Receptor-interacting protein 3 (RIP3) contains a N-terminal kinase domain and interacts with RIP. The binding of RIP to RIP3 causes the RIP3/RIP complex to be shuttled into the tumor necrosis factor receptor-1 signaling cascade. RIP3 is known to be a very effective apoptosis inducer. Two novel splice variants of RIP3 have been discovered, RIP3 beta and RIP3 gamma, that have shown to decrease apoptosis related to full length RIP3. RIP3 gamma has been shown to be significantly up-regulated in colon and lung cancers and may play a role in tumorigenesis.