{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOdrug2.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOCon1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOCon2.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOdrug3.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOdrug1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOCon3.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOdrug1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOCon2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOdrug3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOdrug2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOCon3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069744/RKOCon1.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["ljingxin@sdu.edu.cn"],"submitter":["Dawei Chen"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Colon Cancer"],"software":[""],"submitter_keywords":["ppp1ca","gap","Gaba","Gaba; gap; ppp1ca"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069744"],"tissue":["Epithelial Cell","Cell Culture"],"sample_protocol":["For in-gel tryptic digestion, gel pieces were destained in 50 mM NH₄HCO₃ in 50% acetonitrile (v/v) until clear. Gel pieces were dehydrated with 100 μl of 100% acetonitrile for 5 min, the liquid removed, and the gel pieces rehydrated in 10 mM dithiothreitol and incubated at 56 °C for 60 min. Gel pieces were again dehydrated in 100% acetonitrile, liquid was removed and gel pieces were rehydrated with 55 mM iodoacetamide. Samples were incubated at room temperature, in the dark for 45 min. Gel pieces were washed with 50 mM NH₄HCO₃ and dehydrated with 100% acetonitrile. Gel pieces were rehydrated with 10 ng/μl trypsin resuspended in 50 mM NH₄HCO₃ on ice for 1 h. Excess liquid was removed and gel pieces were digested with trypsin at 37 °C overnight. Peptides were extracted with 50% acetonitrile/5% formic acid, followed by 100% acetonitrile. Peptides were dried to completion and resuspended in 2% acetonitrile/0.1% formic acid.   LC-MS/MS Analysis The tryptic peptides were dissolved in 0.1% formic acid (solvent A), directly loaded onto a home-made reversed-phase analytical column (15-cm length, 75 μm i.d.). The gradient was comprised of an increase from 6% to 23% solvent B (0.1% formic acid in 98% acetonitrile) over 16 min, 23% to 35% in 8 min and climbing to 80% in 3 min then holding at 80% for the last 3 min, all at a constant flow rate of 400 nl/min on an EASY-nLC 1000 UPLC system.  The peptides were subjected to NSI source followed by tandem mass spectrometry (MS/MS) in Q ExactiveTM Plus (Thermo) coupled online to the UPLC. The electrospray voltage applied was 2.0 kV. The m/z scan range was 350 to 1800 for full scan, and intact peptides were detected in the Orbitrap at a resolution of 70,000. Peptides were then selected for MS/MS using NCE setting as 28 and the fragments were detected in the Orbitrap at a resolution of 17,500. A data-dependent procedure that alternated between one MS scan followed by 20 MS/MS scans with 15.0s dynamic exclusion. Automatic gain control (AGC) was set at 5E4."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["The resulting MS/MS data were processed using Proteome Discoverer 1.3. Tandem mass spectra were searched against XXX database. Trypsin/P (or other enzymes if any) was specified as cleavage enzyme allowing up to 2 missing cleavages. Mass error was set to 10 ppm for precursor ions and 0.02 Da for fragment ions. Carbamidomethyl on Cys were specified as fixed modification and oxidation on Met was specified as variable modification. Peptide confidence was set at high, and peptide ion score was set > 20."],"omics_type":["Proteomics"],"labhead":["Jingxin Li"],"instrument_platform":[""],"labhead_affiliation":["Shandong University"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["greenlandice@live.com"],"publication":["Not available"],"submitter_affiliation":["IKMB, Kiel University"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic identification of GAP-binding proteins in colorectal cancer reveals PPP1CA as a direct target of microbial GABA-mediated metabolic rewiring","description":"This dataset corresponds to the proteomic analysis presented in Figure 6A of the manuscript “Obesity-driven microbial GABA depletion promotes metabolic rewiring and colorectal cancer progression.” We performed Drug Affinity Responsive Target Stability (DARTS) and co-immunoprecipitation proteomics using colorectal cancer cell lysates incubated with glyceraldehyde-3-phosphate (GAP) to identify GAP-binding proteins. Mass spectrometry data revealed PPP1CA as a key GAP-interacting protein mediating GABA-dependent suppression of YAP signaling. The dataset supports the mechanistic link between microbiota-derived GABA, TPI1-generated GAP, and YAP-regulated tumor metabolism in obesity-associated colorectal 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