PTMint

PTMint curates experimentally supported post-translational modification (PTM) regulation of protein–protein interactions (PPIs) to enable comparative analysis of PTM effects on signaling, protein complexes, and disease associations.

Key Features:

• Comprehensive Data Collection: PTMint contains manually curated evidence of PTM regulation on PPIs for phosphorylation, acetylation, methylation, sumoylation, ubiquitylation, and glycosylation.
• Multi-Organism Coverage: The database includes entries for Homo sapiens, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Saccharomyces cerevisiae, and Schizosaccharomyces pombe.
• Extensive Annotations: PTMint integrates protein sequences, structural properties, and protein complex analyses.
• Disease Association: PTMint links 2477 non-redundant PTM sites in 1169 proteins to 2371 PPIs and associates these with 357 diseases.

Scientific Applications:

• Disease Mechanism Insights: The resource supports investigation of how PTMs regulate PPIs in diseases including cancer and neurologic disorders.
• Drug Discovery and Development: The mapped PTM sites and affected PPIs can be used to identify candidate targets for therapeutic development.
• Protein Function Regulation: The dataset enables study of PTM-driven modulation of protein function through altered PPIs and complex formation.

Methodology:

Data were compiled by rigorous manual curation of experimental evidence.