{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/Histone_Search.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3WT_Ctrl_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3WT_Ctrl_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3WT_Setd2_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3K36m_Ctrl_22.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3K36m_Ctrl_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3WT_Ctrl_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3K36m_Setd2_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3K36m_Ctrl_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3K36m_Setd2_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/20240822_Stephanie_Amy_H3WT_Setd2_3.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069619/Histones_Human_SwissProt_Sept2020.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["simone.sidoli@einsteinmed.edu"],"submitter":["Simone Sidoli"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Epigenetic vulnerability","Chromatin regulation","Setd2","Nsd2","H3k36m","Immune surveillance","H3k36 methylation","Ervs","Kras lung cancer","Ezh2"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069619"],"tissue":["Lung"],"sample_protocol":["Histone extraction and digestion Histone proteins were extracted from the pellet as described by (1) to ensure good-quality identification and quantification of single histone marks. Briefly, histones were acid-extracted with chilled 0.2 M sulfuric acid (5:1, sulfuric acid : pellet) and incubated with constant rotation for 4 h at 4oC, followed by precipitation with 33% trichloroacetic acid (TCA) overnight at 4oC. Then, the supernatant was removed and the tubes were rinsed with ice-cold acetone containing 0.1% HCl, centrifuged and rinsed again using 100% ice-cold acetone. After the final centrifugation, the supernatant was discarded and the pellet was dried using a vacuum centrifuge. The pellet was dissolved in 50 mM ammonium bicarbonate, pH 8.0, and histones were subjected to derivatization using 5 µL of propionic anhydride and 14 µL of ammonium hydroxide (all Sigma Aldrich) to balance the pH at 8.0. The mixture was incubated for 15 min and the procedure was repeated. Histones were then digested with 1 µg of sequencing grade trypsin (Promega) diluted in 50mM ammonium bicarbonate (1:20, enzyme:sample) overnight at room temperature. Derivatization reaction was repeated to derivatize peptide N-termini. The samples were dried in a vacuum centrifuge.  Sample desalting Prior to mass spectrometry analysis, samples were desalted using a 96-well plate filter (Orochem) packed with 1 mg of Oasis HLB C-18 resin (Waters). Briefly, the samples were resuspended in 100 µl of 0.1% TFA and loaded onto the HLB resin, which was previously equilibrated using 100 µl of the same buffer. After washing with 100 µl of 0.1% TFA, the samples were eluted with a buffer containing 70 µl of 60% acetonitrile and 0.1% TFA and then dried in a vacuum centrifuge.  LC-MS/MS Acquisition and Analysis Samples were resuspended in 10 µl of 0.1% TFA and loaded onto a Dionex RSLC Ultimate 300 (Thermo Scientific), coupled online with an Orbitrap Fusion Lumos (Thermo Scientific). Chromatographic separation was performed with a two-column system, consisting of a C-18 trap cartridge (300 µm ID, 5 mm length) and a picofrit analytical column (75 µm ID, 25 cm length) packed in-house with reversed-phase Repro-Sil Pur C18-AQ 3 µm resin. Peptides were separated using a 30 min gradient from 1-30% buffer B (buffer A: 0.1% formic acid, buffer B: 80% acetonitrile + 0.1% formic acid) at a flow rate of 300 nl/min. The mass spectrometer was set to acquire spectra in a data-independent acquisition (DIA) mode. Briefly, the full MS scan was set to 300-1100 m/z in the orbitrap with a resolution of 120,000 (at 200 m/z) and an AGC target of 5x10e5. MS/MS was performed in the orbitrap with sequential isolation windows of 50 m/z with an AGC target of 2x10e5 and an HCD collision energy of 30."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Histone peptides raw files were imported into EpiProfile 2.0 software (2). From the extracted ion chromatogram, the area under the curve was obtained and used to estimate the abundance of each peptide. In order to achieve the relative abundance of post-translational modifications (PTMs), the sum of all different modified forms of a histone peptide was considered as 100% and the area of the particular peptide was divided by the total area for that histone peptide in all of its modified forms. The relative ratio of two isobaric forms was estimated by averaging the ratio for each fragment ion with different mass between the two species. The resulting peptide lists generated by EpiProfile were exported to Microsoft Excel and further processed for a detailed analysis."],"omics_type":["Proteomics"],"labhead":["Simone Sidoli"],"instrument_platform":[""],"labhead_affiliation":["Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["simone.sidoli@gmail.com"],"publication":["Not available"],"submitter_affiliation":["Albert Einstein College of Medicine"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Antagonistic roles of histone 3 lysine methyltransferases dictate tumor immune surveillance","description":"Histone H3 lysine 36 (H3K36) methyltransferases are frequently mutated in cancer, but their functional roles remain unclear. Using functional genomics approaches within KRAS-driven lung cancer models, we show that NSD2, SETD2, and EZH2 work in concert to regulate expression of endogenous retroviral elements, which act as a molecular rheostat controlling immune surveillance. Specifically, loss of H3K36me2 and H3K36me3 activity through H3K36M oncohistone expression or H3K36me2 alone through NSD2 inactivation leads to derepression of endogenous retroviral element transcripts that activate a dsRNA-mediated antiviral-like immune response that potently eradicates KRAS-driven tumor growth. Surprisingly, derepression of ERV sequences and subsequent immune reactions are completely dependent on SETD2, a tumor suppressor in KRAS-driven lung cancer that directly mediates H3K36me3 deposition. Mechanistically, inactivation of both NSD2 and SETD2 attenuates immune reactions by activating EZH2-dependent H3K27me3 and transcript repression at ERV sequences. These findings define an enzymatic triad of NSD2, SETD2, and EZH2 whose coordinated activities link chromatin regulation and tumor immune surveillance, revealing new epigenetic vulnerabilities in 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