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DisProt in 2026: enhancing intrinsically disordered proteins accessibility, deposition, and annotation
Maria Victoria Nugnes1, Kamel Eddine Adel Bouhraoua1, Mehdi Zoubiri1
1Department of Biomedical Sciences, University of Padova, Padova 35131, Italy.
DisProt, a database for intrinsically disordered proteins (IDPs), has expanded its evidence and features. It now integrates computational predictions and enhances data accessibility for researchers studying protein disorder.
Area of Science:
- Biochemistry
- Bioinformatics
- Structural Biology
Background:
- Intrinsically disordered proteins (IDPs) and regions (IDRs) lack stable 3D structures, playing crucial roles in cellular functions.
- Databases like DisProt are essential for curating and disseminating experimental evidence on IDPs and IDRs.
- The growing body of research on IDPs necessitates continuous updates and improvements in data management and accessibility.
Purpose of the Study:
- To present the latest release of the DisProt database, highlighting its growth and new features.
- To improve the integration and accessibility of experimental data on intrinsically disordered proteins and regions.
- To enhance the utility of DisProt for researchers through new functionalities and data expansion.
Main Methods:
- Systematic adoption of Minimum Information About Disorder Experiments (MIADE) guidelines for detailed annotation.
- Expansion of DisProt data through BLAST-based homology propagation in MobiDB.
- Integration of computational predictions as valid evidence alongside experimental data.
- Updates and restructuring of the Intrinsically Disordered Protein (IDP) Ontology.
Main Results:
- DisProt now contains 3201 IDPs and 13,347 pieces of evidence, with over 1500 new structural state and 1300 new function annotations.
- MIADE adoption has more than doubled annotations with experimental details, improving interpretability.
- Disorder regions and interacting peptides have been extended to hundreds of thousands of proteins via homology propagation.
- The database now integrates computational predictions and features an updated IDP Ontology for enhanced accuracy and interoperability.
Conclusions:
- The enhanced DisProt database offers a more comprehensive and accessible resource for studying intrinsically disordered proteins.
- New features, including integrated computational predictions and an updated ontology, improve data accuracy and semantic clarity.
- DisProt's evolution into a hybrid knowledgebase and deposition system, alongside community engagement tools, supports broader research participation.
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