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. 2014 Jul 29;15(8):13275–13298. doi: 10.3390/ijms150813275

Figure 1.

Figure 1

Amino acid pair propensities in p53 phosphorylation motifs follow similar trends as those of other p53 protein families, indicating evolutionary optimization of p53 phosphorylation motifs for function. (A) Comparison of the propensity of a charged residue (and proline) adjacent to potential phosphorylation sites shows that p53 prefers acidic residues near Ser/Thr, while p63/p73 prefers proline near Ser/Tyr. The distributions of the amino acid pair propensities DPxy among p53 pairs at the position (B) XiYj=i+2 (tripeptide X × Y motif); and (C) pairs at the position XiYj=i+3 (tetrapeptide X ×× Y motif). The red bar indicates pairs that are preferred for all p53, p63, and p73 proteins.