A schematic structure of TRAF2. The full-length TRAF2 is composed of 501 amino acids (molecular weight 55 kDa). The RING-type zinc finger domain possesses an E3 ubiquitin-protein ligase activity through Lys63 (K63) or Lys48 (K48) activation. The coiled coil domain mediates TRAF2 homo- or hetero-oligomerization, and phosphorylation at Thr117 (T117) is needed for NF-κB activation. The MATH/TRAF domain binds to receptor cytoplasmic domains.