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. 2011 Dec 2;6(12):e28228. doi: 10.1371/journal.pone.0028228

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Lu et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Top: (A) The influence of acetylated lysine on neighboring phosphorylation sites was predicted by substituting a leucine for a lysine at all predicted K-Ac sites and then predicting potential phosphorylation sites using NetPhosK 1.0. (B) In all, 51% of nearby phosphorylation sites were affected, and these were classified as Type I (gain of a phosphorylation site, 10%), Type II (loss of a phosphorylation site, 35%), Type III (retention of a phosphorylation site with gain of kinase binding site, 16%), Type IV (retention of a phosphorylation site with loss of kinase binding site, 29%), and Type V (loss of an endogenous kinase binding site with concomitant gain of a new one, 10%). This analysis was repeated by substituting glutamine for lysine (Panels C and D). This analysis was repeated for methylation using BPB-PPMS (middle) and ubiquitination using UbPred (bottom). For further details, see text.