DisEnrich: database of enriched regions in human dark proteome

Motivation: Intrinsically disordered proteins (IDPs) are involved in numerous processes crucial for living organisms. Bias in amino acid composition of these proteins determines their unique biophysical and functional features. Distinct intrinsically disordered regions (IDRs) with compositional bias play different important roles in various biological processes. IDRs enriched in particular amino acids in human proteome have not been described consistently. Results: We developed DisEnrich-the database of human proteome IDRs that are significantly enriched in particular amino acids. Each human protein is described using Gene Ontology (GO) function terms, disorder prediction for the full-length sequence using three methods, enriched IDR composition and ranks of human proteins with similar enriched IDRs. Distribution analysis of enriched IDRs among broad functional categories revealed significant overrepresentation of R- and Y-enriched IDRs in metabolic and enzymatic activities and F-enriched IDRs in transport. About 75% of functional categories contain IDPs with IDRs significantly enriched in hydrophobic residues that are important for protein-protein interactions.

Automated summary

This study developed a database of human proteome IDRs that are significantly enriched in particular amino acids, providing information on function terms, disorder prediction, enriched IDR composition, and ranks of human proteins with similar enriched IDRs. The distribution analysis revealed significant overrepresentation of R- and Y-enriched IDRs in metabolic and enzymatic activities, and F-enriched IDRs in transport. Approximately 75% of functional categories contain IDPs with IDRs significantly enriched in hydrophobic residues important for protein-protein interactions.