a calcium/calmodulin-dependent S/T protein kinase of the CAMK group. Binding of calmodulin is thought to result in a conformational change and can lead to subsequent activation through phosphorylation by CAMKK1 and CAMKK2. Can be activated by CAMKK1 in a calcium-independent manner. Its Ca(2+)/CaM-dependent activity is enhanced 30-fold in vitro by phosphorylation at Thr180 by CaMKK1. Broadly expressed. Highly and mostly expressed in polymorphonuclear leukocytes (neutrophilic and eosinophilic granulocytes) while little or no expression is observed in monocytes and lymphocytes. May regulate calcium-mediated granulocyte function. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta and probably CREB1. Expression increases upon treatment of EC cells with DMSO and retinoic acid. Two isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, CAMK; Protein kinase, Ser/Thr (non-receptor); EC 220.127.116.11; Kinase, protein; CAMK group; CAMK1 family
Cellular Component: cytoplasm; nucleus; calcium- and calmodulin-dependent protein kinase complex
Molecular Function: calmodulin binding; calmodulin-dependent protein kinase activity; ATP binding
Biological Process: positive regulation of apoptosis; positive regulation of phagocytosis; regulation of dendrite development; activation of CREB transcription factor; inflammatory response; protein amino acid phosphorylation; negative regulation of apoptosis
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.