Update publication information. Kidney tissue samples were ground and pulverized in liquid nitrogen and transferred into low protein binding tubes and lysed with 300 µL lysis buffer supplemented with 1 mM PMSF. Then, samples were further lysed with sonication on ice. The parameters were set as 1s/1s intervals, 3 min, and 80 Watts of power. After sonication, samples were centrifuged at 12,000 g for 10 min at room temperature to remove insoluble particles that were repeated once to further exclude precipitation. Protein concentration was determined by Bradford assay and the samples were aliquoted and stored at -80 °C. Total proteins (15 µg) of each sample were acquired and separated by 12% SDS-PAGE gel. All samples were then trypsinized and labeled. The labeling peptide solutions were lyophilized and stored at -80 °C. Protein separation was performed on an 1100 HPLC System (Agilent) using an Agilent Zorbax Extend RP column (5 μm, 150 mm × 2.1 mm). Tryptic peptides were separated at a flow rate of 300 μL/min and monitored at 210 and 280 nm. Dried samples were harvested from 8 min to 50 min and elution buffer was collected every minute and numbered from 1-10 with the pipeline. The separated peptides were lyophilized for MS detection. The MS/MS data were analyzed for protein identification and quantification using Proteome Discoverer TM 2.2 (ThermoFisher Crop.). The local false discovery rate was estimated with the integrated PSPEP tool in the ProteinPilot Software to be 1.0% after searching against a decoy concatenated uniport Mus musculus protein database.