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Updated: May 23, 2026
09:16
Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
PhosphoSiteAnalyzer: a bioinformatic platform for deciphering phospho proteomes using kinase predictions retrieved
Martin V Bennetzen1, Jürgen Cox, Matthias Mann
1Center for Experimental BioInformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark , Odense, Campusvej 55, DK-5230 Odense M, Denmark.
Journal of Proteome Research
|April 5, 2012
Summary
PhosphoSiteAnalyzer is a new freeware tool that analyzes large phosphoproteomic datasets. It integrates kinase predictions from NetworKIN to help researchers explore complex phosphorylation site data.
Area of Science:
- Biochemistry
- Bioinformatics
- Systems Biology
Background:
- Phosphoproteomic experiments generate vast datasets of phosphorylation sites.
- Analyzing these large datasets requires advanced computational and statistical methods.
Purpose of the Study:
- To introduce PhosphoSiteAnalyzer, an advanced bioinformatic platform for exploring large phosphoproteomic datasets.
- To integrate kinase prediction data from the NetworKIN algorithm for in-depth analysis.
Main Methods:
- Development of the PhosphoSiteAnalyzer software.
- Semiautomated retrieval of kinase predictions from the NetworKIN public webpage.
- Application of advanced statistical methods for data analysis.
Main Results:
- PhosphoSiteAnalyzer facilitates user-tailored analysis of phosphoproteomic data.
- The platform integrates kinase-substrate associations predicted by NetworKIN.
- The software offers a high degree of analytical flexibility and an intuitive interface.
Conclusions:
- PhosphoSiteAnalyzer is a valuable freeware tool for researchers working with large phosphoproteomic datasets.
- The platform enhances the exploration of phosphorylation sites by incorporating kinase prediction data.
- It empowers users to answer complex biological questions from their data.
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Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
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During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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