DisProt 7.0: a major update of the database of disordered proteins

By Damiano Piovesan, Francesco Tabaro, I. Mičetić, Marco Necci, F. Quaglia, Christopher J. Oldfield, M. C. Aspromonte, Norman E. Davey, R. Davidovic, Zsuzsanna Dosztányi and 30 more. 2016

203 citations recorded by the source corpus.

The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy, Evaluation & Benchmarks, Computational Biology & Bioinformatics

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Citations in the corpus

SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, neutral): “0 [45].”
IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, methodology): “…phosphorylation, methylation and acetylation sites) from PhosphoSitePlus (48), related structures from the PDB (49) and experimentally verified disordered regions from three different databases: generic disorder from DisProt (10) and disordered binding regions from DIBS (36) and MFIB (50).”
Pi-Pi contacts are an overlooked protein feature relevant to phase separation (2018, methodology): “containing disorder in the Disprot database (42), representing a positive set for disorder, and (D)”
MobiDB‐lite: fast and highly specific consensus prediction of intrinsic disorder in proteins (2017, methodology): “First, ID predictions for a query protein are made with three variants of ESpritz (DisProt, NMR, X-ray) (Walsh et al., 2012), two variants of IUpred (long, short) (Doszt anyi et al., 2005), DisEMBL (465, hot loops) (Linding et al., 2003b) and GlobPlot (Linding et al., 2003a).”