VEGF receptor 2 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 growth factor receptors, upon ligand binding VEGF receptor 2 dimerizes and is autophosphorylated on multiple tyrosine residues. These sites can be involved in the regulation of kinase activity or serve as binding sites for SH2 and phosphotyrosine binding containing signalling 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.