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Nucleic Acids Res. 2015 Jan;43(Database issue):D315-20. doi: 10.1093/nar/gku982. Epub 2014 Oct 31.

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

Author information

1
Department of Biomedical Sciences, University of Padua, 35131 Padova, Italy.
2
Department of Biomedical Sciences, University of Padua, 35131 Padova, Italy silvio.tosatto@unipd.it.

Abstract

MobiDB (http://mobidb.bio.unipd.it/) is a database of intrinsically disordered and mobile proteins. Intrinsically disordered regions are key for the function of numerous proteins. Here we provide a new version of MobiDB, a centralized source aimed at providing the most complete picture on different flavors of disorder in protein structures covering all UniProt sequences (currently over 80 million). 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 from STRING are also classified for disorder content.

PMID:
25361972
PMCID:
PMC4384034
DOI:
10.1093/nar/gku982
[Indexed for MEDLINE]
Free PMC Article

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