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 http://elm.eu.org/ 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.

Gould, C., Diella, F., Via, A., Puntervoll, P., Gemünd, C., Chabanis Davidson, S., et al. (2010). ELM: the status of the 2010 eukaryotic linear motif resource. NUCLEIC ACIDS RESEARCH, 38(Database issue), D167-D180 [10.1093/nar/gkp1016].

ELM: the status of the 2010 eukaryotic linear motif resource

HELMER CITTERICH, MANUELA;
2010-01-01

Abstract

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 http://elm.eu.org/ 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.
1-gen-2010
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/11 - BIOLOGIA MOLECOLARE
English
Con Impact Factor ISI
Computational Biology; Protein Structure, Tertiary; Amino Acid Motifs; Animals; Internet; Eukaryotic Cells; Humans; Databases, Nucleic Acid; Information Storage and Retrieval; Sequence Homology, Amino Acid; Databases, Genetic; Software; Databases, Protein; Molecular Sequence Data; Amino Acid Sequence
http://nar.oxfordjournals.org/content/38/suppl_1/D167.long
Gould, C., Diella, F., Via, A., Puntervoll, P., Gemünd, C., Chabanis Davidson, S., et al. (2010). ELM: the status of the 2010 eukaryotic linear motif resource. NUCLEIC ACIDS RESEARCH, 38(Database issue), D167-D180 [10.1093/nar/gkp1016].
Gould, C; Diella, F; Via, A; Puntervoll, P; Gemünd, C; Chabanis Davidson, S; Michael, S; Sayadi, A; Bryne, J; Chica, C; Seiler, M; Davey, N; Haslam, N; Weatheritt, R; Budd, A; Hughes, T; Pas, J; Rychlewski, L; Travé, G; Aasland, R; HELMER CITTERICH, M; Linding, R; Gibson, T
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/14881
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