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Tumor necrosis factor receptor superfamily, member 1B
Identifiers
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
Orthologs
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]

Contents

Interactions

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

References

  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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch= 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.  

External links

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