Extreme multifunctional proteins identified from a human protein interaction network

Charles E. Chapple, Benoit Robisson, Lionel Spinelli, Céline Guien, Emmanuelle Becker and Christine Brun ()
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Charles E. Chapple: Aix-Marseille University, TAGC
Benoit Robisson: Aix-Marseille University, TAGC
Lionel Spinelli: Aix-Marseille University, TAGC
Céline Guien: Aix-Marseille University, TAGC
Emmanuelle Becker: Aix-Marseille University, TAGC
Christine Brun: Aix-Marseille University, TAGC

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: Abstract Moonlighting proteins are a subclass of multifunctional proteins whose functions are unrelated. Although they may play important roles in cells, there has been no large-scale method to identify them, nor any effort to characterize them as a group. Here, we propose the first method for the identification of ‘extreme multifunctional’ proteins from an interactome as a first step to characterize moonlighting proteins. By combining network topological information with protein annotations, we identify 430 extreme multifunctional proteins (3% of the human interactome). We show that the candidates form a distinct sub-group of proteins, characterized by specific features, which form a signature of extreme multifunctionality. Overall, extreme multifunctional proteins are enriched in linear motifs and less intrinsically disordered than network hubs. We also provide MoonDB, a database containing information on all the candidates identified in the analysis and a set of manually curated human moonlighting proteins.

Date: 2015
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DOI: 10.1038/ncomms8412

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