Phospho.ELM: a database of phosphorylation sites--update 2008

Area of Science:

• Molecular Biology
• Biochemistry
• Proteomics

Background:

• Phosphorylation is a critical post-translational modification regulating numerous cellular processes.
• Identifying and cataloging phosphorylation sites is essential for understanding cell signaling and disease.

Purpose of the Study:

• To present the updated Phospho.ELM database (version 7.0) as a comprehensive resource for eukaryotic phosphorylation data.
• To provide researchers with detailed information on phosphorylation sites, responsible kinases, and integrated external database links.

Main Methods:

• Manual curation of data from published literature and high-throughput studies.
• Inclusion of data on phospho-serine, phospho-threonine, and phospho-tyrosine sites.
• Development of a BLAST search tool for querying phosphorylated peptides.

Main Results:

• The database contains 4078 phospho-protein sequences with 12,025 phospho-serine, 2,362 phospho-threonine, and 2,083 phospho-tyrosine sites.
• Entries include protein information, modification positions, responsible kinases (where known), and bibliographic references.
• Integrated links to UniProt, PubMed, SMART, ELM, MSD, MINT, and STRING databases enhance data accessibility.

Conclusions:

• Phospho.ELM serves as a valuable, manually curated resource for eukaryotic phosphorylation.
• The database facilitates research in cell signaling, molecular biology, and drug discovery by providing integrated and searchable phosphorylation data.