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Proteins samples were subjected to in-solution digestion prior to labelling. Briefly, peptides were eluted from SepPak columns in 2 ml 50% ACN and fully dried in a vacuum concentrator at RT. Fully dried peptides were resuspended in 150 mM HEPES (pH 8.5) in 30% anhydrous acetonitrile. Peptide concentration was then accessed by 280nm absorption, using a Thermo Scientific Nanodrop 200 spectrophotometer (Thermo Scientific, USA); and peptide concentration was adjusted to the sample with the lowest concentration in the set (a minimum of 100 µg was used). Then, unlabeled peptides were mixed with TMTpro 16plex Isobaric label Reagent Set label (25 µg/ µL, A44522) in a ratio of (1:5 w/w), and incubated for 1 hour at room temperature, at 500 rpm in thermoshaker. Reactions were quenched by adding 5% hydroxylamine to an end concentration of 0.4% and incubated for at least 15 minutes at room temperature at 500 rpm. After this, a small aliquot of each sample was mixed in a 1:1 (v/v) proportion and pre-analyzed using mass spectrometry for labelling efficiency. Attending this data, samples concentration was adjusted for the final experiment for equimolar amounts of TMT-labelled peptides. Then, peptide samples were pooled attending the corrected ratios and purified in Sep-PAK columns; followed by fractionation in 8 fractions using micro-tip based strong cation exchange chromatography (Micro-SCX)37, using the following pH fractions for peptide elution: 3, 3.6, 3.9, 4.25, 4.8, 5.5, 7 and 11. Finaly, these fractions were desalted using C18-Stage tips, before injection in the equipment."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Peptide fractions labelled with 16plex TMTpro tags were analyzed using the quadrupole Orbitrap mass spectrometer Exploris 480 (Thermo Scientific, USA), equipped with a UHPLC system (EASY-nLC 1200, Thermo Scientific, USA) as described39,40. Labelled peptides were loaded onto C18 reversed-phase columns (55cm length packed in-house with ReproSil-Pur 120 C18-AQ 1.9-mm beads, Dr. Maisch GmbH)); and eluted with a 120-minute linear gradient of acetonitrile (2.4% to 33.6%) containing 0.1% formic acid. Eluted peptides were ionized via electrospray ionization, with the spray voltage being maintained at 1.5 to 2.2 kV, with the ion transfer tube temperature being set to 250 °C, and source RF lens set to 50%. The 20 most intense peptides, with charges ranging from +2 to +6, were sequentially isolated using the quadrupole within a 0.8 m/z isolation width window. Peptides were then fragmented using a nominal collision energy of 33%, though higher-energy C-trap dissociation (HCD), within a 10 ppm mass tolerance error. The Orbitrap MS1 scan was performed at R= 60 0000 at m/z= 400 , with a scan range of 300-1650 m/z, AGC target of 300% and a minimum intensity of 100000.  If a few precursors were found, restrictions would be relaxed.  For the Orbitrap MS2 scan, a R= 15000 at m/z=100 was used, with an AGC target of 100%, with a maximum injection time of 40 ms."],"omics_type":["Proteomics"],"labhead":["Petra Beli"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Institute of Molecular Biology (IMB), 55128 Mainz, Germany; Institute of Developmental Biology and Neurobiology (IDN), Johannes Gutenberg University, 55128 Mainz, Germany"],"species":["Homo Sapiens (human)"],"submitter_mail":["p.beli@imb-mainz.de"],"publication":["Not available"],"submitter_affiliation":["Institute of Molecular Biology (IMB), Mainz, Germany"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Alterations in proteome and proteostasis networks during replicative senescence","description":"The 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 total proteome, the ubiquitin-modified proteome, the phospho-proteome and in protein solubility during replicative senescence in human IMR90 fibroblasts. This accession contains the proteome data, across 4 distinct time points, with consecutive increasing concentrations of senescent 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