※ Overview
    As one of the most important and ubiquitous post-translational modifications (PTMs) in plants, the reversible phosphorylation catalyzed by protein kinases is involved in regulating a wide range of biological processes such as cellular metabolism, signal transduction and environmental response (Ranjeva et al., 1987; Mundy et al., 2002; Kusakina et al., 2012). Recently with the development of phosphopeptide enrichment techniques and high-throughput mass spectrometry (HTP-MS) technology, large scale phosphoproteomics data in plants have been emerged at a quick pace, stimulating the creation of multiple phosphorylation databases to store and organize them. However, a more comprehensive phosphorylation database of plants is still necessary and useful. In this work, we develop a database of dbPPT 1.0 (database of Phospho-sites in PlanTs), which contains large-scale phosphorylation sites (p-sites) based on mass spectrometry across 20 plant species. Most of the datasets in dbPPT 1.0 were manually curated from literature published before July, 2014. Moreover, we also integrated other phosphorylation resource into this database including PhosPhAt (Durek et al., 2010) and P3DB (Yao et al., 2014). Currently, dbPPT contains 82,175 p-sites in 31,012 proteins for 20 plant species.



            


                  


For publication of results please cite the following articles:


dbPPT: a comprehensive database of protein phosphorylation in plants
Han Cheng, Wankun Deng, Yongbo Wang, Jian Ren, Zexian Liu and Yu Xue.
Database, 2014, 2014: bau121
[Abstract] [FREE Full Text] [PDF][Supplementary Data]