The studies report that TRIP is a negative factor in down-regulation of proinflammatory cytokine production through the TNF-induced NF-κB activation. More so, TRIP is used in pathways and processes like protein-protein interactions, TNF-induced signaling pathway, ubiquitination Assays, TNF-induced Signaling Pathway, TNFinduced p65 Nuclear Translocation Assay, Real-time PCR Analysis, Enzyme-linked Immunosorbent Assay (ELISA), Cytokine Expression Array, and Statistical Analysis. Furthermore, it acts as a regulator of TNF-induced inflammatory response. TRAF2 has a RING domain that participates in ligase activity. TRIP is also used in preventing Lys63-linked TRAF2 Ubiquitination through engagement of TNF receptor associated factor and TRAF-interacting protein. Similarly, TRIP destructively regulates ubiquitination mediated by TRAF-2. Additionally, it negatively affects TNF-induced NF-κB activation via the prevention of a RING domain in ligase. The research shows that TRAF-interacting protein is imperative in the activation through down-regulation of p65 phosphorylation. Moreover, TRIP is a factor in human disease and a sky-binding partner. Studies mention that TNF receptor-associated factor (TRAF)-interacting protein (TRIP) is a novel SyK-binding partner. Other than being a binding partner, TRIP is a factor in the pathogenesis of human diseases. TRIP-deficient mouse models have laid the basis to understand the roles of TRIP in the pathogenesis of human diseases. TRIP is also a key partner in DNA damage response. In fact, previous researches discovered that TRIP is found in DNA replication compartments particularly in DNA damage responses. Further studies show that TRIP also influences mitosis. According to Lee et al., TRIP acts as a novel binding agent of RAP80. It uses a yeast two-hybrid system. As such, it plays a critical role in the conscription of RAP80 to deoxy-ribonucleic acid lesions. Therefore, TRIP is a significant factor in different signaling processes and pathways.