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Following treatment, cells  were harvested by scraping on ice and pelleted by centrifugation for 5 minutes at 300 × g at 4 °C. Pelleted cells were washed twice with cold PBS and resuspended in five volumes of cell lysis buffer (150 mM NaCl, 50 mM Tris pH 8.0, 1 mM EDTA, 10% glycerol, 1% NP-40, 1 mM DTT, and CPI). Per condition, approximately 750 μg whole cell extract was incubated with Streptavidin Sepharose High- Performance beads and 2 μL of 10mg/ml ethidium bromide (Sigma, E1510) for 2 hours in a rotation wheel at 4 °C. For all washing steps, beads were pelleted by centrifugation at 2,000 × g for 2 minutes at 4°C. The beads were washed twice with RIPA buffer (25 mM TRIS, 7.5 pH, 150 mM NaCl, 1% NP-40, 1% Sodium deoxycholate, 0.1% SDS, 0.5 mM DDT and CPI), twice with PBS containing 1% NP40 and twice with PBS. Beads were resuspended in 50 μL of elution buffer (2 M urea, 100 mM Tris pH 8.0, 10 mM DTT) and incubated for 20 minutes at room temperature in a thermo shaker at 1,250 rpm. Then, iodoacetamide (50 mM) was added to the beads and incubated for an additional 10 minutes in the dark while shaking. Next, 0.25 μg trypsin was added, and incubated for 2 hours at room temperature in a thermo shaker at 1,250 rpm. The supernatant was transferred to new tubes and further digested overnight at room temperature with an additional 0.1 μg of trypsin. Peptide solutions were acidified with 1% TFA and desalted using homemade C18 StageTips. Digested peptides were eluted from homemade C18 StageTips using buffer B (0.1% formic acid, 80% acetonitrile) and reconstituted in buffer A (0.1% formic acid) to a final volume of 12 μL. Samples (3 μL) were loaded onto a Vanquish Neo nano-LC system (Thermo Scientific) coupled to an Orbitrap Astral mass spectrometer (Thermo Scientific) operating in data-independent acquisition (DIA) mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw mass spectrometry data were processed using DIA-NN (version 1.9.2) with a library-free search strategy and match-between-runs enabled. Protein identification was performed using a FASTA file of the Homo sapiens proteome, downloaded from UniProt in June 2024 (UniProtKB proteome ID: UP000005640). Additionally, a FASTA file containing common contaminants from the cRAP database (April 2019 release) was included as a contaminant list. Trypsin was specified as the proteolytic enzyme, allowing for up to two missed cleavages. Cysteine carbamidomethylation, methionine oxidation, N-terminal methionine excision, and N-terminal acetylation were included as modifications, with a maximum of five variable modifications per peptide."],"omics_type":["Proteomics"],"labhead":["Prof. Michiel"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Molecular Biology, Faculty of Science, Radboud Institute for Molecular Life Sciences, Oncode Institute, Radboud University Nijmegen, 6525 GA Nijmegen, The Netherlands"],"species":["Homo Sapiens (human)"],"publication":["42561940 Alejo-Vinogradova MT,Strøm YE,Lamers LA,Chang YW,Hendriksen MJ,Moosajee M,Vermeulen M,Stelloo S From stem cells to somites: Revealing genetic and exogenous factors of human embryogenesis. Stem Cell Reports. 2026 Aug 6:103023 10.1016/j.stemcr.2026.103023"],"submitter_mail":["stelloo@science.ru.nl"],"submitter_affiliation":["Department of Urology, Radboud University Medical Center (RUMC), Nijmegen, The Netherlands"],"submitter_country":["Netherlands"],"additional_accession":[]},"is_claimable":false,"name":"P300 proximity labeling in human iPSCs","description":"This dataset presents the results of proximity-dependent biotinylation targeting the transcriptional coactivator p300 in human induced pluripotent stem cells (hiPSCs). We endogenously tagged p300 with the biotin ligase miniTurboID, to enable labeling of proximal proteins and thus proteins locatd at enhancers. hiPSCs were cultured in two different conditions, either StemFit or mTeSR medium, to assess how media composition influences the p300 proximal proteome. Following biotin labeling, proteins were enriched via streptavidin pulldown and analyzed by 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