title: DAPPLE 2: a Tool for the Homology-Based Prediction of Post-Translational Modification Sites.
abstract: The post-translational modification of proteins is critical for regulating their function. Although many post-translational modification sites have been experimentally determined, particularly in certain model organisms, experimental knowledge of these sites is severely lacking for many species. Thus, it is important to be able to predict sites of post-translational modification in such species. Previously, we described DAPPLE, a tool that facilitates the homology-based prediction of one particular post-translational modification, phosphorylation, in an organism of interest using known phosphorylation sites from other organisms. Here, we describe DAPPLE 2, which expands and improves upon DAPPLE in three major ways. First, it predicts sites for many post-translational modifications (20 different types) using data from several sources (15 online databases). Second, it has the ability to make predictions approximately 2-7 times faster than DAPPLE depending on the database size and the organism of interest. Third, it simplifies and accelerates the process of selecting predicted sites of interest by categorizing them based on gene ontology terms, keywords, and signaling pathways. We show that DAPPLE 2 can successfully predict known human post-translational modification sites using, as input, known sites from species that are either closely (e.g., mouse) or distantly (e.g., yeast) related to humans. DAPPLE 2 can be accessed at http://saphire.usask.ca/saphire/dapple2 .
authors.affiliation: Vaccine and Infectious Disease Organization, ‡Department of Computer Science, and §Department of Biochemistry, University of Saskatchewan , Saskatoon, SK S7N 5A2, Canada.
authors.forename: Brett
authors.initials: B
authors.lastname: Trost
authors.affiliation: Vaccine and Infectious Disease Organization, ‡Department of Computer Science, and §Department of Biochemistry, University of Saskatchewan , Saskatoon, SK S7N 5A2, Canada.
authors.forename: Farhad
authors.initials: F
authors.lastname: Maleki
authors.affiliation: Vaccine and Infectious Disease Organization, ‡Department of Computer Science, and §Department of Biochemistry, University of Saskatchewan , Saskatoon, SK S7N 5A2, Canada.
authors.forename: Anthony
authors.initials: A
authors.lastname: Kusalik
authors.affiliation: Vaccine and Infectious Disease Organization, ‡Department of Computer Science, and §Department of Biochemistry, University of Saskatchewan , Saskatoon, SK S7N 5A2, Canada.
authors.forename: Scott
authors.initials: S
authors.lastname: Napper
mesh_terms: D000818:Animals; D001665:Binding Sites; D030562:Databases, Protein; D006801:Humans; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid; D012984:Software
keywords: acetylation; cross-species comparisons; glycosylation; homology; methylation; nitrosylation; phosphorylation; post-translational modifications; ubiquitination