DisProt 7.0: a major update of the database of disordered proteins

Damiano Piovesan(University of Padua), Francesco Tabaro(University of Padua), Ivan Mičetić(University of Padua), Marco Necci(University of Padua), Federica Quaglia(University of Padua), Christopher J. Oldfield(Indiana University School of Medicine), Maria Cristina Aspromonte(University of Padua), Norman E. Davey(University College Dublin), Radoslav Davidović(University of Belgrade), Zsuzsanna Dosztányi(Eötvös Loránd University), Arne Elofsson(Stockholm University), Alessandra Gasparini(University of Padua), András Hatos(University of Padua), Andrey V. Kajava(Centre National de la Recherche Scientifique), Lajos Kalmár(University of Cambridge), Emanuela Leonardi(University of Padua), Tamás Lázár(Vrije Universiteit Brussel), Sandra Macedo‐Ribeiro(i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto), Mauricio Macossay-Castillo(Vrije Universiteit Brussel), Attila Mészáros(Institute of Molecular Life Sciences), Giovanni Minervini(University of Padua), Nikoletta Murvai(Institute of Molecular Life Sciences), Jordi Pujols(Universitat Autònoma de Barcelona), Daniel B. Roche(Centre National de la Recherche Scientifique), Edoardo Salladini(Centre National de la Recherche Scientifique), Éva Schád(Institute of Molecular Life Sciences), Antoine Schramm(Centre National de la Recherche Scientifique), Beáta Szabó(Institute of Molecular Life Sciences), Ágnes Tantos(Institute of Molecular Life Sciences), Fiorella Tonello(University of Padua), Konstantinos D. Tsirigos(Stockholm University), Nevena Veljković(University of Belgrade), Salvador Ventura(Universitat Autònoma de Barcelona), Wim Vranken(Vrije Universiteit Brussel), Per Warholm(Stockholm University), Vladimir N. Uversky(University of South Florida), A. Keith Dunker(Indiana University School of Medicine), Sonia Longhi(Centre National de la Recherche Scientifique), Péter Tompa(Vrije Universiteit Brussel), Silvio C. E. Tosatto(University of Padua)
Nucleic Acids Research
October 21, 2016
Cited by 297Open Access
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Abstract

The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.


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