Published March 26, 2024 | Version v4
Journal article Open

ATR phosphoproteomics - DHX9 validation

Creators

  • 1. MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK
  • 2. MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK; Department of Microbial and Molecular Systems (M2S), Centre for Food and Microbial Technology (CLMT), Laboratory of Enzyme, Fermentation and Brewing Technology (EFBT), Technology Campus Ghent, Ghent, Belgium
  • 3. CHU de Quebec Research Center,Oncology Division, Dept. of Molecular Biology, Medical Biochemistry and Pathology, Laval University Cancer Research Center, 9 McMahon Drive, Quebec Cit, QC G1R 3S3, Canada
  • 4. Dept of Human Genetics, Leiden University Medical Center, Einthovenweg 20, 2333 ZC  Leiden, Netherlands
  • 5. Division of Molecular, Cell and Developmental Biology, School of Life Sciences, Wellcome Trust Biocentre, University of Dundee, DD1 5EH, UK
  • 6. EMD Serono, Research Unit Oncology, EMD Serono, Billerica, MA, USA
  • 7. Dept of Human Genetics, Leiden University Medical Center, Einthovenweg 20, 2333 ZC  Leiden, Netherlands, Oncode Iinstitute, Utrecht, The Netherlands

Description

Data analysis scripts for the validation of DHX9 as ATR substrate. Annotated spectra also available. Further, the exported Skyline transition data for the DHX9 (p)S321 peptide from HeLa and HEK293 cells is provided. Within the Skyline files, the Replicates ending with A1-3 are the ATRi treated samples, C1-3 the Chk1i treated samples, and H1-3 the untreated controls. The non-phosphopeptide precursor has an m/z of 538.2802, the phospho-peptide precursor of 578.2633.

Files

20240314_DHX9_HeLa_Transition_Results_Skyline.csv

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