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
Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Mol Syst Biol. 2007;3:139. doi: 10.1038/msb4100182. Epub 2007 Oct 16.
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.
分析和理解细胞处理信息机制的能力是系统生物学研究的关键问题。此类机制严重依赖于细胞蛋白质的可逆磷酸化,这一过程由蛋白激酶和磷酸酶催化。在此,我们展示了PhosphoPep数据库,其包含一万多个独特的高可信度磷酸化位点,这些位点映射到近3500个基因模型以及果蝇Kc167细胞系的4600种不同的磷酸化蛋白质。这构成了迄今为止任何单一来源最全面的磷酸化图谱。为提高PhosphoPep的实用性,我们还提供了一系列软件工具,允许用户浏览单个蛋白质或信号通路中的磷酸化位点,轻松将数据与其他外部数据类型(如蛋白质 - 蛋白质相互作用)整合,并通过光谱匹配搜索数据库。最后,所有数据都可轻松导出,例如用于靶向蛋白质组学方法,由此产生的数据又可使用PhosphoPep再次验证,支持系统生物学研究中典型的实验和分析迭代循环。