| Modification Notes |
The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. RIP4, also known as RIPK4 (receptor-interacting serine/threonine-protein kinase 4), PKK (PKC ∂-interacting protein kinase), DIK, ANKK2 or ANKRD3 (ankyrin repeat domain-containing protein 3), is a peripheral membrane protein that belongs to the TKL Ser/Thr protein kinase family and functions as a receptor-interacting protein (RIP) that modulates epidermal growth and differentiation. RIPs interact with the intracellular domain of tumor necrosis factor receptors (TNFRs) and facilitate downstream signaling and apoptosis induction. RIP4 contains ten ankyrin-repeats and one protein kinase domain, and participates in the activation of NF˚B. Two isoforms exist due to alternative splicing events. |