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

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...

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Autores principales: Potenza, Emilio, Domenico, Tomás Di, Walsh, Ian, Tosatto, Silvio C.E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384034/
https://www.ncbi.nlm.nih.gov/pubmed/25361972
http://dx.doi.org/10.1093/nar/gku982
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author Potenza, Emilio
Domenico, Tomás Di
Walsh, Ian
Tosatto, Silvio C.E.
author_facet Potenza, Emilio
Domenico, Tomás Di
Walsh, Ian
Tosatto, Silvio C.E.
author_sort Potenza, Emilio
collection PubMed
description 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.
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spelling pubmed-43840342015-04-08 MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins Potenza, Emilio Domenico, Tomás Di Walsh, Ian Tosatto, Silvio C.E. Nucleic Acids Res Database Issue 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. Oxford University Press 2014-10-31 2015-01-28 /pmc/articles/PMC4384034/ /pubmed/25361972 http://dx.doi.org/10.1093/nar/gku982 Text en © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) ), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Database Issue
Potenza, Emilio
Domenico, Tomás Di
Walsh, Ian
Tosatto, Silvio C.E.
MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins
title MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins
title_full MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins
title_fullStr MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins
title_full_unstemmed MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins
title_short MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins
title_sort mobidb 2.0: an improved database of intrinsically disordered and mobile proteins
topic Database Issue
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384034/
https://www.ncbi.nlm.nih.gov/pubmed/25361972
http://dx.doi.org/10.1093/nar/gku982
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