DisProt: the Database of Disordered Proteins

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 2006 Dec 6

PMID 17145717

Citations 371

Authors

Megan Sickmeier

Justin A Hamilton

Tanguy LeGall

Vladimir Vacic

Marc S Cortese

Agnes Tantos

Beata Szabo

Peter Tompa

Jake Chen

Vladimir N Uversky

Zoran Obradovic

A Keith Dunker

Affiliations

Soon will be listed here.

Abstract

The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low-affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These three features are all enabled and enhanced by protein intrinsic disorder. One of the major hindrances in the study of IDPs has been the lack of organized information. DisProt was developed to enable IDP research by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies. DisProt is openly available at http://www.disprot.org.

Citing Articles

MEDOC: A Fast, Scalable, and Mathematically Exact Algorithm for the Site-Specific Prediction of the Protonation Degree in Large Disordered Proteins.

Fossat M J Chem Inf Model. 2025; 65(2):873-881.

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Decoding the biogenesis of HIV-induced CPSF6 puncta and their fusion with the nuclear speckle.

Tomasini C, Cuche C, Ay S, Collard M, Cui B, Rashid M bioRxiv. 2024; .

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Mis-splicing of a neuronal microexon promotes CPEB4 aggregation in ASD.

Garcia-Cabau C, Bartomeu A, Tesei G, Cheung K, Pose-Utrilla J, Pico S Nature. 2024; 637(8045):496-503.

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On the Roles of Protein Intrinsic Disorder in the Origin of Life and Evolution.

Uversky V Life (Basel). 2024; 14(10).

PMID: 39459607 PMC: 11509291. DOI: 10.3390/life14101307.

Structural study of the intrinsically disordered tardigrade damage suppressor protein (Dsup) and its complex with DNA.

Zarubin M, Murugova T, Ryzhykau Y, Ivankov O, Uversky V, Kravchenko E Sci Rep. 2024; 14(1):22910.

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