{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_3.xlsx"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_urea_DDA_2.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_2.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_urea_DDA_1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_1.msfView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_urea_DDA_3.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_3.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_urea_DDA_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_urea_DDA_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_urea_DDA_1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_2.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_1.pdResultView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_3.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057960/HEK293_MG132_6H_STRAP_DDA_3.pdResultView"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["g.sapkota@dundee.ac.uk"],"submitter":["Gajanan Sathe"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Digly","Protac","Dia"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057960"],"tissue":["Kidney"],"sample_protocol":["HEK293 cells (ATCC, CRL-1573) were treated with 20 µM MG132 for 6h, washed twice with ice-cold PBS, and scrapped in freshly prepared 2% SDS buffer in 50 mM TEABC or 8 urea in 50mM buffer. The SDS buffer contained 2% SDC, 10 mM TCEP, 40 mM CAA, 50 mM TEABC at pH = 8.5. The urea buffer contained 8 M urea in 50 mM TEABC, both buffers contain protease and phosphatase inhibitor cocktail tablets. The SDS lysates were heated to 95 °C for 10 min and then sonicated using a ultrasonic probe device (1 min, energy output ~40%). The cells in urea lysate were sonicated and lysate centrifuged, and supernatant were used for the in-solution digestion. All steps for urea lysis were carried out at room temperature to avoid carbamylation. After urea/SDS lysis cells the proteins were measured by BCA protein estimation method. The described amount of proteins were used for in solution digestion. For SDS lysis S-Trap™ midi spin column digestion protocol was used. Cells were lysed in 2% SDS, heated for 95 c for 10 minutes, followed by sonication, centrifugation for 12,000 rpm for 10 minutes. Supernatant were taken and protein measured by BCA method. The SDS concentration were adjusted to 5% using 10% SDS. 1/10 volume of the 12% phosphoric acid added to the lysate, followed by 7-fold volume of wash buffer containing (90% methanol in 10% TEABC). This final lysate was passed through the S-trap column. After that column were wash 4 times with 3ml of the binding buffer. (1:10) trypsin to protein concentration were used for digestion. The column was incubated at 47 c for 1 hr followed by 12 h. at RT. The digested peptides were eluted using 50 mM TEABC, 0.1% formic acid followed by 50% ACN. The peptide solution was dried using speedvac and directly used for the DiGly enrichment. 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 agarose bead enrichment, cross-linked antibodies were used. The antibodies were washed with IAP buffer. The dried peptides were dissolved in 1 mL of IAP buffer. The peptide solution was then centrifuged at 12,000 rpm for 10 minutes, and the supernatant was added to agarose beads cross-linked with DiGly antibodies. These solutions were incubated on a rotator at 4°C for 2 hours with end-over-end rotation. After incubation, the beads were washed twice with 1 mL of IP buffer, followed by an additional wash with cold Milli-Q® water. After removing all the supernatant, the beads were incubated with 200 µL of 0.15% TFA at room temperature while shaking at 1,400 rpm. After a brief spin, the supernatant was recovered and desalted using in-house prepared, 200 µL two-plug StageTips. These peptides were analyzed on an Orbitrap Exploris 480 mass spectrometer interfaced with Dionex Ultimate 3000 nanoflow liquid chromatography system. The dried peptides were reconstituted in 0.1% formic acid and loaded on a trap column (Acclaim PepMap100 C18, 100 μm × 2 cm, 5 μm, 100 Å) and separated on an analytical column (Acclaim PepMap RSLC C18, 75 μm × 50 cm, 2 μm, 100 Å) at a flow rate of 250 nL/min using a step gradient of 0–8% solvent B (90% ACN/0.1% FA) for the first 12 min, followed by 8–25% up to 110 min, 25-37% for 110-125 min. The total run time was set to 145 min. For DDA analysis MS scan the resolution was 120,000, normalised AGC target is 300%. For MS2 the ions were fragmented using HCD with collision energy 30, AGC target is 3000%, resolution was 30,000."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The proteomics DDA raw data were searched using SEQUEST HT search engines with Proteome Discoverer 2.4 (Thermo Fisher Scientific). The following parameters were used for searches: Database: human proteome from uniport, Precursor mass tolerance 10 ppm, Fragment mass tolerance 0.02, Enzyme: trypsin, Mis-cleavage: −2, Fixed modification: carbamidomethylation of cysteine residues, Dynamic modification: oxidation of methionine and GG modification of lysine. The data were filtered for 1% PSM, peptide level."],"omics_type":["Proteomics"],"labhead":["Prof Gopal Sapkota"],"instrument_platform":[""],"labhead_affiliation":["Professor MRC PPU 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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