MobiDB: intrinsically disordered proteins in 2021

Author:

Piovesan Damiano1ORCID,Necci Marco1,Escobedo Nahuel2,Monzon Alexander Miguel1ORCID,Hatos András1ORCID,Mičetić Ivan1ORCID,Quaglia Federica1,Paladin Lisanna1ORCID,Ramasamy Pathmanaban34567,Dosztányi Zsuzsanna8,Vranken Wim F345ORCID,Davey Norman E9,Parisi Gustavo2,Fuxreiter Monika1,Tosatto Silvio C E1ORCID

Affiliation:

1. Dept. of Biomedical Sciences, University of Padua, Via Ugo Bassi 58/B, Padua 35121, Italy

2. Dept. of Science and Technology, Universidad Nacional de Quilmes, Buenos Aires, Argentina

3. Interuniversity Institute of Bioinformatics in Brussels, ULB/VUB, Triomflaan, BC building, 6th floor, CP 263, 1050 Brussels, Belgium

4. Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium

5. Centre for Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium

6. VIB-UGent Center for Medical Biotechnology, VIB, Ghent 9000, Belgium

7. Department of Biomolecular Medicine, Faculty of Health Sciences and Medicine, Ghent University, Ghent 9000, Belgium

8. Dept. of Biochemistry, ELTE Eötvös Loránd University, Budapest, Hungary

9. Division of Cancer Biology, The Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK

Abstract

Abstract The MobiDB database (URL: https://mobidb.org/) provides predictions and annotations for intrinsically disordered proteins. Here, we report recent developments implemented in MobiDB version 4, regarding the database format, with novel types of annotations and an improved update process. The new website includes a re-designed user interface, a more effective search engine and advanced API for programmatic access. The new database schema gives more flexibility for the users, as well as simplifying the maintenance and updates. In addition, the new entry page provides more visualisation tools including customizable feature viewer and graphs of the residue contact maps. MobiDB v4 annotates the binding modes of disordered proteins, whether they undergo disorder-to-order transitions or remain disordered in the bound state. In addition, disordered regions undergoing liquid-liquid phase separation or post-translational modifications are defined. The integrated information is presented in a simplified interface, which enables faster searches and allows large customized datasets to be downloaded in TSV, Fasta or JSON formats. An alternative advanced interface allows users to drill deeper into features of interest. A new statistics page provides information at database and proteome levels. The new MobiDB version presents state-of-the-art knowledge on disordered proteins and improves data accessibility for both computational and experimental users.

Funder

Horizon 2020

Marie Skłodowska-Curie

Italian Ministry of University and Research

Research Foundation Flanders

Cancer Research UK

Universidad Nacional de Quilmes

ANPCyT

Publisher

Oxford University Press (OUP)

Subject

Genetics

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