Nucleic Acids Research Advance Access originally published online on November 16, 2006
Nucleic Acids Research 2007 35(Database issue):D229-D231; doi:10.1093/nar/gkl922
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Nucleic Acids Research, 2007, Vol. 35, Database issue D229-D231
© 2006 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.
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Phospho3D: a database of three-dimensional structures of protein phosphorylation sites
Centre for Molecular Bioinformatics, Department of Biology University of Rome Tor Vergata, Rome 00133, Italy
*To whom correspondence should be addressed. Tel: +39 067 259 4314; Fax: +39 062 023 500; Email: andreas{at}cbm.bio.uniroma2.it
Received August 11, 2006. Revised October 13, 2006. Accepted October 17, 2006.
Phosphorylation is the most common protein post-translational modification. Phosphorylated residues (serine, threonine and tyrosine) play critical roles in the regulation of many cellular processes. Since the amount of data produced by screening assays is growing continuously, the development of computational tools for collecting and analysing experimental data has become a pivotal task for unravelling the complex network of interactions regulating eukaryotic cell life. Here we present Phospho3D, http://cbm.bio.uniroma2.it/phospho3d, a database of 3D structures of phosphorylation sites, which stores information retrieved from the phospho.ELM database and is enriched with structural information and annotations at the residue level. The database also collects the results of a large-scale structural comparison procedure providing clues for the identification of new putative phosphorylation sites.
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