Table 2. The percentages of amino acid residues that are significantly (P < 0.05) enriched and depleted around phosphorylation sites.

	Surface (%)	Buried (%)	Charged (%)	Neutral (%)	Hydrophobic (%)	Hydrophilic (%)	HFPa (%)	LFPb (%)
S enriched	95	5	57	43	13	87	100	0
S depleted	25	75	6	94	68	32	11	89
T enriched	79	21	54	46	25	75	93	7
T depleted	29	71	7	93	71	29	25	75
Y enriched	80	20	36	64	53	47	84	16
Y depleted	31	69	13	87	80	20	31	69

^aResidues with high flexibility parameters by Vihinen et al. (27).

^bResidues with low flexibility parameters.