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Novel phosphorylation sites on H+-ATPase proteins

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Presentation on theme: "Novel phosphorylation sites on H+-ATPase proteins"— Presentation transcript:

1 Novel phosphorylation sites on H+-ATPase proteins
Novel phosphorylation sites on H+-ATPase proteins.Top, MS/MS spectra for the phosphopeptides E889AVNIFPEKGpSYR901 of ATPase 2 (At4g30190) and ELpSEIAEQAK (conserved between ATPase 1 (At2g18960) and ATPase 2). Novel phosphorylation sites on H+-ATPase proteins.Top, MS/MS spectra for the phosphopeptides E889AVNIFPEKGpSYR901 of ATPase 2 (At4g30190) and ELpSEIAEQAK (conserved between ATPase 1 (At2g18960) and ATPase 2). Bottom, ClustalW analysis of the C termini of ATPase isoforms 1–11 of Arabidopsis. The identified phosphopeptides are underlined and phosphorylated residues printed in bold. The peptide ELpSEIAEQAK comes from either AHA1 or AHA2; the peptide LKGLDIETIQQAYYpTV from either AHA4 or AHA11. Thomas S. Nühse et al. Mol Cell Proteomics 2003;2: © 2003 The American Society for Biochemistry and Molecular Biology


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