Src kinases are known for having a characteristically short C-terminal tail that contains an autoinhibitory phosphorylation site.
The SH2 domain of Src family kinases consist of approximately 100 amino acids.
The strength of binding is dependent on the amino acids surrounding the phosphorylated tyrosine.
[8] The C-terminal tail is a location of phosphorylation and dephosphorylation in Src family kinases.
When looking at other Src molecules, most are phosphorylated at this tyrosine residue by action of the Csk family protein kinases.
An absence of regulatory proteins will also affect Src's ability to be activated properly.
Myristoylation and fusion proteins work together to localize Src to cellular membranes.
Src kinases transduce signals related to cellular processes such as proliferation, differentiation, motility, and adhesion.
70% of breast cancer cells overexpress tyrosine kinases (specifically c-Src).