TNFRSF1B

Tumor necrosis factor receptor superfamily, member 1B
Identifiers
Symbols TNFRSF1B; CD120b; TBPII; TNF-R-II; TNF-R75; TNFBR; TNFR1B; TNFR2; TNFR80; p75; p75TNFR
External IDs OMIM191191 MGI1314883 HomoloGene829 GeneCards: TNFRSF1B Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 7133 21938
Ensembl ENSG00000028137 ENSMUSG00000028599
UniProt P20333 Q3U2A9
RefSeq (mRNA) NM_001066 NM_011610.3
RefSeq (protein) NP_001057 NP_035740.2
Location (UCSC) Chr 1:
12.23 – 12.27 Mb
Chr 4:
144.8 – 144.84 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. doi:10.1016/0092-8674(90)90816-W. 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. doi:10.1074/jbc.271.35.21151. 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 14743216. 
  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. PMC 1135706. PMID 7639698. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1135706. 
  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. doi:10.1074/jbc.271.33.19935. 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. doi:10.1073/pnas.93.16.8241. ISSN 0027-8424. PMC 38654. PMID 8710854. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=38654. 
  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. doi:10.1074/jbc.272.22.14029. 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

External links