Nucleic Acids Research Advance Access originally published online on October 17, 2008
Nucleic Acids Research 2009 37(Database issue):D960-D962; doi:10.1093/nar/gkn733
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Nucleic Acids Research, 2009, Vol. 37, Database issue D960-D962
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
This article appears in the following Nucleic Acids Research issue: Database issue [View the issue table of contents]
Articles |
P3DB: a plant protein phosphorylation database
1Department of Computer Science, 2Department of Biochemistry and 3C.S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA
*To whom correspondence should be addressed. Tel: +1 573 884 1887; Fax: +1 573 882 8318; Email: xudong{at}missouri.edu
Received August 15, 2008. Revised September 30, 2008. Accepted October 1, 2008.
P3DB (http://www.p3db.org/) provides a resource of protein phosphorylation data from multiple plants. The database was initially constructed with a dataset from oilseed rape, including 14 670 nonredundant phosphorylation sites from 6382 substrate proteins, representing the largest collection of plant phosphorylation data to date. Additional protein phosphorylation data are being deposited into this database from large-scale studies of Arabidopsis thaliana and soybean. Phosphorylation data from current literature are also being integrated into the P3DB. With a web-based user interface, the database is browsable, downloadable and searchable by protein accession number, description and sequence. A BLAST utility was integrated and a phosphopeptide BLAST browser was implemented to allow users to query the database for phosphopeptides similar to protein sequences of their interest. With the large-scale phosphorylation data and associated web-based tools, P3DB will be a valuable resource for both plant and nonplant biologists in the field of protein phosphorylation.