Tumor necrosis factor (TNF) receptor associated factors (TRAFs) were initially discovered as adaptor proteins that link the TNF receptor superfamily to signaling pathways and are thus important regulators of cell death and cellular response to stress. TRAF proteins share a homology region that allows them to bind to cell receptors and other TRAF proteins, causing the activation of different signal cascades depending on the TRAFs involved. For example, TRAF2 and TRAF3 directly bind to the CD40, a NF receptor superfamily member involved in inducing B cell immunity, and are critical for NF-kappa-B activation in mouse B lymphocytes. TRAF2 along with TRAF6 has also been shown to be required for CD40 signaling in nonhemopoietic cells. TRAF2 also interacts with the TRFR superfamily member lymphotoxin-beta receptor (LTbetaR) in association with TRAF3 and the apoptosis inhibitors cIAP1 and Smac.
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Protein Aliases: E3 ubiquitin-protein ligase TRAF6; Interleukin-1 signal transducer; RING finger protein 85; RING-type E3 ubiquitin transferase TRAF6; TNF receptor-associated factor 6; TNF receptor-associated factor 6, E3 ubiquitin protein ligase
Gene Aliases: MGC:3310; RNF85; TRAF6
UniProt ID: (Human) Q9Y4K3
Entrez Gene ID: (Human) 7189
Molecular Function: scaffold/adaptor protein