ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins (2003)
| Venue: | Nucleic Acids Res |
| Citations: | 32 - 5 self |
BibTeX
@ARTICLE{Linding03elmserver:,
author = {Rune Linding and Christine Gemünd and Sophie Chabanis-davidson and Morten Mattingsdal and Scott Cameron and David M. A. Martin and Gabriele Ausiello and Barbara Brannetti and Anna Costantini and Fabrizio Ferrè and Vincenza Maselli and Allegra Via and Gianni Cesareni and Francesca Diella and Giulio Superti-furga and Lucjan Wyrwicz and Chenna Ramu and Caroline Mcguigan and Rambabu Gudavalli and Ivica Letunic and Peer Bork and Leszek Rychlewski and Bernhard Küster and Manuela Helmer-citterich and William N. Hunter and Rein Aasl and Toby J. Gibson},
title = {ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins},
journal = {Nucleic Acids Res},
year = {2003},
volume = {31},
pages = {3625--3630}
}
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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
