{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,11]],"date-time":"2026-04-11T17:47:50Z","timestamp":1775929670332,"version":"3.50.1"},"reference-count":19,"publisher":"Oxford University Press (OUP)","issue":"15","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2012,8,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Motivation: Disordered protein regions are key to the function of numerous processes within an organism and to the determination of a protein's biological role. The most common source for protein disorder annotations, DisProt, covers only a fraction of the available sequences. Alternatively, the Protein Data Bank (PDB) has been mined for missing residues in X-ray crystallographic structures. Herein, we provide a centralized source for data on different flavours of disorder in protein structures, MobiDB, building on and expanding the content provided by already existing sources. In addition to the DisProt and PDB X-ray structures, we have added experimental information from NMR structures and five different flavours of two disorder predictors (ESpritz and IUpred). These are combined into a weighted consensus disorder used to classify disordered regions into flexible and constrained disorder. Users are encouraged to submit manual annotations through a submission form. MobiDB features experimental annotations for 17 285 proteins, covering the entire PDB and predictions for the SwissProt database, with 565 200 annotated sequences. Depending on the disorder flavour, 6\u201320% of the residues are predicted as disordered.<\/jats:p>\n               <jats:p>Availability: The database is freely available at http:\/\/mobidb.bio.unipd.it\/.<\/jats:p>\n               <jats:p>Contact: \u00a0silvio.tosatto@unipd.it<\/jats:p>","DOI":"10.1093\/bioinformatics\/bts327","type":"journal-article","created":{"date-parts":[[2012,6,4]],"date-time":"2012-06-04T14:09:02Z","timestamp":1338818942000},"page":"2080-2081","source":"Crossref","is-referenced-by-count":139,"title":["MobiDB: a comprehensive database of intrinsic protein disorder annotations"],"prefix":"10.1093","volume":"28","author":[{"given":"Tom\u00e1s","family":"Di Domenico","sequence":"first","affiliation":[{"name":"Department of Biology, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ian","family":"Walsh","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alberto J.M.","family":"Martin","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Silvio C.E.","family":"Tosatto","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2012,6,1]]},"reference":[{"key":"2023012512531199900_B1","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"2023012512531199900_B2","doi-asserted-by":"crossref","first-page":"R14","DOI":"10.1186\/gb-2011-12-2-r14","article-title":"Bringing order to protein disorder through comparative genomics and genetic interactions","volume":"12","author":"Bellay","year":"2011","journal-title":"Genome Biol."},{"key":"2023012512531199900_B3","doi-asserted-by":"crossref","first-page":"D301","DOI":"10.1093\/nar\/gkl971","article-title":"The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data","volume":"35","author":"Berman","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"2023012512531199900_B4","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/j.jmb.2005.01.071","article-title":"The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins","volume":"347","author":"Dosztanyi","year":"2005","journal-title":"J. Mol. Biol."},{"issue":"Suppl 2","key":"2023012512531199900_B5","doi-asserted-by":"crossref","first-page":"S1","DOI":"10.1186\/1471-2164-9-S2-S1","article-title":"The unfoldomics decade: an update on intrinsically disordered proteins","volume":"9","author":"Dunker","year":"2008","journal-title":"BMC Genom."},{"key":"2023012512531199900_B6","doi-asserted-by":"crossref","first-page":"D211","DOI":"10.1093\/nar\/gkp985","article-title":"The Pfam protein families database","volume":"38","author":"Finn","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"2023012512531199900_B7","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"2023012512531199900_B8","doi-asserted-by":"crossref","first-page":"2916","DOI":"10.1093\/bioinformatics\/btq537","article-title":"MOBI: a web server to define and visualize structural mobility in NMR protein ensembles","volume":"26","author":"Martin","year":"2010","journal-title":"Bioinformatics"},{"key":"2023012512531199900_B9","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/j.sbi.2011.03.014","article-title":"Protein disorder\u2014a breakthrough invention of evolution?","volume":"21","author":"Schlessinger","year":"2011","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2023012512531199900_B10","doi-asserted-by":"crossref","first-page":"D786","DOI":"10.1093\/nar\/gkl893","article-title":"DisProt: the Database of Disordered Proteins","volume":"35","author":"Sickmeier","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"2023012512531199900_B11","doi-asserted-by":"crossref","first-page":"D214","DOI":"10.1093\/nar\/gkq1020","article-title":"Ongoing and future developments at the Universal Protein Resource","volume":"39","author":"The UniProt Consortium","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"2023012512531199900_B12","volume-title":"Structure and Function of Intrinsically Disordered Proteins.","author":"Tompa","year":"2010"},{"key":"2023012512531199900_B13","doi-asserted-by":"crossref","first-page":"D262","DOI":"10.1093\/nar\/gki058","article-title":"E-MSD: an integrated data resource for bioinformatics","volume":"33","author":"Velankar","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"2023012512531199900_B14","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1002\/prot.10437","article-title":"Flavors of protein disorder","volume":"52","author":"Vucetic","year":"2003","journal-title":"Proteins"},{"key":"2023012512531199900_B15","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1093\/bioinformatics\/btr682","article-title":"ESpritz: accurate and fast prediction of protein disorder","volume":"28","author":"Walsh","year":"2012","journal-title":"Bioinformatics"},{"key":"2023012512531199900_B16","doi-asserted-by":"crossref","first-page":"W190","DOI":"10.1093\/nar\/gkr411","article-title":"CSpritz: accurate prediction of protein disorder segments with annotation for homology, secondary structure and linear motifs","volume":"39","author":"Walsh","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"2023012512531199900_B17","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.jmb.2004.02.002","article-title":"Prediction and functional analysis of native disorder in proteins from the three kingdoms of life","volume":"337","author":"Ward","year":"2004","journal-title":"J. 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