Aldosterone rapidly alters activity of the thiazide-sensitive NaCl cotransporter to modulate renal NaCl excretion
Description
These data contain phosphopeptides/phosphoproteins identified from mass spectrometry based proteomic studies using cultured mpkDCT cells (originally derived from microdissected mouse distal convoluted tubules) stimulated with 1nM aldosterone (Aldo) for 30 mins. Data are from control/Aldo treated conditions combined. All data are obtained from polarized mpkDCT cells grown on semi-permeable membrane supports. Mass spectrometry was carried out on a Q Exactive mass spectrometer (Thermo Scientific) with a top 10 data dependent scan and dynamic exclusion enabled. Data were searched using SEQUEST and MASCOT against the uniprot mouse protein database (dated 26/01/2018). Only rank 1 and high confidence (with a target-decoy false discovery rate below 0.01) peptides were used. A protein (one gene symbol) is considered identified if it has at least one identified peptide sequence that is a unique match to a singleprotein accession number. The phosphorylation sites identified were assigned to the protein sequences corresponding to their protein accession number. Peptide sequences matched with multiple accession numbers for the same gene symbol (e.g. isoforms) are included for protein identifications. The column "Peptide Count" lists numbers of different unique peptides identified for the matched proteins. The confidence of phosphorylation site assignment was evaluated by phosphoRS score (Proteome Discoverer, Thermo Scientific). Phosphorylation sites marked with a "?" meaning that they have a phosphoRS score of lower than 80, and that they are ambiguously assigned. Phosphorylation sites marked with a "*" meaning that they are confidently assigned. Site and motif conservation scores were generated using CPhos.