Baculoviral IAP repeat-containing 3 Adenovirus

TRAF-interacting proteins include TANK (also designated I-TRAF), ILP, ML-IAP, XAF1, c-IAP and survivin. TANK binds to the conserved TRAF-C domain common to TRAF1, TRAF2 and TRAF3. ML-IAP, c-IAP1 and c-IAP2 are related to the inhibitor of apoptosis protein (IAP) family of Baculovirus proteins. The c-IAPs associate with TRAF1 and TRAF2 through their N-terminal BIR motif-containing domain. IAP-like protein (ILP) also contains an N-terminal BIR motif-containing domain. ILP inhibits activated caspase-3, leading to the resistance of FAS-mediated apoptosis. An additional IAP family member, survivin (also designated TIAP), is expressed in the G2/M phase of the cell cycle and associates with microtubules of the mitotic spindles. Caspase-3 activity increases when a disruption of survivin-microtubule interactions occurs.