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Nucleic Acids Res. 2018 Jan 4;46(D1):D428-D434. doi: 10.1093/nar/gkx1077.

The eukaryotic linear motif resource - 2018 update.

Author information

1
Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg 69117, Germany.
2
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest H-1117, Hungary.
3
European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
4
Protein Structure-Function and Engineering Laboratory, Fundación Instituto Leloir and IIBBA-CONICET, Buenos Aires CP 1405, Argentina.
5
Departamento de Fisiología y Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires CP 2160, Argentina.
6
Instituto de Investigaciones Biotecnoltógicas, Universidad Nacional de General San Martín, IIB-INTECH-CONICET, San Martín, Buenos Aires CP 1650, Argentina.
7
UCD School of Medicine & Medical Science, University College Dublin, Belfield, Dublin 4, Ireland.
8
Ruprecht-Karls-Universität, Heidelberg 69117, Germany.
9
Department of Science and Technology, Universidad Nacional de Quilmes, CONICET, Bernal B1876BXD, Buenos Aires, Argentina.
10
Leibniz-Institute on Aging, Fritz Lipmann Institute (FLI), Jena D-07745, Germany.

Abstract

Short linear motifs (SLiMs) are protein binding modules that play major roles in almost all cellular processes. SLiMs are short, often highly degenerate, difficult to characterize and hard to detect. The eukaryotic linear motif (ELM) resource (elm.eu.org) is dedicated to SLiMs, consisting of a manually curated database of over 275 motif classes and over 3000 motif instances, and a pipeline to discover candidate SLiMs in protein sequences. For 15 years, ELM has been one of the major resources for motif research. In this database update, we present the latest additions to the database including 32 new motif classes, and new features including Uniprot and Reactome integration. Finally, to help provide cellular context, we present some biological insights about SLiMs in the cell cycle, as targets for bacterial pathogenicity and their functionality in the human kinome.

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