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.

Puntervoll, P., Linding, R., Gemünd, C., Chabanis Davidson, S., Mattingsdal, M., Cameron, S., et al. (2003). ELM server: A new resource for investigating short functional sites in modular eukaryotic proteins. NUCLEIC ACIDS RESEARCH, 31(13), 3625-3630 [10.1093/nar/gkg545].

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

AUSIELLO, GABRIELE;CESARENI, GIOVANNI;HELMER CITTERICH, MANUELA;
2003-07-01

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.
1-lug-2003
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/11 - BIOLOGIA MOLECOLARE
English
Con Impact Factor ISI
Protein Structure, Tertiary; User-Computer Interface; Sequence Analysis, Protein; Amino Acid Motifs; Proteins; Software; Internet; Eukaryotic Cells
http://nar.oxfordjournals.org/content/31/13/3625.full
Puntervoll, P., Linding, R., Gemünd, C., Chabanis Davidson, S., Mattingsdal, M., Cameron, S., et al. (2003). ELM server: A new resource for investigating short functional sites in modular eukaryotic proteins. NUCLEIC ACIDS RESEARCH, 31(13), 3625-3630 [10.1093/nar/gkg545].
Puntervoll, P; Linding, R; Gemünd, C; Chabanis Davidson, S; Mattingsdal, M; Cameron, S; Martin, D; Ausiello, G; Brannetti, B; Costantini, A; Ferrè, F; Maselli, V; Via, A; Cesareni, G; Diella, F; Superti Furga, G; Wyrwicz, L; Ramu, C; Mcguigan, C; Gudavalli, R; Letunic, I; Bork, P; Rychlewski, L; Küster, B; HELMER CITTERICH, M; Hunter, W; Aasland, R; Gibson, T
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/14889
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