{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/conditions_NS0909-2.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/output_NS0909-2.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/parameters.setup_NS0909-2.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/setup.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-40.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-26.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-33.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-32.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-35.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/oecf5-NS0909-30.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/NS0909_new.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/2025-01-21_UP000000589_10090_one_prot_seq_per_gene.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070740/contaminants.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["w.palm@dkfz-heidelberg.de"],"submitter":["Wilhelm Palm"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Mefs","Lysosomal enzymes","Lysosomes","Secretome","Wdr7","Iko","Secreted proteins"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070740"],"tissue":["Embryonic Fibroblast"],"sample_protocol":["Samples were centrifugated for 5 min at 15,000 rpm at room temperature. Supernatants were transferred to fresh Eppendorf tubes and mixed with an equal amount of RIPA buffer. Concentrations were determined using BCA assay. 10 µg protein was digested (trypsin) using an AssayMAP Bravo liquid handling system (Agilent technologies) running the autoSP3 protocol according to Müller et al. (PMID: 32129943). Dried peptide samples were reconstituted (97.4% Water, 2.5% Hexafluoro-2-propanol and 0.1% trifluoroacetic acid), and equivalent of 1 µg was used for the analysis. An LC-MS/MS analysis was carried out using a Vanquish Neo UPLC system (Thermo Fisher Scientific) directly connected to an Orbitrap Exploris 480 mass spectrometer for a total of 60 min per sample. Peptides were online desalted on a trapping cartridge (Acclaim PepMap300 C18, 5 µm, 300 Å wide pore; Thermo Fisher Scientific) with a loading volume of 60 µl using 30 µl/min flow of 0.05% TFA in water. The analytical multistep gradient (300 nl/min) was performed with a nanoEase MZ Peptide analytical column (300Å, 1.7 µm, 75 µm x 200 mm, Waters) using solvent A (0.1% formic acid in water) and solvent B (0.1% formic acid in acetonitrile). For 45 min the concentration of B was linearly ramped from 5% to 30%, followed by a quick ramp to 80%, after four minutes the concentration of B was lowered to 2% and a three column volumes equilibration appended. Eluting peptides were analyzed in the mass spectrometer using data independent acquisition (DIA) mode. A full scan at 120k resolution (350-1400 m/z, 300% AGC target, 45 ms maxIT) was followed 20 DIA windows. The DIA acquisition covered a mass range of 400-1000 m/z using windows of a variable width. Windows overlapped by 1 m/z, the AGC target was 1000% with a maxIT of 54 ms and spectra were recorded at a resolution of 30k. Each sample was followed by a wash run (22 min) to minimize carry-over between samples. Instrument performance throughout the course of the measurement was monitored by regular (approx. one per 48 hours) injections of a standard sample and an in-house shiny application."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["All sample handling (sample preparation and LC-MS/MS analysis) were performed in block randomization (PMID: 32969222) order. Analysis of DIA RAW files was performed with Spectronaut ((Biognosys, version 20.2.250922.92449; Bruderer R. et al (PMID: 25724911) in directDIA+ (deep) library-free mode. Default settings were applied with the following adaptions. Within DIA Analysis under Identification the Precursor PEP Cutoff was set to 0.01, the Protein Qvalue Cutoff (Run) set to 0.01, the Protein PEP Cutoff set to 0.01 and Run-level Protein scoring set to Highest Sxoring Observation (SN19 default). In Quantification the Proteotypicity Filter was set to Only Protein Group Specific, the Protein LFQ Method was set to MaxLFQ, Cross-Run Normalization was disabled and the Quantification window was set to Not Synchronized (SN 17). In Post Analysis Use All MS-Level Quantities was set to True. The data was searched against the mouse proteome from Uniprot (mouse reference database with one protein sequence per gene, containing 21,757 unique entries from January 2025), the Cas9 sequence and the contaminants FASTA from MaxQuant (246 unique entries from August 2025). Conditions were included in the setup."],"omics_type":["Proteomics"],"labhead":["Dr. Wilhelm Palm"],"instrument_platform":[""],"labhead_affiliation":["German Cancer Research Center (DKFZ) Cell Signaling and Metabolism Division Head"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["w.palm@dkfz-heidelberg.de"],"publication":["10.1038/S44318-026-00838-5"],"submitter_affiliation":["German Cancer Research Center (DKFZ)"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Secretome from Wdr7 iKO MEFs","description":"Extracellular medium was collected from Wdr7 iKO MEFs after 24h in OptiMEM, and  secreted proteins were 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