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BeliMass SpectrometryBottom-up proteomicsData-independent acquisitionOtubd pulldownBortezomib treatmentReplicative senescenceImr90 modelhttps://www.ebi.ac.uk/pride/archive/projects/PXD077923Fibroblast Of LungPulldown of proteins modified by ubiquitin was carried out using the OtUBD probe38. The OtUBD probe was conjugated to SulfoLink Coupling Resin (Thermo Fisher Scientific, USA) and then used for pulldown of ubiquitylated proteins in denaturing conditions, using a protocol adapted from Zhang et al., 202238. Briefly, cells were directly lysed in denaturing buffer (8 M urea, 100 mM NaCl, 50 mM TEAB). Protein concentrations were quantified using Bradford, and 1 mg of protein was used for the pulldown. The beads were pre-incubated with 2 bed volumes of elution buffer (100 mM glycine-HCl, pH 2.5) and equilibrated using 20 bed volumes of column buffer (50 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, 0.5% Triton-X, 10% glycerol, pH 7.5). The protein lysate was diluted 1:1 with native lysis buffer (50 mM Tris-HCl, 300 mM NaCl, 1 mM EDTA, 0.5% Triton-X100, pH 7.5) to reduce urea concentration to 4 M, and samples were incubated overnight, with rotation, at 4°C with the OtUBD-conjugated beads. The beads were then washed sequentially with column buffer, wash buffer-1 (50 mM Tris-HCl, 150 mM NaCl, 0.05% Tween 20, pH 7.5), wash buffer-2 (50 mM Tris-HCl, 1 M NaCl, pH 7.5), and ultrapure water. Finally, ubiquitylated proteins were eluted from the beads by incubation with SDS buffer (50 mM Tris-HCl, pH 6.8, 2% SDS, 5% glycerol, 100 mM DTT, 0.005% bromophenol blue) with heating at 65°C, 500 rpm, for at least 30 minutes. In-gel based digestion was used, where proteins were mixed in a 1:1 volume ratio with 1×NuPAGE LDS Sample Buffer (Life Technologies) with 1 mM DTT and heated at 70°C for 10 minutes. After cooling down, proteins were alkylated using 5.5 mM chloroacetamide and allowed to incubate for 30 minutes in the dark at RT. Samples were then loaded onto Bis-Tris NuPAGE gels (Life Technologies) and allowed to run approximately 1 cm into the resolving gel, followed by fixing using a fixing solution (50% methanol, 10% acetic acid) and staining with a Colloidal Blue staining kit (Life Technologies) following the manufacturer’s instructions. Each lane was then cut into small cubes (~1 mm³) that were subsequently destained (25 mM ammonium bicarbonate, 50% ethanol) and dehydrated (100% ethanol, for 10 minutes). After dehydration, gel pieces were rehydrated with trypsin solution (T6567, Sigma, Germany; 12.5 μg/mL in 50 mM ammonium bicarbonate), and the digestion reaction was allowed to proceed overnight at 37°C. After protein trypsinization, peptide extraction buffer (30% ACN, 3% trifluoroacetic acid (TFA)) was added to stop the reaction, and peptides were extracted in three steps using successively increasing concentrations of ACN: peptide extraction buffer solution, buffer B (80% ACN, 0.5% acetic acid) and 100% ACN. Peptide-enriched supernatants were then combined and concentrated using vacuum centrifugation at 45°C to decrease ACN concentration to < 30% (v/v). Samples were then acidified using TFA solution to pH < 2 and loaded onto C18 StageTips for desalting before MS injection.PrideNot availableDIA raw files were