Activated PTK6 (BRK) phosphorylates AKT1 on tyrosine residues Y315 and Y326. The SH2 domain of PTK6 binds phosphorylated tyrosines in AKT1, thus enhancing the interaction between PTK6 and AKT1. PTK6-mediated phosphorylation may facilitate subsequent activating phosphorylation of AKT1 in response to generation of PIP3 by PI3K (Zheng et al. 2010). In addition, binding of PTK6 to AKT1 may prevent AKT1 activity in unstimulated cells; however, this effect may be cell type specific (Zhang et al. 2005). EGF-stimulation causes the complex of PTK6 and AKT1 to dissociate, but the exact mechanism is not known (Zhang et al. 2005).