ELM: the status of the 2010 eukaryotic linear motif resource
Open Access
- 17 November 2009
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 38 (suppl_1) , D167-D180
- https://doi.org/10.1093/nar/gkp1016
Abstract
Linear motifs are short segments of multidomain proteins that provide regulatory functions independently of protein tertiary structure. Much of intracellular signalling passes through protein modifications at linear motifs. Many thousands of linear motif instances, most notably phosphorylation sites, have now been reported. Although clearly very abundant, linear motifs are difficult to predict de novo in protein sequences due to the difficulty of obtaining robust statistical assessments. The ELM resource at http://elm.eu.org/ provides an expanding knowledge base, currently covering 146 known motifs, with annotation that includes >1300 experimentally reported instances. ELM is also an exploratory tool for suggesting new candidates of known linear motifs in proteins of interest. Information about protein domains, protein structure and native disorder, cellular and taxonomic contexts is used to reduce or deprecate false positive matches. Results are graphically displayed in a ‘Bar Code’ format, which also displays known instances from homologous proteins through a novel ‘Instance Mapper’ protocol based on PHI-BLAST. ELM server output provides links to the ELM annotation as well as to a number of remote resources. Using the links, researchers can explore the motifs, proteins, complex structures and associated literature to evaluate whether candidate motifs might be worth experimental investigation.Keywords
This publication has 90 references indexed in Scilit:
- Predicting intrinsic disorder in proteins: an overviewCell Research, 2009
- An EB1-Binding Motif Acts as a Microtubule Tip Localization SignalCell, 2009
- Comparative profiling identifies C13orf3 as a component of the Ska complex required for mammalian cell divisionThe EMBO Journal, 2009
- Kinome signaling through regulated protein–protein interactions in normal and cancer cellsCurrent Opinion in Cell Biology, 2009
- Linking folding and bindingCurrent Opinion in Structural Biology, 2009
- Recent developments in the MAFFT multiple sequence alignment programBriefings in Bioinformatics, 2008
- Structure of the Eps15–stonin2 complex provides a molecular explanation for EH-domain ligand specificityThe EMBO Journal, 2008
- Intrinsic disorder as a mechanism to optimize allosteric coupling in proteinsProceedings of the National Academy of Sciences, 2007
- Towards a theory of biological robustnessMolecular Systems Biology, 2007
- PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylationProteomics, 2004