07.103. PMID 18671942.  

Further reading

  • Kollias G, Kontoyiannis D (2003). "Role of TNF/TNFR in autoimmunity: specific TNF receptor blockade may be advantageous to anti-TNF treatments.". Cytokine Growth Factor Rev. 13 (4-5): 315–21. doi:10.1016/S1359-6101(02)00019-9. PMID 12220546.  
  • Holtmann MH, Schuchmann M, Zeller G, et al. (2003). "The emerging distinct role of TNF-receptor 2 (p80) signaling in chronic inflammatory disorders.". Arch. Immunol. Ther. Exp. (Warsz.) 50 (4): 279–88. PMID 12371624.  
  • Horiuchi T, Kiyohara C, Tsukamoto H, et al. (2007). "A functional M196R polymorphism of tumour necrosis factor receptor type 2 is associated with systemic lupus erythematosus: a case-control study and a meta-analysis.". Ann. Rheum. Dis. 66 (3): 320–4. doi:10.1136/ard.2006.058917. PMID 17028114.  

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