Scop3P

Scop3P provides a comprehensive, structure-aware resource of human phosphorylation sites (phosphosites) by integrating sequence, proteomics, structural, and biophysical annotations to support identification, annotation, and structure–function analysis of phosphosites.

Key Features:

• Integration of Diverse Data Sources: Integrates sequences from UniProtKB/Swiss-Prot, structural data from the Protein Data Bank (PDB), and uniformly reprocessed phosphoproteomics data from PRIDE into a unified dataset of human phosphosites.
• Contextual Annotation: Maps phosphosites onto protein structures to provide structural context for phosphorylation events.
• Biophysical Contextualization: Annotates each phosphoprotein with per-residue structural propensity, solvent accessibility, disordered probability, and early folding information.
• Experimental Provenance Information: Records experimental provenance linking phosphosite identifications to specific experiments.

Scientific Applications:

• Functional Analysis: Understanding how phosphorylation affects protein function and interaction networks.
• Disease Research: Investigating roles of specific phosphosites in disease mechanisms, including cancer and metabolic disorders.
• Drug Discovery: Identifying structurally contextualized phosphosites as potential therapeutic targets.

Methodology:

Systematic integration and uniform reprocessing of phosphoproteomics data from PRIDE combined with sequences from UniProtKB/Swiss-Prot and structural data from the Protein Data Bank (PDB), with mapping of phosphosites onto protein structures.