Figure 1.

The amino acid residues significantly enriched and depleted around phosphorylation sites. Each residue is assigned a property: surface (red) or buried (black) according to Janin’s scale (28) (A), charged (black) or neutral (green) (B), hydrophobic (black) or hydrophilic (blue) according to Eisenberg’s scale (39) (C), high (pink) or low (blue) flexibility index according to flexibility scale (27) (D). Following the definition of Vihinen et al. (27) alanine and threonine were considered to have high flexibility if flanked by residues with HFP, and they were considered to have low flexibility if surrounded by residues with LFP.