TRAF1
Domain
The coiled coil domain mediates homo- and hetero-oligomerization.
The MATH/TRAF domain binds to receptor cytoplasmic domains.
Cleavage by CASP8 liberates a C-terminal fragment that promotes apoptosis and inhibits the activation of NF-kappa-B in response to TNF signaling.
Function
Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.
Post-translational modifications
Polyubiquitinated by BIRC2 and/or BIRC3, leading to its subsequent proteasomal degradation (PubMed:15468071, PubMed:19937093). Ubiquitinated by the SCF(FBXL2) complex, leading to its degradation by the proteasome (By similarity).
Alternative names
EBI6, TRAF1, TNF receptor-associated factor 1, Epstein-Barr virus-induced protein 6