Methylarginine datasets from Maron et al If used, please cite the iScience paper below
Spreadsheets with data from Maron et al, iScience (2021) https://doi.org/10.1016/j.isci.2021.102971
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Supplemental Table S1 - Transcriptomic and Proteomic Consequence of Type I and PRMT5 inhibition, related to Figure 4. Sheets 1 and 2 highlight transcriptomic changes promoted by either GSK591 or MS023 treatment relative to DMSO, respectively, as determined by DESeq2. Sheets 3 and 4 demonstrate proteomic changes promoted by either GSK591 or MS023 treatment relative to DMSO, respectively, as determined by either trypsin or GluC digestion.
Supplemental Table S2 - PTMScan identified methylarginine modified residues, related to Figures 3, 6, 7, and 8. PTMScan identified methylarginine modified residues from either trypsin or GluC digests with IDR information
Supplemental Table S3 - PTMScan identified methylarginine modified peptides and their Type I PRMT- or PRMT5-dependent abundance, related to Figure 6. Methylarginine modified peptides and their abundance changes due to either GSK591 or MS023 treatment relative to DMSO. Peptides are categorized based on immunoprecipitation strategy (Rme1/MMA, Rme2a/ADMA, or Rme2s/SDMA) and protease digestion (either trypsin or GluC).
Supplemental Table S4 - Table S4. Human proteome characteristics, related to Figure 7. . Compiled human proteome molecular weight, hydrophobicity, isoelectric point, and predicted intrinsic disorder.
Supplemental Table S5 - Table S5. Compiled publicly available human methylarginine sites, related to Figure 7. All identified human methylarginine sites across publicly available datasets (Fedoriw et al., 2019; Fong et al., 2019; Guo et al., 2014; Hornbeck et al., 2015; Larsen et al., 2016; Li et al., 2021; Lim et al., 2020; Musiani et al., 2019; Wei et al., 2020).