EPSD

EPSD compiles and annotates experimentally validated eukaryotic protein phosphorylation sites to support analysis of phosphorylation-mediated protein function and regulation.

Key Features:

• Scope and content: Contains 1,616,804 experimentally validated phosphorylation sites across 209,326 phosphoproteins from 68 eukaryotic species.
• High-throughput contributions: Incorporates 1,451,629 phosphorylation sites newly identified from high-throughput mass spectrometry-based phosphoproteomic studies.
• Database integration: Integrates known phosphorylation sites from 13 external databases.
• Model organism annotations: Provides detailed annotations for phosphoproteins and phosphorylation sites in eight model organisms.
• Comprehensive annotation types: Annotations draw on information from 100 additional resources covering phosphorylation regulators, genetic variations, functional and structural annotations, physicochemical properties, functional domains, disease associations, protein–protein interactions, drug–target relationships, orthologous information, biological pathways, transcriptional regulators, mRNA expression, protein expression/proteomics, and subcellular localization.
• Data volume: Aggregated dataset size of 14.1 GB.

Scientific Applications:

• Phosphoproteomics data integration: Integration and analysis of mass spectrometry-based phosphoproteomics datasets.
• Functional interpretation: Interpretation of phosphorylation impacts on protein function and regulation.
• Cross-species comparison: Comparative and evolutionary analyses using data from 68 eukaryotic species and orthologous information.
• Disease and drug research: Investigation of disease associations and drug–target relationships involving phosphoproteins.
• Interaction and pathway analysis: Analysis of protein–protein interactions and biological pathways involving phosphorylation sites.

Methodology:

Collection, integration and curation of experimentally identified phosphorylation sites from high-throughput mass spectrometry-based phosphoproteomic studies and 13 external databases, with annotation sourced from 100 additional resources.