Sample MS data

Samples (2 μg of yeast cell lysate + different spiked levels of UPS1) were analyzed in triplicate by nanoLC–MS/MS on an LTQ-Orbitrap Velos mass spectrometer. For more information on samples preparation and LC-MS/MS analyses, please refer to Ramus et al., J Proteomics. 2016 Jan 30;132:51-62. doi: 10.1016/j.jprot.2015.11.011.


SAMPLE RAW File Mascot dat File mzDB File
2µg levure UPS1 100fmol- Replicat 1 OEMMA121101_61b.raw F083068.dat OEMMA121101_61b.mzdb
2µg levure UPS1 100fmol- Replicat 2 OEMMA121101_63b.raw F083069.dat OEMMA121101_63b.mzdb
2µg levure UPS1 100fmol- Replicat 3 OEMMA121101_65b.raw F083070.dat OEMMA121101_65b.mzdb
2µg levure UPS1 10fmol – Replicat 1 OEMMA121101_36b.raw F083064.dat OEMMA121101_36b.mzdb
2µg levure UPS1 10fmol – Replicat 2 OEMMA121101_38b.raw F083066.dat OEMMA121101_38b.mzdb
2µg levure UPS1 10fmol – Replicat 3 OEMMA121101_40b.raw F083067.dat OEMMA121101_40b.mzdb
Short protocol description:
Peaklist were generated using the Extract_msn.exe macro provided with Xcalibur. Peaklists were submitted to Mascot database searches (version 2.5.1). ESI-TRAP was chosen as the instrument, trypsin/P as the enzyme and 2 missed cleavages were allowed. Precursor and fragment mass error tolerances were set at 5 ppm and 0.8 Da, respectively. Peptide variable modifications allowed during the search were: acetyl (Protein N-ter), oxidation (M), whereas carbamidomethyl (C) was set as fixed modification. Databases used were yeast database from UniprotKB (S_cerevisiae_ 20121108.fasta, 7798 sequences), a compiled database containing the UPS1 human sequences (48 sequences) and the corresponding reversed databases in order to calculate FDR.