a member of the MAPKAPK family of protein kinases. Activated by growth inducers and stress stimulation of cells. In vitro studies demonstrated that ERK, p38 MAP kinase and Jun N-terminal kinase were all able to phosphorylate and activate this kinase, which suggested the role of this kinase as an integrative element of signaling in both mitogen and stress responses. This kinase was reported to interact with, phosphorylate and repress the activity of E47, which is a basic helix-loop-helix transcription factor known to be involved in the regulation of tissue-specific gene expression and cell differentiation. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; EC 220.127.116.11; Protein kinase, CAMK; Protein kinase, Ser/Thr (non-receptor); CAMK group; MAPKAPK family; MAPKAPK subfamily
Molecular Function: ATP binding; calcium-dependent protein serine/threonine kinase activity; calmodulin binding; calmodulin-dependent protein kinase activity; MAP kinase kinase activity; protein binding; protein serine/threonine kinase activity
Biological Process: activation of MAPK activity; cell surface receptor linked signal transduction; MAPKKK cascade; peptidyl-serine phosphorylation; protein amino acid autophosphorylation; Ras protein signal transduction; response to cytokine stimulus; response to lipopolysaccharide; response to stress; signal transduction; toll-like receptor signaling pathway; vascular endothelial growth factor receptor signaling pathway
LTP: 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.