| 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. TNIK (TRAF2 and NCK-interacting protein kinase) is a 1,360 amino acid protein that contains one protein kinase domain and belongs to a subfamily of Ser/Thr protein kinases. Expressed ubiquitously with highest expression in brain, heart and skeletal muscle, TNIK functions as a stress-activated Ser/Thr kinase that catalyzes the ATP-dependent phosphorylation of target proteins and is thought to play a role in the response to environmental stress. Additionally, via its catalytic activity, TNIK may participate in cytoskeletal regulation events throughout the cell. TNIK exists as 8 isoforms that are produced by alternative splicing events. |