Src kinase family is a family of non-receptor tyrosine kinases that includes nine members: Src, Yes, Fyn, and Fgr, forming the SrcA subfamily, Lck, Hck, Blk, and Lyn in the SrcB subfamily, and Frk in its own subfamily. Frk has homologs in invertebrates such as flies and worms, and Src homologs exist in organisms as diverse as unicellular choanoflagellates, but the SrcA and SrcB subfamilies are specific to vertebrates. Src family kinases contain six conserved domains: a N-terminalmyristoylated segment, a SH2 domain, a SH3 domain, a linker region, a tyrosine kinase domain, and C-terminal tail.[1]
Src family kinases interact with many cellular cytosolic, nuclear and membrane proteins, modifying these proteins by phosphorylation of tyrosine residues. A number of substrates have been discovered for these enzymes.[2][3][4] Deregulation, including constitutive activation or over expression, may contribute to the progression of cellular transformation and oncogenic activity.[5]
^Parsons SJ, Parsons JT (October 2004). "Src family kinases, key regulators of signal transduction". Oncogene. 23 (48): 7906–9. doi:10.1038/sj.onc.1208160. PMID15489908.