Abstract
The data reported here are associated with the article “Comparative phosphoproteome analysis upon ethylene and abscisic acid treatment in Glycine max leaves” [1]. Phosphorylation plays a critical role in the regulation of the biological activities of proteins. However, phosphorylation-mediated regulation of proteins and pathways involved in ethylene (ET) and abscisic acid (ABA) signaling is currently poorly understood. Therefore, we used a shotgun proteomics approach to identify the phosphopeptides and phosphoproteins in response to ET, ABA and combined ET+ABA treatments. Here, we present the Mass spectrometry, protein–protein interaction, Gene ontology and KEGG data associated with the ET and ABA signaling in soybean leaves [1].
Highlights
The data reported here are associated with the article “Comparative phosphoproteome analysis upon ethylene and abscisic acid treatment in Glycine max leaves” [1]
Data Figures reported here depict the interaction network obtained from the identified phosphoproteins (Fig. 1), and functional annotation of the abscisic acid (ABA) and ET modulated phosphoproteins (Fig. 2) from soybean leaves
Gene Ontology (GO) and KEGG pathways was used for the functional annotation of the identified phosphoproteins
Summary
This dataset provides information about the 802 phosphopeptides, identified phosphosites and associated upstream kinase(s). The identified phosphopeptides, phosphosites and enriched motifs further supplement the known phosphoproteome map of soybean. Results reported here enhance our understanding of phosphorylation mediated regulation of ABA and ET responses to soybean leaves. Figures reported here depict the interaction network obtained from the identified phosphoproteins (Fig. 1), and functional annotation of the ABA and ET modulated phosphoproteins (Fig. 2) from soybean leaves. Detailed description of the data and methods is reported previously [1]
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