Abstract
The Database of Intrinsically Disordered Proteins (DisProt, URL: https://disprot.org) is the major repository of manually curated annotations of intrinsically disordered proteins and regions from the literature. We report here recent updates of DisProt version 9, including a restyled web interface, refactored Intrinsically Disordered Proteins Ontology (IDPO), improvements in the curation process and significant content growth of around 30%. Higher quality and consistency of annotations is provided by a newly implemented reviewing process and training of curators. The increased curation capacity is fostered by the integration of DisProt with APICURON, a dedicated resource for the proper attribution and recognition of biocuration efforts. Better interoperability is provided through the adoption of the Minimum Information About Disorder (MIADE) standard, an active collaboration with the Gene Ontology (GO) and Evidence and Conclusion Ontology (ECO) consortia and the support of the ELIXIR infrastructure.
Highlights
Whereas our traditional view of protein function is rooted in the model of proteins assuming a stable structure, a welldefined 3D fold, it is >20 years since the concept of structural disorder of proteins has been proposed [1,2]
The prediction of protein disorder from sequence, for example, has always been an area of continuous activity. It has received a boost with the establishment of the Critical Assessment of Protein Intrinsic Disorder prediction (CAID) experiment as a community-wide blind test to compare state-of-the-art approaches to predict disorder [4]
The adoption of stable and well established ontologies, Gene Ontology (GO) and Evidence and Conclusion Ontology (ECO), plays a crucial role by allowing the curators to effortlessly expand the coverage of functions and experimental techniques available in DisProt
Summary
Whereas our traditional view of protein function is rooted in the model of proteins assuming a stable structure, a welldefined 3D fold, it is >20 years since the concept of structural disorder of proteins has been proposed [1,2]. Combined with data in the MobiDB database, which provides predictions and annotations for all IDPs/IDRs [14], this effort is critical for integrating disorder-related information into other data resources, such as UniProtKB [15] or PDBe [16]. The previous release of the database, DisProt 8 [30] contained about 1500 entries and 3500 disordered protein regions.
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