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. 2019 Jul 19;9:10503. doi: 10.1038/s41598-019-46385-4

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Characteristics of serine or threonine-directed kinases. (a) Correlation between serine/threonine preference of STKs and the maximum fold-increase in their phosphorylation motifs. (b) The box plot of a ratio of multiply phosphorylated peptides identified by in vitro kinase profiling for serine-directed, threonine-directed tyrosine kinases. (c) Relationship between Ser/Thr specificity and the amino acid at the +1 position of the common sequence “DFG” in the kinase domains.