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ready MobiDB

General Information
A database of protein disorder and mobility annotations. MobiDB was designed to offer a centralized resource for annotations of intrinsic protein disorder. The database features three levels of annotation: manually curated, indirect and predicted. Manually curated data is extracted from the DisProt database. Indirect data is inferred from PDB structures that are considered an indication of intrinsic disorder. The 10 predictors currently included (three ESpritz flavors, two IUPred flavors, two DisEMBL flavors, GlobPlot, VSL2b and JRONN) enable MobiDB to provide disorder annotations for every protein in absence of more reliable data. The new version also features a consensus annotation and classification for long disordered regions. In order to complement the disorder annotations, MobiDB features additional annotations from external sources. Annotations from the UniProt database include post-translational modifications and linear motifs. Pfam annotations are displayed in graphical form and are link-enabled, allowing the user to visit the corresponding Pfam page for further information. Experimental protein–protein interactions are also classified for disorder content.

How to cite this record MobiDB; MobiDB; DOI: 10.25504/FAIRsharing.jwra3e; Last edited: Feb. 22, 2018, 2:58 p.m.; Last accessed: Jun 23 2018 2:49 p.m.

This record is maintained by BioComputingUP  (ivanmicetic)

Record updated: Oct. 17, 2017, 7:27 p.m. by The FAIRsharing Team.



Additional Information

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Conditions of Use

Applies to: Data use

Data Release

Data Curation

Data Access

REST Web Services


MobiDB: a comprehensive database of intrinsic protein disorder annotations.

Di Domenico T, Walsh I, Martin AJ, Tosatto SC.
Bioinformatics 2012

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MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins.

Emilio Potenza, Tomás Di Domenico, Ian Walsh, and Silvio C.E. Tosatto
Nucleic Acids Research 2014

View Paper (PubMed) View Paper (DOI)

MobiDB 3.0: More annotations for intrinsic disorder, conformational diversity and interactions in proteins

Piovesan, D, Tabaro, F, Paladin, F, Necci, M, Mičetić, I, Camilloni, C, Davey, N, Dosztanyi, Z, Meszaros, B, Monzon, A, Parisi, G, Schad, E, Sormanni, P, Tompa, P, Vendruscolo, M, Vranken, W, Tosatto, SCE
Nucleic Acids Research 2017