DisProt in 2024: improving function annotation of intrinsically disordered proteins

Aspromonte Maria Cristina; Nugnes Maria Victoria; Quaglia Federica; Bouharoua Adel; Tosatto Silvio C. E.; Piovesan Damiano: DisProt in 2024: improving function annotation of intrinsically disordered proteins.
NUCLEIC ACIDS RESEARCH, 52 (D1). D434-D441. ISSN 0305-1048 (2024)

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Folyóiratcikk

Szerző azonosítók:

Név	ORCID	MTMT szerző azonosító
Aspromonte Maria Cristina	0000-0002-4937-6952
Nugnes Maria Victoria	0000-0001-8399-7907
Quaglia Federica	0000-0002-0341-4888
Bouharoua Adel
Tosatto Silvio C. E.
Piovesan Damiano	0000-0001-8210-2390

Absztrakt (kivonat):

DisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions. The latest version of DisProt brings significant advancements, including a broader representation of functions and an enhanced curation process. These improvements aim to increase both the quality of annotations and their coverage at the sequence level. Higher coverage has been achieved by adopting additional evidence codes. Quality of annotations has been improved by systematically applying Minimum Information About Disorder Experiments (MIADE) principles and reporting all the details of the experimental setup that could potentially influence the structural state of a protein. The DisProt database now includes new thematic datasets and has expanded the adoption of Gene Ontology terms, resulting in an extensive functional repertoire which is automatically propagated to UniProtKB. Finally, we show that DisProt's curated annotations strongly correlate with disorder predictions inferred from AlphaFold2 pLDDT (predicted Local Distance Difference Test) confidence scores. This comparison highlights the utility of DisProt in explaining apparent uncertainty of certain well-defined predicted structures, which often correspond to folding-upon-binding fragments. Overall, DisProt serves as a comprehensive resource, combining experimental evidence of disorder information to enhance our understanding of intrinsically disordered proteins and their functional implications.Graphical Abstract

Folyóirat címe:

NUCLEIC ACIDS RESEARCH

Megjelenés éve:

2024

Kötet:

Szám:

Oldalak:

D434-D441

ISSN:

0305-1048

Intézmény:

Pázmány Péter Katolikus Egyetem