Phospho.ELM

Phospho.ELM curates a relational database of experimentally determined phosphorylation sites from in vivo and in vitro studies and phosphoproteomic analyses, comprising 42,574 non-redundant serine, threonine, and tyrosine phosphorylation sites.

Key Features:

• Extensive Data Repository: A comprehensive collection of 42,574 non-redundant phosphorylation sites on serine, threonine, and tyrosine residues derived from literature and phosphoproteomic analyses.
• Structural Disorder/Order Information: Annotates the local structural disorder or order at phosphorylation sites.
• Accessibility Data: Provides solvent accessibility information for individual phosphosites.
• Conservation Score: Reports a conservation score quantifying evolutionary conservation of phosphorylation sites across species.
• Multiple Sequence Alignment Visualization: Visualizes conservation of phosphosites on the multiple sequence alignments used to calculate conservation scores.
• Integration with External Resources: Links phosphorylation sites to interaction networks and other external databases.

Scientific Applications:

• Functional Annotation: Supports prediction and interpretation of phosphorylation site functional roles using structural and conservation context.
• Protein Interaction Studies: Enables analysis of how phosphorylation events may affect protein-protein interactions and signaling pathways via linked interaction data.
• Drug Discovery and Development: Informs targeting of kinase-substrate interactions by providing structural, accessibility, and conservation information for phosphosites.
• Systems Biology Approaches: Facilitates systems-level analyses of cellular signaling networks using a comprehensive, integrated phosphorylation dataset.

Methodology:

Data are stored in a relational database and curated from in vivo and in vitro studies and phosphoproteomic analyses; conservation scores are calculated from multiple sequence alignments used for visualization.