DILIMOT: discovery of linear motifs in proteins

Nucleic Acids Res. 2006 Jul 1;34(Web Server issue):W350-5. doi: 10.1093/nar/gkl159.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs*
  • Binding Sites
  • Internet
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / metabolism
  • Protein Kinases / metabolism
  • Protein Sorting Signals
  • Sequence Analysis, Protein / methods*
  • Software*
  • User-Computer Interface

Substances

  • Microtubule-Associated Proteins
  • Protein Sorting Signals
  • Protein Kinases