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Sequence- and structure-based analysis of tissue-specific phosphorylation sites.
PLoS ONE 11:e0157896 (2016)
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.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Lysine Acetylation Sites; Protein-phosphorylation; Prediction; Kinase; Substrate; Database; Mouse; Motifs; Sets; Identification
ISSN (print) / ISBN
1932-6203
Journal
PLoS ONE
Quellenangaben
Volume: 11,
Issue: 6,
Article Number: e0157896
Publisher
Public Library of Science (PLoS)
Publishing Place
Lawrence, Kan.
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Peer reviewed