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DisProt: intrinsic protein disorder annotation in 2020
András Hatos1, Borbála Hajdu-Soltész2, Alexander M Monzon1
1Department of Biomedical Sciences, University of Padova, Padova 35121, Italy.
Nucleic Acids Research
|November 13, 2019
Summary
The DisProt database now has double the entries of intrinsically disordered proteins. This enhanced resource aids in understanding protein function and disorder, illuminating the
Area of Science:
- Proteomics
- Bioinformatics
- Structural Biology
Background:
- Intrinsically disordered proteins (IDPs) lack stable 3D structures, playing crucial roles in cellular regulation.
- Manual curation of IDP literature is essential for building reliable databases.
- The DisProt database serves as a key resource for IDP information.
Purpose of the Study:
- To report recent developments and improvements in the DisProt database (version 8).
- To enhance the accessibility, usability, and data richness of the DisProt resource.
- To facilitate the study and prediction of protein disorder.
Main Methods:
- Manual curation of intrinsically disordered protein annotations from scientific literature.
- Development of a new, formalized disorder ontology in OWL format.
- Implementation of a redesigned website with improved search, API, and annotation interfaces.
- Integration of text mining technologies into the annotation process.
Main Results:
- DisProt database entries have doubled in version 8.
- A new, interoperable disorder ontology has been implemented.
- The website features a redesigned interface, enhanced search, and clearer API.
- The new annotation interface streamlines curation and integrates text mining.
Conclusions:
- The updated DisProt database offers a more comprehensive and user-friendly resource for intrinsically disordered proteins.
- Improvements facilitate faster and more effective curation, accelerating data growth.
- Enhanced DisProt data can improve disorder prediction tools, aiding in the exploration of the 'dark proteome'.
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