| 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. RIP5 (receptor interacting protein kinase 5), also known as RIPK5, DustyPK or SGK496 (Sugen kinase 496), is a 929 amino acid protein that localizes to the cytoplasm, contains one protein kinase domain and belongs to the Ser/Thr protein kinase family. Expressed at low levels in placenta, heart, brain, kidney, pancreas, testis and skeletal muscle, RIP5 catalyzes the ATP-dependent phosphorylation of target proteins and is thought to induce both caspase-dependent and -independent cell death. Four isoforms of RIP5 exist due to alternative splicing events. |