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Vascular endothelial growth factor receptor 2 (VEGFR2) is a member of a receptor tyrosine kinase family whose activation plays an essential role in a large number of biological processes such as embryonic development, wound healing, cell proliferation, migration and differentiation. Like other common growth factor receptors, VEGF receptor 2 dimerises upon ligand binding and is autophosphorylated at multiple tyrosine residues. These sites can be involved in the regulation of kinase activity or can serve as binding sites for SH2 and phosphotyrosine binding containing signaling proteins. Phosphorylation of Tyrosines 1054 and 1059 in the activation loop is required for activation of VEGF receptor 2 and its intrinsic tyrosine kinase activity.
Defects in the VEGFR2 gene are associated with susceptibility to benign, highly proliferative lesions involving aberrant localized growth of capillary endothelium called hemangioma capillary infantile. HCI is the most common tumor found in infants, found in up to 10% of all births.