Change search
ReferencesLink to record
Permanent link

Direct link
ELM: the status of the 2010 eukaryotic linear motif resource.
Show others and affiliations
2010 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 38Article in journal (Refereed) Published
Abstract [en]

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 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.

Place, publisher, year, edition, pages
2010. Vol. 38
National Category
Bioinformatics and Systems Biology
URN: urn:nbn:se:uu:diva-282509DOI: 10.1093/nar/gkp1016PubMedID: 19920119OAI: diva2:917137
Available from: 2016-04-05 Created: 2016-04-05 Last updated: 2016-04-07Bibliographically approved

Open Access in DiVA

fulltext(2521 kB)7 downloads
File information
File name FULLTEXT01.pdfFile size 2521 kBChecksum SHA-512
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Sayadi, Ahmed
In the same journal
Nucleic Acids Research
Bioinformatics and Systems Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 7 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 17 hits
ReferencesLink to record
Permanent link

Direct link