Catalytic activity:ATP + a protein = ADP + a phosphoprotein. ,Domain:The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate. ,enzyme regulation:Activated by Ca (2+) /calmodulin. Binding of calmodulin results in a conformational change that generates functional binding sites for both , substrate and ATP , and thus releaves intrasteric autoinhibition. Must be phosphorylated to be maximally active. Phosphorylated by CAMKK1 or CAMKK2. ,Function:Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes like transcriptional regulation , hormone production , translational regulation , regulation of actin filament organization and neurite outgrowth. Involved in calcium-dependent activation of the ERK pathway (By similarity) . Recognizes the substrate consensus sequence [MVLIF]-x-R-x (2) -[ST]-x (3) -[MVLIF]. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1 , ATF1 , CTFR , MYL9 , SYN1/synapsin I and SYNII/synapsin II. ,similarity:Belongs to the protein kinase superfamily. ,similarity:Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. ,similarity:Contains 1 protein kinase domain. ,subcellular location:Predominantly cytoplasmic. ,subunit:Monomer. Interacts with XPO1. ,tissue specificity:Ubiquitous. ,
展开内容