Deglycosylation and Digestion: 20 µg total protein were digested following previously described methods. Briefly, proteins were denatured and reduced with 10% SDS and 10 mM TCEP at 95°C for 10 minutes. 0.2% DCA was included as a passivating agent and 100 mM TEAB was included for buffering. Proteins were alkylated using 10 mM IAA for 30 minutes at room temperature in the dark. The alkylation reaction was quenched with 1.2% phosphoric acid. A protein suspension was formed by the addition of 100 mM TEAB in 90% methanol, and the suspension was spun onto an S-Trap device and washed following manufacturer's instructions. One µL PNGase F in 100 mM TEAB was added to the S-Trap to deglycosylate the proteins retained on the S-Trap and incubated at 37°C for 0, 2, or 4 hours. Proteins were then digested using 750 ng Trypsin Gold in 100 mM TEAB. Following digestion, peptides were eluted using 100 mM TEAB followed by 0.1% formic acid in water. The reaction was quenched with 10% FA and a third elution was performed with 50% acetonitrile (ACN) and 0.1% FA. All eluates were combined, peptides were desalted using ZipTips, and reconstituted at 200 ng/µL in 0.5% FA, 4% ACN for mass spectrometry analysis.