PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells
Open Access
- 1 January 2007
- journal article
- review article
- Published by Springer Nature in Molecular Systems Biology
- Vol. 3 (1) , 139
- https://doi.org/10.1038/msb4100182
Abstract
The ability to analyze and understand the mechanisms by which cells process information is a key question of systems biology research. Such mechanisms critically depend on reversible phosphorylation of cellular proteins, a process that is catalyzed by protein kinases and phosphatases. Here, we present PhosphoPep, a database containing more than 10 000 unique high‐confidence phosphorylation sites mapping to nearly 3500 gene models and 4600 distinct phosphoproteins of the Drosophila melanogaster Kc167 cell line. This constitutes the most comprehensive phosphorylation map of any single source to date. To enhance the utility of PhosphoPep, we also provide an array of software tools that allow users to browse through phosphorylation sites on single proteins or pathways, to easily integrate the data with other, external data types such as protein–protein interactions and to search the database via spectral matching. Finally, all data can be readily exported, for example, for targeted proteomics approaches and the data thus generated can be again validated using PhosphoPep, supporting iterative cycles of experimentation and analysis that are typical for systems biology research.Keywords
This publication has 60 references indexed in Scilit:
- Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometryNature Methods, 2007
- Large‐scale mapping of human protein–protein interactions by mass spectrometryMolecular Systems Biology, 2007
- A uniform proteomics MS/MS analysis platform utilizing open XML file formatsMolecular Systems Biology, 2005
- Mass spectrometry-based proteomicsNature, 2003
- Empirical Statistical Model To Estimate the Accuracy of Peptide Identifications Made by MS/MS and Database SearchAnalytical Chemistry, 2002
- Functional organization of the yeast proteome by systematic analysis of protein complexesNature, 2002
- Genomic binding sites of the yeast cell-cycle transcription factors SBF and MBFNature, 2001
- Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. CohenJournal of Molecular Biology, 2001
- An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein databaseJournal of the American Society for Mass Spectrometry, 1994
- A novel genetic system to detect protein–protein interactionsNature, 1989