title: DILIMOT: discovery of linear motifs in proteins.
abstract: Discovery of protein functional motifs is critical in modern biology. Small segments of 3-10 residues play critical roles in protein interactions, post-translational modifications and trafficking. DILIMOT (DIscovery of LInear MOTifs) is a server for the prediction of these short linear motifs within a set of proteins. Given a set of sequences sharing a common functional feature (e.g. interaction partner or localization) the method finds statistically over-represented motifs likely to be responsible for it. The input sequences are first passed through a set of filters to remove regions unlikely to contain instances of linear motifs. Motifs are then found in the remaining sequence and ranked according to a statistic that measure over-representation and conservation across homologues in related species. The results are displayed via a visual interface for easy perusal. The server is available at http://dilimot.embl.de.
authors.affiliation: EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
authors.forename: Victor
authors.initials: V
authors.lastname: Neduva
authors.forename: Robert B
authors.initials: RB
authors.lastname: Russell
mesh_terms: D020816:Amino Acid Motifs; D001665:Binding Sites; D020407:Internet; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D021382:Protein Sorting Signals; D020539:Sequence Analysis, Protein / Q000379:methods*; D012984:Software; D014584:User-Computer Interface
chemical_list: D008869:Microtubule-Associated Proteins; D021382:Protein Sorting Signals; D011494:Protein Kinases