DisProt: Intrinsic protein disorder annotation in 2020

András Hatos, Borbála Hajdu-Soltész, Alexander M. Monzon, Nicolas Palopoli, Lucía Álvarez, Burcu Aykac-Fas, Claudio Bassot, Guillermo I. Benítez, Martina Bevilacqua, Anastasia Chasapi, Lucia Chemes, Norman E. Davey, Radoslav Davidović, A. Keith Dunker, Arne Elofsson, Julien Gobeill, Nicolás S.González Foutel, Govindarajan Sudha, Mainak Guharoy, Tamas HorvathValentin Iglesias, Andrey V. Kajava, Orsolya P. Kovacs, John Lamb, Matteo Lambrughi, Tamas Lazar, Jeremy Y. Leclercq, Emanuela Leonardi, Sandra MacEdo-Ribeiro, Mauricio MacOssay-Castillo, Emiliano Maiani, José A. Manso, Cristina Marino-Buslje, Elizabeth Martínez-Pérez, Bálint Mészáros, Ivan Mičetić, Giovanni Minervini, Nikoletta Murvai, Marco Necci, Christos A. Ouzounis, Mátyás Pajkos, Lisanna Paladin, Rita Pancsa, Elena Papaleo, Gustavo Parisi, Emilie Pasche, Pedro J. Barbosa Pereira, Vasilis J. Promponas, Jordi Pujols, Federica Quaglia, Patrick Ruch, Marco Salvatore, Eva Schad, Beata Szabo, Tamás Szaniszló, Stella Tamana, Agnes Tantos, Nevena Veljkovic, Salvador Ventura, Wim Vranken, Zsuzsanna Dosztányi, Peter Tompa, Silvio C.E. Tosatto, Damiano Piovesan

Research output: Contribution to journalArticle

8 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)D269-D276
JournalNucleic acids research
Issue numberD1
StatePublished - Jan 1 2020

ASJC Scopus subject areas

  • Genetics

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    Hatos, A., Hajdu-Soltész, B., Monzon, A. M., Palopoli, N., Álvarez, L., Aykac-Fas, B., Bassot, C., Benítez, G. I., Bevilacqua, M., Chasapi, A., Chemes, L., Davey, N. E., Davidović, R., Dunker, A. K., Elofsson, A., Gobeill, J., Foutel, N. S. G., Sudha, G., Guharoy, M., ... Piovesan, D. (2020). DisProt: Intrinsic protein disorder annotation in 2020. Nucleic acids research, 48(D1), D269-D276. https://doi.org/10.1093/nar/gkz975