DisProt: intrinsic protein disorder annotation in 2020

HATOS, ANDRÁS; PALOPOLI, NICOLAS; HATOS, ANDRÁS; PALOPOLI, NICOLAS; HAJDU-SOLTÉSZ, BORBÁLA; MARINO-BUSLJE, CRISTINA; HAJDU-SOLTÉSZ, BORBÁLA; MARINO-BUSLJE, CRISTINA; MONZON, ALEXANDER M; MARTÍNEZ-PÉREZ, ELIZABETH; MONZON, ALEXANDER M; MARTÍNEZ-PÉREZ, ELIZABETH

NUCLEIC ACIDS RESEARCH

OXFORD UNIV PRESS

Lugar: Oxford; Año: 2019 p. 269 - 276

0305-1048

D270Nucleic Acids Research, 2020, Vol. 48, Database issueResearch University of Copenhagen, Copenhagen DK-2200, Denmark,24Bioinformatics Research Laboratory,Department of Biological Sciences, University of Cyprus, Nicosia, CY 1678, Cyprus,25Interuniversity Institute ofBioinformatics in Brussels (IB2), ULB-VUB, Brussels 1050, Belgium and26CNR Institute of Neurosceince, Padova35121, ItalyReceived September 15, 2019; Revised October 11, 2019; Editorial Decision October 11, 2019; Accepted October 12, 2019ABSTRACTThe Database of Protein Disorder (DisProt, URL:https://disprot.org) provides manually curated anno-tations of intrinsically disordered proteins from theliterature. Here we report recent developments withDisProt (version 8), including the doubling of proteinentries, a new disorder ontology, improvements ofthe annotation format and a completely new web-site. The website includes a redesigned graphicalinterface, a better search engine, a clearer API forprogrammatic access and a new annotation inter-face that integrates text mining technologies. Thenew entry format provides a greater flexibility, sim-plifies maintenance and allows the capture of moreinformation from the literature. The new disorder on-tology has been formalized and made interoperableby adopting the OWL format, as well as its structureand term definitions have been improved. The newannotation interface has made the curation processfaster and more effective. We recently showed thatnew DisProt annotations can be effectively used totrain and validate disorder predictors. We believe thegrowth of DisProt will accelerate, contributing to theimprovement of function and disorder predictors andtherefore to illuminate the ?dark? proteome