Related Experiment Video
Updated: May 20, 2026
09:39
Mapping Dysfunctional Protein-Protein Interactions in Disease
Published on: October 24, 2025
A functional map of the human intrinsically disordered proteome
Iva Pritišanac1,2,3,4, T Reid Alderson5,6, Đesika Kolarić5,6
1Department of Cell and Systems Biology, University of Toronto, Toronto, ON M5S 3G5, Canada.
Summary
Evolutionarily conserved features within intrinsically disordered regions (IDRs) allow for functional classification of the human disordered proteome (IDRome). This new map aids in understanding IDR biology and disease-associated proteins.
Area of Science:
- Proteomics
- Bioinformatics
- Genomics
Background:
- Intrinsically disordered regions (IDRs) comprise a significant portion of the human proteome, challenging traditional structure-function relationships.
- Limited sequence conservation in IDRs hinders functional classification using standard bioinformatics approaches.
Purpose of the Study:
- To develop a method for functionally classifying intrinsically disordered regions (IDRs) based on conserved molecular features.
- To create a comprehensive map of the human disordered proteome (IDRome) with functional enrichments.
Main Methods:
- Analysis of evolutionary conservation patterns within IDRs.
- Clustering of the human disordered proteome based on conserved IDR features.
- Correlation of conserved IDR features with functional annotations and protein localization.
Main Results:
- Demonstrated that conserved molecular features of IDRs enable functional clustering of the human disordered proteome.
- Quantified the correlation between conserved IDR features and functional terms, enabling proteome-wide annotation predictions.
- Showcased the ability of conserved IDR features to predict protein localization to biomolecular condensates and identify associated interaction partners.
Conclusions:
- Conserved features of intrinsically disordered regions (IDRs) provide a powerful means for functional classification and annotation.
- The developed map of the human IDR-ome offers a valuable resource for exploring IDR biology, including disease-associated proteins.
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