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ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins

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Item Type:Article
Title:ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins
Creators Name:Puntervoll, P. and Linding, R. and Gemund, C. and Chabanis-Davidson, S. and Mattingsdal, M. and Cameron, S. and Martin, D.M.A. and Ausiello, G. and Brannetti, B. and Costantini, A. and Ferre, F. and Maselli, V. and Via, A. and Cesareni, G. and Diella, F. and Superti-Furga, G. and Wyrwicz, L. and Ramu, C. and McGuigan, C. and Gudavalli, R. and Letunic, I. and Bork, P. and Rychlewski, L. and Kuester, B. and Helmer-Citterich, M. and Hunter, W.N. and Aasland, R. and Gibson, T.J.
Abstract:Multidomain proteins predominate in eukaryotic proteomes. Individual functions assigned to different sequence segments combine to create a complex function for the whole protein. While on-line resources are available for revealing globular domains in sequences, there has hitherto been no comprehensive collection of small functional sites/motifs comparable to the globular domain resources, yet these are as important for the function of multidomain proteins. Short linear peptide motifs are used for cell compartment targeting, protein-protein interaction, regulation by phosphorylation, acetylation, glycosylation and a host of other post-translational modifications. ELM, the Eukaryotic Linear Motif server at http://elm.eu.org/, is a new bioinformatics resource for investigating candidate short non-globular functional motifs in eukaryotic proteins, aiming to fill the void in bioinformatics tools. Sequence comparisons with short motifs are difficult to evaluate because the usual significance assessments are inappropriate. Therefore the server is implemented with several logical filters to eliminate false positives. Current filters are for cell compartment, globular domain clash and taxonomic range. In favourable cases, the filters can reduce the number of retained matches by an order of magnitude or more.
Keywords:Amino Acid Motifs, Eukaryotic Cells, Internet, Tertiary Protein Structure, Proteins, Protein Sequence Analysis, Software, User-Computer Interface
Source:Nucleic Acids Research
ISSN:0305-1048
Publisher:Oxford University Press
Volume:31
Number:13
Page Range:3625-3630
Date:1 July 2003
Official Publication:https://doi.org/10.1093/nar/gkg545
PubMed:View item in PubMed

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