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MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteins

Sebastian Maurer-Stroh1*, Masaki Gouda2, Maria Novatchkova1, Alexander Schleiffer1, Georg Schneider1, Fernanda L Sirota3, Michael Wildpaner1, Nobuhiro Hayashi2 and Frank Eisenhaber1

Author Affiliations

1 IMP Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria

2 Division of Biomedical Polymer Science, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan

3 Service de Conformation de Macromolecules Biologiques et de Bioinformatique, Université Libre de Bruxelles, Boulevard du Triomphe - CP 263, 1050 Bruxelles, Belgium

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Genome Biology 2004, 5:R21  doi:10.1186/gb-2004-5-3-r21

Published: 13 February 2004


We evaluated the evolutionary conservation of glycine myristoylation within eukaryotic sequences. Our large-scale cross-genome analyses, available as MYRbase, show that the functional spectrum of myristoylated proteins is currently largely underestimated. We give experimental evidence for in vitro myristoylation of selected predictions. Furthermore, we classify five membrane-attachment factors that occur most frequently in combination with, or even replacing, myristoyl anchors, as some protein family examples show.