Extended Data Fig. 3: Human Tyr kinases display strong selectivities and diverse preferences for the amino acids near their Tyr phosphorylation sites.
From: The intrinsic substrate specificity of the human tyrosine kinome
a-c, Log-selectivity of the 78 conventional RTKs and nRTKs on PSPA substrate peptides containing Tyr sites flanked by isoleucine (a), serine (b), or glutamate (c) residues relative to the 18 natural amino acids excluding cysteine and tyrosine. d, Kinome-wide variability in log-selectivity for specific amino acid residues at each position surrounding the substrate Tyr phosphorylation site. Horizontal line indicates a value of 0.5 logs, identifying positions −1 to +3 as the most variably selective positions. e, Experimental kinase selectivity for each Tyr kinase on all amino acids across the highly selective substrate positions −1 to +3.