Additional file 2 of Correction to: Phospho-heavy-labeled-spiketide FAIMS stepped-CV DDA (pHASED) provides real-time phosphoproteomics data to aid in cancer drug selection

Additional file 2: Table S1. SBDS heavy-labeled phosphorylated peptide standards. Table S2. Common and unique phosphoproteins identifed across all four CVs based on PSM acquisition. Table S3. High confdence modifcation sites identifed in LFQ (p < 0.01). Table S4. High confdence modifcation sites identifed in pHASED (p < 0.01). Table S5. Unique and common phosphoproteins identifed in LFQ and pHASED datasets. Table S6. Phosphorylated master protein kinases identifed in LFQ dataset (p < 0.01). Table S7. Phosphorylated master protein kinases identifed in pHASED dataset (p < 0.01). Table S8. FLT3-D835 mutations associated with resistance to tyrosine kinase FLT3 inhibitors. Table S9. Kinase-Substrate analysis of LFQ dataset for resistant cells in comparison to FLT3-ITD (log2 fold change±0.5). Table S10. Kinase-Substrate analysis of pHASED data?set for resistant cells in comparison to FLT3-ITD (log2 fold change±0.5). Table S11. Canonical pathways identifed as signifcantly associated with LFQ dataset for resistant cells in comparison to FLT3-ITD. Table S12. Canonical pathways identifed as signifcantly associated with pHASED dataset for resistant cells in comparison to FLT3-ITD. Table S13. Kinase activity inferred by KSEA analysis of phosphorylation changes in pHASED dataset (log2±0.5, p≤0.05) for resistant cells in comparison to FLT3-ITD. Table S14. Mutation-specifc response to sorafenib. IC50 compared to FLT3-ITD. Table S15. Bliss Synergy scores for sorafenib in combination with KU-60019 at diferent doses. Table S16. Unique ATM substrates identifed with increased phosphorylation (log2≥0.5) in pHASED dataset for resistant cells in comparison to FLT3-ITD. Table S17. Vector mutations in FLT3 gene.