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. 2008 Dec;26(12):1339-40.
doi: 10.1038/nbt1208-1339.

PhosphoPep--a database of protein phosphorylation sites in model organisms

Bernd Bodenmiller, David Campbell, Bertran Gerrits, Henry Lam, Marko Jovanovic, Paola Picotti, Ralph Schlapbach, Ruedi Aebersold

PhosphoPep--a database of protein phosphorylation sites in model organisms

Bernd Bodenmiller et al. Nat Biotechnol. 2008 Dec.
No abstract available

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Figures

Figure 1
Figure 1
Figure 1A. Analysis of phosphorylation site conservation. As an example the yeast protein Hog1 is used. In the upper half, the orthologous proteins of Hog1 in worm, fly and human are displayed. In the lower half, the amino acid sequences of the proteins are shown and the identified phosphorylation sites are highlighted. It can be seen that the phosphorylation of the TXY motif, which is known to activate MAP kinases, is conserved between all species.
See this image and copyright information in PMC

References

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    1. Diella F, et al. Phospho. ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins. BMC Bioinf. 2004;5:79. - PMC - PubMed
    1. Gnad F, et al. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol. 2007;8:R250. - PMC - PubMed
    1. Bodenmiller B, et al. PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Mol Syst Biol. 2007;3:139. - PMC - PubMed
    1. Bodenmiller B, Mueller LN, Mueller M, Domon B, Aebersold R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat Methods. 2007;4:231–237. - PubMed

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