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The gel pieces washed with water and dehydrated in acetonitrile. The bands were then reduced with DTT and alkylated with iodoacetamide prior to the in-gel digestion. All bands were digested in-gel using trypsin, by adding 5 μL 10 ng/μL trypsin or chymotrypsin in 50 mM ammonium bicarbonate and incubating overnight digestion at room temperature to achieve complete digestion. The peptides that were formed were extracted from the polyacrylamide in two aliquots of 30µL 50% acetonitrile with 5% formic acid.  These extracts were combined and evaporated to <10 μL in Speedvac and then resuspended in 1% acetic acid to make up a final volume of ~30 μL for LC-MS analysis. The LC-MS system was a ThermoScientific Fusion Lumos mass spectrometry system. The HPLC column was a Dionex 15 cm x 75 µm id Acclaim Pepmap C18, 2μm, 100 Å reversed-phase capillary chromatography column. Five μL volumes of the extract were injected and the peptides eluted from the column by an acetonitrile/0.1% formic acid gradient at a flow rate of 0.25 μL/min were introduced into the source of the mass spectrometer on-line. The microelectrospray ion source is operated at 2.5 kV. The digest was analyzed using the data dependent multitask capability of the instrument acquiring full scan mass spectra to determine peptide molecular weights and product ion spectra to determine amino acid sequence in successive instrument scans."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["The data were analyzed using Proteome Discoverer V2.4 with the search engine Sequest which is integrated in PD software and the parameters used were default settings for an Orbitrap instrument.  Search Parameters Program: Protein ID Proteome Discoverer v2.4  Database Mouse SwissProtKB Downloaded on 3-23-2022 Entries 17552  Protease Trypsin, full  Missed Cleavages 2  Mass Accuracy 10 ppm MS1 0.5 Da MS2  Variable Modifications Oxidation of Met N-terminal Acetyl: Protein  Static Modifications Carbamidomethylation of Cis  Program: Protein/Peptide validation Scaffold vs 5.0.1  Protein ID Requirements 2 Peptides, 1 unique  FDR Rate: Peptide Peptide Prophet 0.1%  FDR Rate: Protein Peptide Prophet 1%"],"omics_type":["Proteomics"],"labhead":["Dr. Wen-Cheng Xiong"],"instrument_platform":[""],"labhead_affiliation":["Department of Neurosciences, School of Medicine, Case Western Reserve University, 10900 Euclid Ave, Cleveland, Ohio, 44106"],"submission_type":["COMPLETE"],"species":["Mus Musculus (mouse)"],"submitter_mail":["willarb@ccf.org"],"publication":["Not available"],"submitter_affiliation":["Cleveland Clinic"],"submitter_country":["United States"],"doi":["10.6019/PXD079754"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic Analysis of Plasma Membrane Proteins in Atp6ap2 (PRR)-Deficient Osteoblast-Lineage Cells","description":"ATP6AP2 (also known as PRR) is required for osteocyte maturation and cortical bone development. To identify downstream effectors of ATP6AP2, plasma membrane-enriched proteins were isolated from control and Atp6ap2-deficient osteoblast-lineage cells and analyzed by mass spectrometry. Comparative proteomic analysis identified MMP14 as a major ATP6AP2-regulated membrane protein. These data support a role for ATP6AP2 in regulating MMP14 surface localization and osteocyte 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