analyzed using DIA-NN v2.02 Academia software85. We started by generating a spectral library, using the UniProtKB/Swiss-Prot file from the analysis of the DDA-data as a reference, using the DIA-NN pipeline for library generation. All libraries were generated considering the raw data needed to be analyzed. The DIA raw files were analyzed with the predicted library, allowing for N-terminal M excision, C carbamidomethylation on cysteine and 2 missed cleavages. The number of variable modifications was set to 5. Oxidation was enabled as a variable modification. Peptide range was set from 7 to 30; with precursor charges enabled from +1 to +4. A precursor range of 350 – 1,050 m/z was used, as well as a fragment ion range of 150 – 2,000 m/z. Mass tolerance was automatically inferred by DIA-NN. False discovery rates were set to 1% at both protein and peptide levels.ProteomicsPetra BeliInstitute of Molecular Biology (IMB), 55128 Mainz, Germany; Institute of Developmental Biology and Neurobiology (IDN), Johannes Gutenberg University, 55128 Mainz, GermanyPARTIALHomo Sapiens (human)Not availablep.beli@imb-mainz.deInstitute of Molecular Biology (IMB), Mainz, GermanyGermanyfalseAlterations in proteome and proteostasis networks during replicative senescenceThe accumulation of senescent cells constitutes a pivotal hallmark of tissue ageing, contributing to disruption of tissue homeostasis and thus, to the development of several aging-related diseases. Despite this, our knowledge about the molecular, spatial and temporal changes that drive aging on a cellular basis remains poorly understood. To elucidate these mechanisms, we employed mass spectrometry-based proteomics to determine changes in the proteome and its post translational modifications, as well as protein solubility, during replicative senescence in human IMR90 fibroblasts. This accession contains data regarding alterations on the ubiquitin-modified proteome, in control and Bortezomib-treated conditions.2026-07-162026-05-01PXD077923NEWT:6945NEWT:3555NEWT:2NEWT:157546NEWT:35554NEWT:38942NEWT:307972NEWT:32046NEWT:544496NEWT:2042546NEWT:45351NEWT:43179NEWT:4513NEWT:5722NEWT:376741NEWT:55153NCBITaxon:10407NEWT:1736309NEWT:1211601NEWT:876138NEWT:237561NEWT:5833NEWT:6928NEWT:10036NEWT:36745NEWT:1351NEWT:1438992NEWT:2649997NEWT:272563NEWT:224326NCBITaxon:79857NEWT:1096976NEWT:95648NEWT:3885NEWT:3888NEWT:1589NEWT:135622NEWT:6915NEWT:3649NEWT:101510NEWT:3880NEWT:272559NEWT:3641NEWT:383379NEWT:10029NEWT:1000589NEWT:85963NEWT:85962NEWT:317447NEWT:7955NEWT:7959NEWT:2261NEWT:31156NEWT:4565NEWT:1264690NEWT:515619NEWT:192875NEWT:34305NEWT:59729NCBITaxon:183674NEWT:224308NEWT:84645NEWT:626528NEWT:139927NEWT:4558NEWT:209285NEWT:1283NEWT:931281NEWT:4550NEWT:1000561NEWT:197NCBITaxon:79824NEWT:4787NCBITaxon:4563NEWT:5755NEWT:44689NEWT:3218NEWT:5759NEWT:1736231NEWT:1270NEWT:2242NEWT:4784NEWT:11320NEWT:360106NEWT:287NEWT:10117NEWT:10239NEWT:10116NEWT:1280NEWT:1735272NEWT:83334NEWT:83332NEWT:44685NEWT:317513NEWT:1148NEWT:580240NEWT:294128NEWT:11676NEWT:55571NEWT:100226NEWT:4530NEWT:4896NEWT:75058NEWT:13616NEWT:1094343NEWT:296543NEWT:1773NEWT:1895NEWT:1182590NEWT:935293NEWT:64152NEWT:4924NEWT:749200NEWT:990346NEWT:145953NEWT:257309NEWT:100816NEWT:263NEWT:230741NEWT:52283NEWT:284812NCBITaxon:1313NEWT:43330NEWT:408169NEWT:44544NEWT:4911NEWT:645463NEWT:3702NEWT:129249NEWT:990119NEWT:408172NEWT:408170NEWT:493760NEWT:260710NEWT:257313NEWT:400772NEWT:3708NEWT:128161NEWT:332648NEWT:106592NEWT:536231NEWT:460519NEWT:1432138NEWT:10312NEWT:1424507NCBITaxon:1773NEWT:9598NEWT:8030NEWT:1639NEWT:188229NEWT:3818NEWT:480NEWT:4909NEWT:67767NEWT:432359NEWT:46835NEWT:2711NEWT:376686NEWT:95486NEWT:9103NEWT:29159NEWT:10306NCBITaxon:2759NEWT:1233435NEWT:8022NEWT:145943NCBITaxon:4932NEWT:595536NEWT:240906NEWT:593117NEWT:3635NEWT:5811NEWT:235443NEWT:272624NEWT:411483NEWT:884019NEWT:198215NEWT:411490NEWT:983964NEWT:169963NEWT:32644NEWT:499175NEWT:476272NEWT:3747NEWT:367830NEWT:178616NEWT:410289NEWT:373153NEWT:352472NEWT:360094NEWT:470NEWT:1313NEWT:411469NEWT:84023NEWT:559292NCBITaxon:5811NEWT:411464NEWT:411460NEWT:2762NEWT:1174673NEWT:562NEWT:411470NEWT:33952NEWT:2094720NCBITaxon:2697049NEWT:28038NEWT:1423NEWT:4932NEWT:3603NEWT:2759NEWT:3847NEWT:327159NEWT:178876NEWT:327160NEWT:573NEWT:9031NEWT:7091NEWT:241368NEWT:42528NEWT:190802NEWT:9778NEWT:150475NEWT:9417NEWT:7111NEWT:347515NEWT:1216979NEWT:5180NEWT:256737NEWT:115104NEWT:1121114NEWT:1081927NEWT:1238993NEWT:67825NEWT:185579NEWT:13076NEWT:1249668NEWT:317NEWT:7227NEWT:7469NEWT:885318NEWT:9402NEWT:415540NEWT:550NEWT:675060NEWT:4081NEWT:554NEWT:98334NEWT:426428NEWT:7574NEWT:7215NEWT:575412NEWT:29204NEWT:2172103NEWT:507601NCBITaxon:6157NEWT:746360NEWT:6239NEWT:470150NEWT:216257NEWT:102169NEWT:9986NEWT:4054NEWT:73239NEWT:226186NEWT:1268063NEWT:8782NEWT:1263854NEWT:435590NEWT:1902NEWT:160488NEWT:28104NEWT:1908NCBITaxon:2NEWT:985076NEWT:1215323NEWT:52641NEWT:7038NEWT:6192NEWT:28532NCBITaxon:38727NEWT:353152NEWT:2829NEWT:366581NEWT:216599NEWT:216595NEWT:243230NEWT:8355NEWT:9685NEWT:7029NEWT:1080772NEWT:1283300NEWT:6183NEWT:6063NEWT:334747NEWT:61235NEWT:6289NEWT:436486NEWT:6287NEWT:300641NEWT:727NEWT:9796NEWT:725NEWT:170187NEWT:260707NCBITaxon:6191NEWT:1836NEWT:185431NEWT:29760NEWT:260704NEWT:703612NEWT:260705NEWT:80863NEWT:2697049NEWT:105231NEWT:1216981NCBITaxon:6073NEWT:884204NEWT:6279NEWT:1123869NEWT:9544NEWT:7370NEWT:83906NEWT:607699NEWT:6282NEWT:208964NEWT:1134506NEWT:575584NEWT:38783NEWT:8727NEWT:4006NEWT:8726NEWT:6426NEWT:6669NEWT:10090NEWT:4120NEWT:51515NEWT:5693NEWT:8724NEWT:51511NEWT:92867NEWT:8723NEWT:5334NEWT:37334NEWT:382352NCBITaxon:10359NEWT:242619NEWT:632957NEWT:373995NEWT:5689NEWT:544404NEWT:9925NEWT:8839NEWT:4232NEWT:2758385NEWT:4113NEWT:837NEWT:11298NEWT:171101NEWT:714NEWT:421932NEWT:196627NEWT:5691NEWT:48479NEWT:627025NEWT:1097677NEWT:61674NEWT:1117957NEWT:9913NEWT:4100NEWT:1076NEWT:6763NEWT:803NEWT:29722NEWT:380394NEWT:1692259NEWT:180066NEWT:135588NEWT:1843183NEWT:58002NEWT:326423NEWT:4577NEWT:1416333NEWT:5664NEWT:2157NEWT:1678078NEWT:749906NEWT:418985NEWT:146479NEWT:1911079NEWT:264203NEWT:1480154NEWT:1274414NEWT:27606NEWT:59202NEWT:9975NEWT:9612NEWT:38865NEWT:51953NEWT:3197NEWT:9615NEWT:10299NEWT:860688NEWT:36329NEWT:1147787NCBITaxon:3044782NEWT:72407NEWT:349741NEWT:9605NEWT:9606NEWT:157295NEWT:641501NEWT:7668NEWT:915099NEWT:74940NEWT:9721NEWT:137221NEWT:1450511NEWT:1143193NEWT:411901NEWT:9838NEWT:105884NCBITaxon:9615NEWT:58334NEWT:1193501NEWT:3055NEWT:58331NEWT:6326NEWT:6689NEWT:5476NEWT:1274432NEWT:1274426NEWT:70448NEWT:9825NEWT:1274423NEWT:393765NEWT:698936NEWT:39946NEWT:9823NEWT:9940NEWT:521001NEWT:39947NEWT:1274420NEWT:5784580000-0001-9507-9820