{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077818/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077818/evidence.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077818/peptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077818/proteinGroups.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077818/E2-R.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077818/EZH2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ouxj@sustech.edu.cn"],"submitter":["Zhijian Zhu"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Pull down","Ezh2"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077818"],"tissue":["Spleen","B Cell"],"sample_protocol":["LC-MS/MS experiments were performed on a Q Exactive HF-X mass spectrometer coupled to an Easy nLC1200 (Thermo Scientific). Peptides were first loaded onto a trap column (100 μm × 20 mm, 5 μm, C18, Dr. Maisch GmbH, Ammerbuch, Germany) using mobile phase A consisting of 0.1% formic acid in water. Reverse-phase high-performance liquid chromatography (RP-HPLC) separation was then carried out on a self-packed analytical column (75 μm × 150 mm; 3 μm ReproSil-Pur C18 beads, 120 Å, Dr. Maisch GmbH, Ammerbuch, Germany) at a flow rate of 300 nL/min.  Mobile phase A consisted of 0.1% formic acid in water, and mobile phase B consisted of 0.1% formic acid in 95% acetonitrile. The gradient elution program was as follows: 2%–4% B from 0 to 2 min, 4%–30% B from 2 to 47 min, 30%–45% B from 47 to 52 min, 45%–90% B from 52 to 54 min, and 90% B maintained from 54 to 60 min.  MS data were acquired in data-dependent acquisition (DDA) Top20 mode. The most abundant precursor ions from the full scan range of 350–1800 m/z were dynamically selected for HCD fragmentation. A lock mass of 445.120025 Da was used for internal mass calibration. Full MS scans were acquired at a resolution of 60,000 at m/z 200, and MS/MS scans at a resolution of 15,000 at m/z 200. The maximum injection time was set to 50 ms for MS and 25 ms for MS/MS scans. The normalized collision energy was 28, the isolation window was 1.6 Th, and the dynamic exclusion duration was 30 s."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["he MS data were analyzed using MaxQuant software version 1.6.1.0. MS data were searched against the UniProtKB Rattus norvegicus database (36080 total entries, downloaded 08/14/2018). The trypsin was seleted as digestion enzyme. The maximal two missed cleavage sites and the mass tolerance of 4.5 ppm for precursor ions and 20 ppm for fragment ions were defined for database search.  The database search results were filtered and exported with <1% false discovery rate (FDR) at peptide-spectrum-matched level, and protein level, respectively."],"omics_type":["Proteomics"],"labhead":["Xijun Ou"],"instrument_platform":[""],"labhead_affiliation":["southern university of science and technology"],"species":["Mus Musculus (mouse)"],"submission_type":["PARTIAL"],"publication":["Not available"],"submitter_mail":["zhuzhijian2017@gmail.com"],"submitter_affiliation":["southern university of science and technology"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"EZH2 pre-mRNA pull-down screening for proteins that regulate EZH2 alternative splicing","description":"Post-transcriptional regulation mediated by RNA-binding proteins is essential for B cell development and differentiation. EZH2 is a key regulatory protein involved in B cell development and the germinal center response, and its expression is subject to alternative splicing regulation. Skipping of exon 14 in EZH2 disrupts its catalytic activity for H3K27me3 deposition. To identify proteins that regulate EZH2 alternative splicing in B cells, we performed an RNA pull-down assay using exon 14 together with part of intron 14 of EZH2 pre-mRNA, followed by mass spectrometry analysis of the pulled-down 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