Extended Data Fig. 3: LC-MS/MS spectra of Ser48, Thr86, and Ser88 phosphorylated peptide and High-resolution (HR) MS/MS spectra of Ser88 phosphorylated peptides (NSTLSphEEDYIER) in BNIP3 protein. | Nature Metabolism

Extended Data Fig. 3: LC-MS/MS spectra of Ser48, Thr86, and Ser88 phosphorylated peptide and High-resolution (HR) MS/MS spectra of Ser88 phosphorylated peptides (NSTLSphEEDYIER) in BNIP3 protein.

From: STK3/STK4 signalling in adipocytes regulates mitophagy and energy expenditure

Extended Data Fig. 3: LC-MS/MS spectra of Ser48, Thr86, and Ser88 phosphorylated peptide and High-resolution (HR) MS/MS spectra of Ser88 phosphorylated peptides (NSTLSphEEDYIER) in BNIP3 protein.

a, Detection of phosphorylated peptide sequences in BNIP3 protein from MaxQuant. After comparative phosphoproteomic analysis, Ser48 and Thr86 phosphorylated peptides were identified and Ser88 were quantified using MaxQuant search program in BNIP3 (false discovery rate (FDR) <0.01, score>40). b, High-resolution (HR)-MS/MS spectra of 16O-labeled NSTLSphEEDYIER identified in BNIP3 overexpressed C3H10T1/2 adipocytes. c, HR-MS/MS spectra of 18O-labeled NSTLSphEEDYIER* identified in BNIP3 overexpressed C3H10T1/2 adipocytes after XMU-MP-1 for 4 h. d, HR-MS/MS spectra of the AQUA peptides for NSTL*SphEEDYIER synthesized with stable isotope-labeled L-leucine.

Back to article page