DisProt: intrinsic protein disorder annotation in 2020

András Hatos(University of Padua), Borbála Hajdu-Soltész(Eötvös Loránd University), Alexander Miguel Monzón(University of Padua), Nicolás Palópoli(National University of Quilmes), Lucı́a Álvarez(Consejo Nacional de Investigaciones Científicas y Técnicas), Burcu Aykaç Fas(Danish Cancer Society), Claudio Bassot(Stockholm University), Guillermo Ignacio Benítez(National University of Quilmes), Martina Bevilacqua(University of Padua), Anastasia Chasapi(Centre for Research and Technology Hellas), Lucía B. Chemes(Consejo Nacional de Investigaciones Científicas y Técnicas), Norman E. Davey(Institute of Cancer Research), Radoslav Davidović(University of Belgrade), A. Keith Dunker(Indiana University School of Medicine), Arne Elofsson(Stockholm University), Julien Gobeill(SIB Swiss Institute of Bioinformatics), Nicolás S. González Foutel(Consejo Nacional de Investigaciones Científicas y Técnicas), Govindarajan Sudha(Stockholm University), Mainak Guharoy(Vrije Universiteit Brussel), Tamás Horváth(Institute of Molecular Life Sciences), Valentín Iglesias(Universitat Autònoma de Barcelona), Andrey V Kajava(Centre National de la Recherche Scientifique), Orsolya Panna Kovacs(Institute of Molecular Life Sciences), John Lamb(Stockholm University), Matteo Lambrughi(Danish Cancer Society), Tamás Lázár(Vrije Universiteit Brussel), Jérémy Leclercq(Centre National de la Recherche Scientifique), Emanuela Leonardi(University of Padua), Sandra Macedo‐Ribeiro(i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto), Mauricio Macossay-Castillo(Vrije Universiteit Brussel), Emiliano Maiani(Danish Cancer Society), José A. Manso(i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto), Cristina Marino‐Buslje(Fundación Instituto Leloir), Elizabeth Martínez‐Pérez(Fundación Instituto Leloir), Bálint Mészáros(Eötvös Loránd University), Ivan Mičetić(University of Padua), Giovanni Minervini(University of Padua), Nikoletta Murvai(Institute of Molecular Life Sciences), Marco Necci(University of Padua), Christos Ouzounis(Centre for Research and Technology Hellas), Mátyás Pajkos(Eötvös Loránd University), Lisanna Paladin(University of Padua), Rita Pancsa(Institute of Molecular Life Sciences), Elena Papaleo(University of Copenhagen), Gustavo Parisi(National University of Quilmes), Emilie Pasche(SIB Swiss Institute of Bioinformatics), Pedro J Barbosa Pereira(i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto), Vasilis J. Promponas(University of Cyprus), Jordi Pujols(Universitat Autònoma de Barcelona), Federica Quaglia(University of Padua), Patrick Ruch(SIB Swiss Institute of Bioinformatics), Marco Salvatore(Stockholm University), Éva Schád(Institute of Molecular Life Sciences), Beáta Szabó(Institute of Molecular Life Sciences), Tamás Szaniszló(Eötvös Loránd University), Stella Tamana(University of Cyprus), Ágnes Tantos(Institute of Molecular Life Sciences), Nevena Veljković(University of Belgrade), Salvador Ventura(Universitat Autònoma de Barcelona), Wim Vranken(Vrije Universiteit Brussel), Zsuzsanna Dosztányi(Eötvös Loránd University), Péter Tompa(Vrije Universiteit Brussel), Silvio C. E. Tosatto(University of Padua), Damiano Piovesan(University of Padua)
Nucleic Acids Research
October 12, 2019
Cited by 246Open Access
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Abstract

The Database of Protein Disorder (DisProt, URL: https://disprot.org) provides manually curated annotations of intrinsically disordered proteins from the literature. Here we report recent developments with DisProt (version 8), including the doubling of protein entries, a new disorder ontology, improvements of the annotation format and a completely new website. The website includes a redesigned graphical interface, a better search engine, a clearer API for programmatic access and a new annotation interface that integrates text mining technologies. The new entry format provides a greater flexibility, simplifies maintenance and allows the capture of more information from the literature. The new disorder ontology has been formalized and made interoperable by adopting the OWL format, as well as its structure and term definitions have been improved. The new annotation interface has made the curation process faster and more effective. We recently showed that new DisProt annotations can be effectively used to train and validate disorder predictors. We believe the growth of DisProt will accelerate, contributing to the improvement of function and disorder predictors and therefore to illuminate the 'dark' proteome.


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