Large-scale discovery and characterization of protein regulatory motifs in eukaryotes.

• Main Authors: Daniel S Lieber, Olivier Elemento, Saeed Tavazoie
• Format: Article
• Language: English
• Published: Public Library of Science (PLoS) 2010-12-01
• Series: PLoS ONE
• Online Access: http://europepmc.org/articles/PMC3012054?pdf=render

The increasing ability to generate large-scale, quantitative proteomic data has brought with it the challenge of analyzing such data to discover the sequence elements that underlie systems-level protein behavior. Here we show that short, linear protein motifs can be efficiently recovered from proteome-scale datasets such as sub-cellular localization, molecular function, half-life, and protein abundance data using an information theoretic approach. Using this approach, we have identified many known protein motifs, such as phosphorylation sites and localization signals, and discovered a large number of candidate elements. We estimate that ~80% of these are novel predictions in that they do not match a known motif in both sequence and biological context, suggesting that post-translational regulation of protein behavior is still largely unexplored. These predicted motifs, many of which display preferential association with specific biological pathways and non-random positioning in the linear protein sequence, provide focused hypotheses for experimental validation.