a serine/threonine kinase of the Raf family with no demonstrated kinase activity. A location-regulated scaffolding protein connecting MEK to RAF. Promotes MEK and RAF phosphorylation and activity through assembly of an activated signaling complex. Interacts with RAF and MAPK/ERK, in a Ras-dependent manner. The binding of 14-3-3 proteins to phosphorylated KSR prevents the membrane localization. In unstimulated cells, the phosphorylated form is bound to a 14-3-3 protein and sequestered in the cytoplasm. Translocates from the cytoplasm to the cell periphery following TNF treatment. When Bad is available, ceramide signaling through the Ras/Raf cascade can lead to apoptosis. Three alternatively-spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, Ser/Thr (non-receptor); Kinase, protein; Protein kinase, TKL; TKL group; RAF family
Molecular Function: protein serine/threonine kinase activity; protein binding; MAP-kinase scaffold activity; mitogen-activated protein kinase kinase binding; metal ion binding; ATP binding; protein kinase activity
Biological Process: positive regulation of MAPKKK cascade; Ras protein signal transduction; protein amino acid phosphorylation
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.