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. 2019 Jan 21;2:30. doi: 10.1038/s42003-019-0281-1

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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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Fig. 3 — Phosphoproteomic analysis of P. patens WT and Ppsnrk2 QKO plants. a Principal component analysis of quantitative data of phosphopeptides from wild-type (WT) and QKO plants under ABA treatment. b A Venn diagram of two phosphopeptide groups; one is the ABA-responsive (upregulated) group in WT, and the other is the SnRK2-dependent group. Phosphorylation motifs in those phosphopeptides were analyzed by the Motif-X algorithm. c Examples of ABA-responsive phosphopeptides in WT (solid) and QKO (empty). Pp3c20_7230V3.2.p; ABF transcription factor, Pp3c27_6350V3.1.p; MRF1 (MA3 domain-containing translation regulatory factor), Pp3c5_11880V3.1.p; COR (dehydrin), and Pp3c22_17930V3.1.p; NRP1 (nucleosome assembly protein 1). The relative peak areas to that of WT control (0 min) for respective phosphopeptides were calculated in each replicate using the quantitative data described in Supplementary Data 4. The values are mean ± S.E. (n = 3)