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. Author manuscript; available in PMC: 2014 Mar 3.
Published in final edited form as: Sci Signal. 2011 Jun 28;4(179):ra42. doi: 10.1126/scisignal.2001796

Fig. 2. Phosphorylation motifs for Cdk1/cyclin B and Plk1.

Fig. 2

(A) The substrate motif for Cdk1/cyclin B reveals near exclusive selection for Pro in the Ser/Thr+1 position, strong selectivity for Arg and Lys in the Ser/Thr+3 position, and Lys in the Ser/Thr+4 position. (B) Comparison of the expanded Cdk1/cyclin B motif with mapped substrate sites (49). Bold represents residues that distinguish the submotifs. (C) The substrate motif for Plk1 reveals selection for Asp, Asn, or Glu in the Ser/Thr-2 position and hydrophobic amino acids (Φ) in the Ser/Thr+1 position, and discrimination against Pro in the Ser/Thr+1 position.