DisProt: the Database of Disordered Proteins

By Megan Sickmeier, J. Hamilton, T. LeGall, Vladimir Vacic, Marc S. Cortese, Á. Tantos, Beáta Szabó, Peter Tompa, J. Chen, Vladimir N Uversky and 2 more. Nucleic Acids Res., 2006

822 citations recorded by the source corpus.

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 .

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/78597d4989a7f7f892067637dd3271e60569b087

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Citations in the corpus

Composition Profiler: a tool for discovery and visualization of amino acid composition differences (2007, background): “4, is a set of consensus sequences of experimentally determined disordered regions [4].”
Comprehensive comparative assessment of in-silico predictors of disordered regions. (2012, methodology): “Another commonly used source of the disorder annotations is the manually curated DisProt database [[19]], which includes annotations of experimentally verified and biologically relevant unstructured regions.”
Improved sequence-based prediction of disordered regions with multilayer fusion of multiple information sources (2010, background): “It combines three complementary disorder predictors, sequence, sequence profiles, predicted secondary structure, solvent accessibility, backbone dihedral torsion angles, residue flexibility and B-factors.”
FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies (2016, background): “Intrinsically disordered protein databases (Disprot (15), MobiDB (16)) collect information on ID regions of isolated proteins, which may not represent IDPs in their biological context.”
Genome‐scale prediction of proteins with long intrinsically disordered regions (2014, background): “11–13 However, currently only a limited number of disordered proteins were characterized experimentally,14 and these efforts lag behind the rapidly accumulating number of protein chains.”
Continuous Distributed Representation of Biological Sequences for Deep Proteomics and Genomics (2015, neutral): “DisProt is a database of experimentally identified disordered proteins that categorizes disordered and ordered regions of a collection of proteins [26].”
Intrinsically Semi-disordered State and Its Role in Induced Folding and Protein Aggregation (2013, background): “1b for all three datasets SL477, DX4080, and Control703 that respectively represent re-annotated disordered proteins from Disprot [12, 14, 15], high-resolution X-ray structures (ordered proteins) with residues without coordinates as disordered residues [12], and a negative control set of stably fold”
The s2D method: simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins. (2015, methodology): “(b) Distribution of the predicted coil population of the residues belonging to regions annotated as disordered in the DisProt database [35] (yellow) and to regions annotated as structurally determined (blue).”
Understanding eukaryotic linear motifs and their role in cell signaling and regulation. (2008, methodology): “In general, the most recent programs outperform the earlier methods: a key factor has been the establishment of the DisProt IUP database (12), which was not available to the earlier generation of predictors.”