Transferase(Phosphotransferase); domain 1
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
Kit receptor dimerization is driven by bivalent binding of stem cell factor.
Inhibition of spontaneous receptor phosphorylation by residues in a putative alpha-helix in the KIT intracellular juxtamembrane region.
Structure of a c-kit product complex reveals the basis for kinase transactivation.
Autoinhibition of the kit receptor tyrosine kinase by the cytosolic juxtamembrane region.
Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase.
Structure and regulation of Kit protein-tyrosine kinase--the stem cell factor receptor.
Stem cell factor and its receptor c-Kit as targets for inflammatory diseases.
Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
Detailed conformational dynamics of juxtamembrane region and activation loop in c-Kit kinase activation process.
KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients.
This enzyme belongs to platelet-derived growth factor (PDGF) receptor family, along with homologous enzymes, such as colony-stimulating factor-1 receptor (CSF-1-R, cFMS) (M00330 in EzCatDB) and Receptor-type tyrosine-protein kinase FLT3 (M00331 in EzCatDB). This enzyme seems to interact with different proteins from those proteins which are interacted with the homologous enzymes. The catalytic domain of this enzyme is homologous to that of vascular endothelial growth factor receptor (M00131 in EzCatDB).