Anti-TRAIP (TRIP)

TRIP (TRAF-interacting protei),also known as TRAIP is a component of receptor-TRAF signaling complexes. Structurally it contains an N-terminal RING finger motif and a putative coiled-coil domain and composed of 469 amino acid approximately. TRIP has been shown to associate with TRNFR2 or CD30 signaling complexes through its interaction with TRAF proteins and inhibit TRAF2-mediated NF-kB activation. The recruitment of different TRAFs and TRAF associated proteins like TRIP to receptor complexes can help regulate and provide specificity to the intracellular signals triggered by the cell surface receptors. Protein function: E3 ubiquitin ligase acting as a negative regulator of innate immune signaling. Inhibits activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation (PubMed:22945920). Involved in response to genotoxic lesions during genome replication. Promotes H2AX and RPA2 phosphorylation after replication-associated DNA damage and assists fork progression at UV-induced replication-blocking lesions during S phase (PubMed:26595769). Has also been proposed to play a role in promoting translesion synthesis by mediating the assembly of 'Lys- 63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity (PubMed:24553286). The function in translesion synthesis is controversial (PubMed:26595769). [The UniProt Consortium]