Background: Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes. The fast growing number of research reports on protein phosphorylation points to a general need for an accurate database dedicated to phosphorylation to provide easily retrievable information on phosphoproteins. Description: Phospho.ELM http://phospho.elm.eu.org is a new resource containing experimentally verified phosphorylation sites manually curated from the literature and is developed as part of the ELM (Eukaryotic Linear Motif) resource. Phospho.ELM constitutes the largest searchable collection of phosphorylation sites available to the research community. The Phospho.ELM entries store information about substrate proteins with the exact positions of residues known to be phosphorylated by cellular kinases. Additional annotation includes literature references, subcellular compartment, tissue distribution, and information about the signaling pathways involved as well as links to the molecular interaction database MINT. Phospho.ELM version 2.0 contains 1703 phosphorylation site instances for 556 phosphorylated proteins. Conclusion: Phospho.ELM will be a valuable tool both for molecular biologists working on protein phosphorylation sites and for bioinformaticians developing computational predictions on the specificity of phosphorylation reactions. © 2004 Diella et al; licensee BioMed Central Ltd.
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|Titolo:||Phospho.ELM: A database of experimentally verified phosphorylation sites in eukaryotic proteins|
|Data di pubblicazione:||2004|
|Citazione:||Phospho.ELM: A database of experimentally verified phosphorylation sites in eukaryotic proteins / F., Diella; S., Cameron; C., Gemund; R., Linding; Via, Allegra; B., Kuster; T., Sicheritz Ponten; N., Blom; T. J., Gibson. - In: BMC BIOINFORMATICS. - ISSN 1471-2105. - 5(2004), pp. 79-84.|
|Appartiene alla tipologia:||01a Articolo in rivista|