title: Sequence- and Structure-Based Analysis of Tissue-Specific Phosphorylation Sites.
abstract: Phosphorylation is the most widespread and well studied reversible posttranslational modification. Discovering tissue-specific preferences of phosphorylation sites is important as phosphorylation plays a role in regulating almost every cellular activity and disease state. Here we present a comprehensive analysis of global and tissue-specific sequence and structure properties of phosphorylation sites utilizing recent proteomics data. We identified tissue-specific motifs in both sequence and spatial environments of phosphorylation sites. Target site preferences of kinases across tissues indicate that, while many kinases mediate phosphorylation in all tissues, there are also kinases that exhibit more tissue-specific preferences which, notably, are not caused by tissue-specific kinase expression. We also demonstrate that many metabolic pathways are differentially regulated by phosphorylation in different tissues.
authors.affiliation: Department of Genome Oriented Bioinformatics, Technische Universität München, Freising, Germany.
authors.forename: Nermin Pinar
authors.initials: NP
authors.lastname: Karabulut
authors.affiliation: Department of Genome Oriented Bioinformatics, Technische Universität München, Freising, Germany.|Helmholtz Zentrum Munich; German Research Center for Environmental Health (GmbH), Institute of Bioinformatics and Systems Biology, Neuherberg, Germany.|St Petersburg State Polytechnical University, St Petersburg, Russia.
authors.forename: Dmitrij
authors.initials: D
authors.lastname: Frishman
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D030562:Databases, Protein; D053858:Metabolic Networks and Pathways; D008958:Models, Molecular; D009928:Organ Specificity; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism
chemical_list: D010750:Phosphoproteins; D011494:Protein Kinases