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. 2022 Jul;2(7):e484.
doi: 10.1002/cpz1.484.

Exploring Manually Curated Annotations of Intrinsically Disordered Proteins with DisProt

Federica Quaglia  1   2 , András Hatos  2 , Edoardo Salladini  2 , Damiano Piovesan  2 , Silvio C E Tosatto  2
Affiliations

Exploring Manually Curated Annotations of Intrinsically Disordered Proteins with DisProt

Federica Quaglia et al. Curr Protoc. 2022 Jul.

Abstract

DisProt is the major repository of manually curated data for intrinsically disordered proteins collected from the literature. Although lacking a stable three-dimensional structure under physiological conditions, intrinsically disordered proteins carry out a plethora of biological functions, some of them directly arising from their flexible nature. A growing number of scientific studies have been published during the last few decades to shed light on their unstructured state, their binding modes, and their functions. DisProt makes use of a team of expert biocurators to provide up-to-date annotations of intrinsically disordered proteins from the literature, making them available to the scientific community. Here we present a comprehensive description on how to use DisProt in different contexts and provide a detailed explanation of how to explore and interpret manually curated annotations of intrinsically disordered proteins. We describe how to search DisProt annotations, both using the web interface and the API for programmatic access. Finally, we explain how to visualize and interpret a DisProt entry, the SARS-CoV-2 Nucleoprotein, characterized by the presence of unstructured N-terminal and C-terminal regions and a flexible linker. © 2022 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Performing a search in DisProt Support Protocol 1: Downloading options Support Protocol 2: Programmatic access with DisProt REST API Basic Protocol 2: Exploring the DisProt Ontology page Basic Protocol 3: Visualizing and interpreting DisProt entries-the SARS-CoV-2 Nucleoprotein use case.

Keywords: DisProt; IDPs; biocuration; database; intrinsically disordered proteins.

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