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. 2018 May 9;8:7365. doi: 10.1038/s41598-018-25738-5

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© The Author(s) 2018

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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Autophosphorylation activity of PfCK2. (A) Autoradiograph kinase activity assay was carried out using 2 μg of wild type (lane 1) or D179S mutant PfCK2 (lane 2) with Mg [γ³²P]-ATP. (B) The proteins were resolved by SDS-PAGE, stained with Coomassie blue and their activity analysed by autoradiography. (C) Annotated MS/MS spectra showing identification of Y30 phosphorylation using the Mascot protein database search software. The Tyr³⁰ (labeled Y16 in the spectrum) is unambiguously identified as it is sandwiched by a series of y-ions [y16,y17,y18(phosphorylation site),y19,y20]. y13 ion was trimmed 10 times to show the weaker ions in the spectrum.