DisProt in 2024: improving function annotation of intrinsically disordered proteins

DisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions. The latest version of DisProt brings significant advancements, including a broader representation of functions and an enhanced curation process. These improvements aim to increase both the quality of annotations and their coverage at the sequence level. Higher coverage has been achieved by adopting additional evidence codes. Quality of annotations has been improved by systematically applying Minimum Information About Disorder Experiments (MIADE) principles and reporting all the details of the experimental setup that could potentially influence the structural state of a protein. The DisProt database now includes new thematic datasets and has expanded the adoption of Gene Ontology terms, resulting in an extensive functional repertoire which is automatically propagated to UniProtKB. Finally, we show that DisProt's curated annotations strongly correlate with disorder predictions inferred from AlphaFold2 pLDDT (predicted Local Distance Difference Test) confidence scores. This comparison highlights the utility of DisProt in explaining apparent uncertainty of certain well-defined predicted structures, which often correspond to folding-upon-binding fragments. Overall, DisProt serves as a comprehensive resource, combining experimental evidence of disorder information to enhance our understanding of intrinsically disordered proteins and their functional implications.Fil: Aspromonte, Maria Cristina. Università di Padova; ItaliaFil: Nugnes, María Victoria. Università di Padova; Italia. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Quaglia, Federica. Università di Padova; ItaliaFil: Bouharoua, Adel. Università di Padova; ItaliaFil: Sagris, Vasileios. UNIVERSITY OF CYPRUS (UC);Fil: Promponas, Vasilis J.. UNIVERSITY OF CYPRUS (UC);Fil: Chasapi, Anastasia. Centre For Research And Technology - Hellas ; Chemical Process & Energy Resources Institute;Fil: Fichó, Erzsébet. Cytocast Hungary; HungríaFil: Balatti, Galo Ezequiel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: González Buitrón, Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Erdos, Gabor. Eötvös University; ArgentinaFil: Pajkos, Matyas. Eotvos University, Budapest. Department Of Materials Physics; ArgentinaFil: Dosztányi, Zsuzsanna. Eotvos University, Budapest. Department Of Materials Physics; ArgentinaFil: Dobson, Laszlo. Semmelweis University; HungríaFil: Conte, Alessio Del. Università di Padova; ItaliaFil: Clementel, Damiano. Università di Padova; ItaliaFil: Salladini, Edoardo. Università di Padova; ItaliaFil: DisProt Consortium. Università di Padova; ItaliaFil: Ku, Luiggi G Tenorio. Università di Padova; ItaliaFil: Monzon, Alexander Miguel. Università di Padova; ItaliaFil: Tompa, Peter. Vrije Unviversiteit Brussel; BélgicaFil: Lazar, Tamas. Vrije Unviversiteit Brussel; BélgicaFil: Tosatto, Silvio C E. Università di Padova; ItaliaFil: Piovesan, Damiano. Università di Padova; Itali

DisProt in 2024: improving function annotation of intrinsically disordered proteins

DisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions. The latest version of DisProt brings significant advancements, including a broader representation of functions and an enhanced curation process. These improvements aim to increase both the quality of annotations and their coverage at the sequence level. Higher coverage has been achieved by adopting additional evidence codes. Quality of annotations has been improved by systematically applying Minimum Information About Disorder Experiments (MIADE) principles and reporting all the details of the experimental setup that could potentially influence the structural state of a protein. The DisProt database now includes new thematic datasets and has expanded the adoption of Gene Ontology terms, resulting in an extensive functional repertoire which is automatically propagated to UniProtKB. Finally, we show that DisProt's curated annotations strongly correlate with disorder predictions inferred from AlphaFold2 pLDDT (predicted Local Distance Difference Test) confidence scores. This comparison highlights the utility of DisProt in explaining apparent uncertainty of certain well-defined predicted structures, which often correspond to folding-upon-binding fragments. Overall, DisProt serves as a comprehensive resource, combining experimental evidence of disorder information to enhance our understanding of intrinsically disordered proteins and their functional implications