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Nucleic Acids Research 2006 34(Database Issue):D436-D441; doi:10.1093/nar/gkj003
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Nucleic Acids Research, 2006, Vol. 34, Database issue D436-D441
© The Author 2006. Published by Oxford University Press. All rights reserved
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Article

MPact: the MIPS protein interaction resource on yeast

Ulrich Güldener1,*, Martin Münsterkötter1, Matthias Oesterheld1, Philipp Pagel1, Andreas Ruepp1, Hans-Werner Mewes1,2 and Volker Stümpflen1

1Institute for Bioinformatics, GSF National Research Center for Environment and Health Ingolstädter Landstrasse 1, D-85764 Neuherberg, Germany 2Technische Universität München, Chair of Genome Oriented Bioinformatics, Center of Life and Food Science D-85350 Freising-Weihenstephan, Germany

*To whom correspondence should be addressed. Tel: +49 89 3187 3579; Fax: +49 89 3187 3585; Email: u.gueldener{at}gsf.de

Received May 23, 2005. Revised July 28, 2005. Accepted July 28, 2005.

In recent years, the Munich Information Center for Protein Sequences (MIPS) yeast protein–protein interaction (PPI) dataset has been used in numerous analyses of protein networks and has been called a gold standard because of its quality and comprehensiveness [H. Yu, N. M. Luscombe, H. X. Lu, X. Zhu, Y. Xia, J. D. Han, N. Bertin, S. Chung, M. Vidal and M. Gerstein (2004) Genome Res., 14, 1107–1118]. MPact and the yeast protein localization catalog provide information related to the proximity of proteins in yeast. Beside the integration of high-throughput data, information about experimental evidence for PPIs in the literature was compiled by experts adding up to 4300 distinct PPIs connecting 1500 proteins in yeast. As the interaction data is a complementary part of CYGD, interactive mapping of data on other integrated data types such as the functional classification catalog [A. Ruepp, A. Zollner, D. Maier, K. Albermann, J. Hani, M. Mokrejs, I. Tetko, U. Güldener, G. Mannhaupt, M. Münsterkötter and H. W. Mewes (2004) Nucleic Acids Res., 32, 5539–5545] is possible. A survey of signaling proteins and comparison with pathway data from KEGG demonstrates that based on these manually annotated data only an extensive overview of the complexity of this functional network can be obtained in yeast. The implementation of a web-based PPI-analysis tool allows analysis and visualization of protein interaction networks and facilitates integration of our curated data with high-throughput datasets. The complete dataset as well as user-defined sub-networks can be retrieved easily in the standardized PSI-MI format. The resource can be accessed through http://mips.gsf.de/genre/proj/mpact.


The authors wish it to be known that, in their opinion, the first three authors should be regarded as joint First Authors


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