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Updated: May 11, 2026

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
Published on: October 12, 2009
The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update
Ivan Sadowski1, Bobby-Joe Breitkreutz, Chris Stark
1Department of Biochemistry and Molecular Biology, Molecular Epigenetics, Life Sciences Institute, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia, Canada V6T 1Z3. ijs.ubc@gmail.com
PhosphoGRID 2.0 significantly expands its curated database of yeast phosphorylation sites, integrating new high-throughput studies. This comprehensive resource aids in understanding yeast cell signaling networks.
Area of Science:
- Proteomics
- Yeast molecular biology
- Post-translational modifications
Background:
- Phosphorylation is a key post-translational modification regulating protein function.
- Understanding phosphorylation networks is crucial for deciphering cellular signaling pathways.
- The Saccharomyces cerevisiae proteome offers a model system for studying fundamental cellular processes.
Purpose of the Study:
- To update and expand the PhosphoGRID database with new experimentally verified in vivo phosphorylation sites.
- To provide comprehensive annotations for phosphosites, including associated kinases/phosphatases and functional effects.
- To facilitate the development of predictive models for phosphorylation-based signaling networks.
Main Methods:
- Curating and integrating data from high-throughput (HTP) mass spectrometry studies.
- Incorporating data from focused low-throughput (LTP) studies.
- Annotating phosphosites with protein kinases, phosphatases, conditions, and functional impacts.
Main Results:
- The PhosphoGRID version 2.0 dataset includes 20,177 unique phosphorylated residues and 1,614 unique phosphosites from LTP studies.
- This represents a four-fold increase in unique phosphorylated residues compared to version 1.0.
- A significant overlap exists between HTP and LTP data, with 45% of functionally defined LTP sites found in at least two HTP studies.
Conclusions:
- The expanded PhosphoGRID database provides a rich resource for yeast phosphoproteomics research.
- The near-saturation of phosphoprotein coverage suggests a comprehensive understanding of yeast phosphorylation.
- Integration of HTP and LTP data holds promise for building predictive models of cellular signaling.
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