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Updated: May 5, 2026

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Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
Published on: October 12, 2009
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An AI-Ready Phosphorylation Meta-Analysis for Saccharomyces cerevisiae.
Ellen L Boswell1, Kerry A Ramsbottom1, Jun Fan2
1Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 7BE, U.K.
Journal of Proteome Research
|May 4, 2026
Summary
This study mapped 56,694 phosphosites in yeast, finding phosphorylation often occurs on disordered residues. The high-quality data is FAIR and AI-ready for future proteomics research.
Area of Science:
- Proteomics
- Yeast Biology
- Post-Translational Modifications
Background:
- Phosphorylation is a key post-translational modification (PTM) regulating cellular processes.
- Accurate mapping of phosphosites is crucial for understanding kinase signaling networks.
- High-quality, accessible data is essential for advancing artificial intelligence (AI) in proteomics.
Purpose of the Study:
- To create a comprehensive map of phosphosites in Saccharomyces cerevisiae.
- To analyze the structural context and sequence motifs of identified phosphosites.
- To ensure data quality and accessibility for AI-driven proteomics research.
Main Methods:
- Meta-analysis of eight high-quality datasets, identifying 56,694 phosphosites with strict false discovery rate control.
- Classification of phosphosites into Gold, Silver, and Bronze confidence categories.
- Utilized disorder region predictions and AlphaFold 3 for structural context analysis of phosphosites.
Main Results:
- Identified 56,694 phosphosites in Saccharomyces cerevisiae, classified by confidence.
- Discovered 55 significant phosphorylation motifs, grouped into kinase classes for pathway enrichment.
- Phosphorylation predominantly occurs on disordered serine and threonine residues, potentially inducing short alpha helices.
Conclusions:
- The study provides a high-confidence, comprehensive phosphosite map of Saccharomyces cerevisiae.
- Phosphorylation sites are frequently located in disordered regions and influence protein structure.
- The FAIR and AI-ready dataset (PRIDE: PXD071918) supports downstream analyses and AI model training in proteomics.

