The human c-fes proto-oncogene encodes a protein-tyrosine kinase (c-Fes) distinct from c-Src, c-Abl and other non-receptor protein-tyrosine kinases. Although originally identified as the cellular homolog of several transforming retroviral oncoproteins, c-Fes kinase activity is tightly regulated in vivo. Unique to c-Fes is its long N terminal region, which contains a Fer/CIP4 Homology (FCH) region, followed by at least two coiled-coil homology domains which have essential roles in the regulation of kinase activity and mediate c-Fes oligomerization in vivo. c-Fes is involved in the activation of phosphoinositide 3-kinase (PI3-kinase) downstream of a variety of cytokine receptors. The PI3- kinase/c-Akt pathway regulates cell survival, migration,and morphological differentiation of endothelial cells during angiogenesis, and c-Fes thus may be a potential target of anti-cancer therapy, especially for patients with anti-VEGF refractory cancer. 

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