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Phosphoproteome-wide kinase assignments suggest more widespread multi-kinase phosphorylation than existing literature annotations do.

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posted on 13.05.2022, 17:43 by Brandon M. Invergo

a) Histograms of the number of kinases associated with sites in the phosphoproteome reveal different views of the phosphorylation network. Literature annotations in PhosphoSitePlus suggest most sites are regulated by one or two kinases. In vitro Naïve Bayes+ predicts some S/T sites are “hubs” and all Y sites can be phosphorylated by most Y kinases. LinkPhinder and IV-KAPhE, in contrast, predict a long tail of hub sites. b) Histograms of the median number of kinases assigned per site for all proteins likewise show different predictions for hub proteins. Literature annotations suggest most proteins are phosphorylated by one kinase at each site. The computational methods all hypothesize multiple kinases per site, with some substrate proteins being very promiscuous at all their sites.