OBSCN
Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle. Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1. Binds (via the PH domain) strongly to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. 5 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: CAMK group; EC 2.7.11.1; Kinase, protein; Protein kinase, CAMK; Protein kinase, Ser/Thr (non-receptor); Trio family
Cellular Component: cell-cell junction; cytosol; M band; myofibril; nuclear body; plasma membrane; sarcolemma; Z disc
Molecular Function: ankyrin binding; ATP binding; calmodulin binding; cell adhesion molecule binding; guanyl-nucleotide exchange factor activity; metal ion binding; phosphatidylinositol-3,4,5-trisphosphate binding; phosphatidylinositol-3,4-bisphosphate binding; phosphatidylinositol-3-phosphate binding; phosphatidylinositol-4,5-bisphosphate binding; phosphatidylinositol-4-phosphate binding; phosphatidylinositol-5-phosphate binding; protein binding; protein serine kinase activity; protein serine/threonine kinase activity; structural constituent of muscle; titin binding
Biological Process: cell-cell adhesion; protein localization to M-band; protein phosphorylation; regulation of catalytic activity; regulation of small GTPase mediated signal transduction; sarcomere organization