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. 2002 Jan 1;30(1):303-5.
doi: 10.1093/nar/30.1.303.

DIP, the Database of Interacting Proteins: a research tool for studying cellular networks of protein interactions

Ioannis Xenarios  1 , Lukasz Salwínski, Xiaoqun Joyce Duan, Patrick Higney, Sul-Min Kim, David Eisenberg
Affiliations

DIP, the Database of Interacting Proteins: a research tool for studying cellular networks of protein interactions

Ioannis Xenarios et al. Nucleic Acids Res. .

Abstract

The Database of Interacting Proteins (DIP: http://dip.doe-mbi.ucla.edu) is a database that documents experimentally determined protein-protein interactions. It provides the scientific community with an integrated set of tools for browsing and extracting information about protein interaction networks. As of September 2001, the DIP catalogs approximately 11 000 unique interactions among 5900 proteins from >80 organisms; the vast majority from yeast, Helicobacter pylori and human. Tools have been developed that allow users to analyze, visualize and integrate their own experimental data with the information about protein-protein interactions available in the DIP database.

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Figures

Figure 1
Figure 1
Three illustrations of protein interactions and their descriptions by machine readable text of the sort that would automate database entry. (A) A set of four proteins (A, B, C and D) have been studied and shown to interact by a given method. The condensed text is shown below. (B) Example of the SWI6–SWI4 interactions observed by Siegmund and Nasmyth (15) using immunoprecipitation, copurification and in vitro binding. In this case the protein PIR codes are used RGBYW6 for SWI6p and S50614 for SWI4p. (C) Example of the Zip3 interactions demonstrated by two-hybrid screen and immunoprecipitation by Agarwal and Roeder (16). In this case S55950 (Zip3p) can be immunoprecipitated with RA57p (RA57_YEAST), MR11p (MR11_YEAST) and Zip2p (YGZ9_YEAST). Two-hybrid screen was performed and showed interactions of Zip3p with ZIP1p, MSH5p, RAD57p, RAD51p.
See this image and copyright information in PMC

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