{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report-first-pass.unique_genes_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report-first-pass.gg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report-first-pass.pg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report.pr_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report-first-pass.stats.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report.gg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report.unique_genes_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report-first-pass.pr_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report.stats.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report.pg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report-first-pass.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/report.log.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/206_2024_GS-5min-R3-E.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/206_2024_GS-5min-R2-E.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/227_2024_GS-DMSO-R1-E.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/227_2024_GS-DMSO-R3-E1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/227_2024_GS-DMSO-R2-E.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077594/206_2024_GS-5min-R1-E.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["g.sapkota@dundee.ac.uk"],"submitter":["Gajanan Sathe"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Astral","Dia"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077594"],"tissue":["Kidney Epithelial Cell"],"sample_protocol":["HEK293  cells were treated with d BET6 and DMSO for 15 minutes.The cells were lysed by 8M urea buffer in 50 mM TEABC, both buffers contain protease and phosphatase inhibitor cocktail tablets. All steps for urea lysis were carried out at room temperature to avoid carbamylation. Proteins were measured by BCA protein estimation method. The described amount of proteins were used for in solution digestion. For urea lysis protein were reduced using 5mM DTT for 60 min at RT, followed by alkylation using 10 mM CAA for 20 min at RT in dark. This were incubated with LysC for 4h in (1:100) enzyme to protein ratio. After LysC the lysate were diluted with 50 mM TEABC to reduce the concentration of urea less than 2M. Trypsin with (1:20) enzyme to substrate were used for the in-solution digestion and incubated 12-16 hr at RT. The reaction was quenched with the addition of trifluoroacetic acid (TFA) to give a final concentration of 1% TFA (v/v) and samples were desalted on 200 mg Sep-Pak C18 cartridges (Waters). For Sep-Pak clean-up, the following solvents were prepared fresh: activation solvent (100% (v/v) acetonitrile (ACN)); Solvent-1 (0.1% (v/v) TFA); Solvent-2 (0.1% (v/v) formic acid (FA)); Solvent-3 (50% (v/v) ACN in 0.1% (v/v) FA). Sep-Pak cartridges were equilibrated with 5 mL 100% ACN, followed by 5 mL 50% ACN, 0.1% FA and finally with 5 mL 0.1% TFA twice. Samples were then loaded onto the equilibrated C18 cartridges, washed with 5 mL 0.1% TFA four times, followed by washing with 5 mL 0.1% FA. Samples were then eluted with 6 mL 50% ACN, 0.1% FA. Desalted samples were then dried to completeness in a SpeedVac concentrator. These dried peptides were used for the DiGly immunoprecipitation.  For Astral MS peptides were analysed on an Orbitrap Astral mass spectrometer coupled to a Thermo Fisher Scientific Vanquish Neo UHPLC system. Samples were first loaded onto a trap column and subsequently separated on an analytical column (Easy-Spray PepMap Neo, 2 μm C18, 75 μm × 150 mm) at a flow rate of 800 nL/min. Peptide separation was achieved using a gradient reaching 22.5% solvent B at 14 minutes and 35% at 21 minutes, followed by re-equilibration to 9%, resulting in a total run time of 22.6 minutes. Data were acquired in data-independent acquisition (DIA) mode using the Astral analyzer. Full MS scans were recorded in the Orbitrap over an m/z range of 380–980 at a resolution of 240,000, with a fixed cycle time of 5 ms. The AGC target was set to 500%, and ion injection times were dynamically determined. Precursor ions were isolated using a 4 Th window and fragmented by higher-energy collisional dissociation (HCD) at a normalized collision energy of 25%. For DIA scans, a mass range of 150–2000 m/z was used, with an AGC target of 500%, dynamic injection times, and detection performed in the Astral analyzer."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The raw data files acquired in DIA mode were processed using DIA-NN, version 1.8 (https://github.com/vdemichev/DiaNN). Human UniProt was used as protein sequence database. Two missed cleavages and a maximum of two variable modifications per peptide were allowed (acetylation of protein N-termini and oxidation of methionine). Carbamidomethylation of cysteines was set as fixed modification and K-GG was added as dynamic modification. This data analysis was carried out using library-free analysis mode in DIA-NN by enabling “deep learning-based spectra and RTs prediction”. Match between the runs (MBR) was enabled"],"omics_type":["Proteomics"],"labhead":["Prof Gopal Sapkota"],"instrument_platform":[""],"labhead_affiliation":["MRC Investigator, University of Dundee"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["gsathe001@dundee.ac.uk"],"publication":["Not available"],"submitter_affiliation":["Centre for Targeted Protein Degradation (CeTPD)\nUniversity of Dundee"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Ubiquitinome Profiling: Optimizing the enrichment and Data-Independent Analysis for Deeper Insights into Targeted Protein Degradation","description":"Targeted protein degradation has emerged as a highly promising therapeutic strategy for a wide range of diseases, including cancer and neurodegenerative disorders. The ubiquitin-proteasome system, which is responsible for protein degradation, plays a critical role in this process. Gaining comprehensive insights into the landscape of ubiquitination events is essential for the development of effective targeted protein degradation approaches. In recent years, data-independent analysis (DIA) has gained significant popularity as a robust and unbiased approach for quantitative proteomics. By leveraging on this method, we have developed a cutting-edge workflow that combines diGly antibody-based enrichment with an optimized Orbitrap-based data-independent acquisition method for the identification of ubiquitylated 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