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PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells
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 prese...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063582/ https://www.ncbi.nlm.nih.gov/pubmed/17940529 http://dx.doi.org/10.1038/msb4100182 |
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author | Bodenmiller, Bernd Malmstrom, Johan Gerrits, Bertran Campbell, David Lam, Henry Schmidt, Alexander Rinner, Oliver Mueller, Lukas N Shannon, Paul T Pedrioli, Patrick G Panse, Christian Lee, Hoo-Keun Schlapbach, Ralph Aebersold, Ruedi |
author_facet | Bodenmiller, Bernd Malmstrom, Johan Gerrits, Bertran Campbell, David Lam, Henry Schmidt, Alexander Rinner, Oliver Mueller, Lukas N Shannon, Paul T Pedrioli, Patrick G Panse, Christian Lee, Hoo-Keun Schlapbach, Ralph Aebersold, Ruedi |
author_sort | Bodenmiller, Bernd |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2063582 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-20635822007-11-06 PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells Bodenmiller, Bernd Malmstrom, Johan Gerrits, Bertran Campbell, David Lam, Henry Schmidt, Alexander Rinner, Oliver Mueller, Lukas N Shannon, Paul T Pedrioli, Patrick G Panse, Christian Lee, Hoo-Keun Schlapbach, Ralph Aebersold, Ruedi Mol Syst Biol Report 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. Nature Publishing Group 2007-10-16 /pmc/articles/PMC2063582/ /pubmed/17940529 http://dx.doi.org/10.1038/msb4100182 Text en Copyright © 2007, EMBO and Nature Publishing Group http://creativecommons.org/licenses/by-nc-nd/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation or the creation of derivative works without specific permission. |
spellingShingle | Report Bodenmiller, Bernd Malmstrom, Johan Gerrits, Bertran Campbell, David Lam, Henry Schmidt, Alexander Rinner, Oliver Mueller, Lukas N Shannon, Paul T Pedrioli, Patrick G Panse, Christian Lee, Hoo-Keun Schlapbach, Ralph Aebersold, Ruedi PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells |
title | PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells |
title_full | PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells |
title_fullStr | PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells |
title_full_unstemmed | PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells |
title_short | PhosphoPep—a phosphoproteome resource for systems biology research in Drosophila Kc167 cells |
title_sort | phosphopep—a phosphoproteome resource for systems biology research in drosophila kc167 cells |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063582/ https://www.ncbi.nlm.nih.gov/pubmed/17940529 http://dx.doi.org/10.1038/msb4100182 |
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