Protein complexes and functional modules in molecular networks

Protein complexes and functional modules in molecular networks

Copyright (c) 2003 Massachusetts Institute of Technology. All rights reserved.

Proteins, nucleic acids, and small molecules form a dense network of molecular interactions in a cell. Molecules are nodes of this network, and the interactions between them are edges. The architecture of molecular networks can reveal important principles of cellular organization and function, similarly to the way that protein structure tells us about the function and organization of a protein. Computational analysis of molecular networks has been primarily concerned with node degree [Wagner, A. & Fell, D. A. (2001) Proc. R. Soc. London Ser. B 268, 1803-1810; Jeong, H., Tombor, B., Albert, R., Oltvai, Z. N. & Barabasi, A. L. (2000) Nature 407, 651-654] or degree correlation [Maslov, S. & Sneppen, K. (2002) Science 296, 910-913], and hence focused on single/two-body properties of these networks. Here, by analyzing the multibody structure of the network of protein-protein interactions, we discovered molecular modules that are densely connected within themselves but sparsely connected with the rest of the network. Comparison with experimental data and functional annotation of genes showed two types of modules: (i) protein complexes (splicing machinery, transcription factors, etc.) and (ii) dynamic functional units (signaling cascades, cell-cycle regulation, etc.). Discovered modules are highly statistically significant, as is evident from comparison with random graphs, and are robust to noise in the data. Our results provide strong support for the network modularity principle introduced by Hartwell et al. [Hartwell, L. H., Hopfield, J. J., Leibler, S. & Murray, A. W. (1999) Nature 402, C47-C52], suggesting that found modules constitute the "building blocks" of molecular networks.

The full text of the paper can be found here.

This web site contains the lists of complexes and modules found by the methods described in the paper, the lists of complexes catalogued in the databases, comparisons of our results with experimental complexes, and predicted novel complexes.

List of complexes catalogued in the databases
All catalogued complexes   All complexes catalogued in MIPS, BIND, and Cellzome databases
Statistically significant complexes   Complexes catalogued in MIPS, BIND, and Cellzome databases with high number   of pairwise interations between proteins.
List of discovered complexes and functional modules
Triangles on the graph with excluded hubs   this list contains triangles on the graph with excluded nodes with high number   of connections.
Triangles on the graph with no nodes excluded   this list contains triangles
All statistically significant clusters   this list contains statistically significant clusters of all sizes larger than 3
Comparisons of discovered and catalogued complexes
Identified experimental complexes   Complexes in the databases which we identified
Best match   Best experimental match for all our clusters
List of predicted novel complexes and functional modules
Predicted clusters   this file contains predicted complexes and functional modules

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