{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/list_of_raw_files_uploaded.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/Mass_spectrometry-TurboID-results.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-03_FTMSms2hcd.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-04_FTMSms2hcd.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-07_FTMSms2hcd.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-13_FTMSms2hcd.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-05_FTMSms2hcd.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-12_FTMSms2hcd.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-11_FTMSms2hcd.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-08_FTMSms2hcd.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077507/S20231013-09_FTMSms2hcd.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["manish.aghi@ucsf.edu"],"submitter":["Juan Oses-Prieto"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Glioblastome","Acp1","Turboid","Aurkb"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077507"],"tissue":["Glioblastoma Cell Line"],"sample_protocol":["The biotinylation of proximal proteins of ACP1 and AURKB was performed via lentiviral transduction using a TurboID vector C1(1-29)-TurboID-V5_pLX304 (Addgene 107175). The coding sequences for the amino acids of ACP1 and AURKB were cloned onto this vector using Gibson Assembly (NEB Gibson Assembly Master Mix, E2611S). The protein sequences of ACP1 and AURKB were PCR amplified from expression plasmids obtained from Origene (ACP1, CAT#: RC212653; AURKB, CAT#: RC210288). Cells transduced with TurboID were subjected to 10 µg/ml blasticidin selection. Prior to collection, GBM43 cells were treated with 10 µM biotin and incubated at 37°C for 10 minutes. Protein lysates were prepared using RIPA buffer, and after calibrating protein concentrations, streptavidin magnetic beads (Thermo Fisher, 88816) were added to the lysates and incubated at room temperature for one hour to allow bead-protein conjugation without introducing unspecific binding. Following the washing protocol (RIPA, KCL, Na2CO3, and Urea) (55), eluted proteins from the beads were collected for western blot analysis. Protein lysates were verified using antibodies against the V5 protein tag and biotin, and the streptavidin beads were sent for iTRAQ/TMT-based mass spectrometry analysis. In preparation for digestion, sample-incubated streptavidin magnetic beads were resuspended in 9.4 µl of 5 mM Tris(2-carboxyethyl)phosphine (TCEP) 20mM triethylammonium bicarbonate (TEAB) pH 8.5, and incubated for 30 min at 56°C. After this, iodoacetamide was added to a final concentration of 7.5 mM and samples incubated for 30 additional minutes at room temperature. 1 µg of MS grade trypsin (Thermo Scientific) was added to each sample and incubated at 37°C overnight. After that, supernatants were recovered in clean 0.6 ml low protein binding vials, and 10 µl of TEAB containing 1 µg of trypsin was added to each sample and incubated at 37°C for 4 hours. Supernatants of the beads were recovered into the same set of low protein binding tubes as before, and acidified with 5% formic acid. Peptides were recovered by solid phase extraction using C18 ZipTips (Millipore) and resuspended in 0.1% formic acid for analysis by LC-MS/MS."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peak lists were generated using PAVA in-house software (Guan, S., Price, J.C., Prusiner, S.B., Ghaemmaghami, S., and Burlingame, A.L. (2011). A data processing pipeline for mammalian proteome dynamics studies using stable isotope metabolic labeling. Mol Cell Proteomics 10, M111 010728).  All generated peak lists were searched against the human subset of the SwissProt database (SwissProt.2019.07.31) using Protein Prospector (Clauser, K.R., Baker, P., and Burlingame, A.L. (1999). Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Analytical chemistry 71, 2871-2882) . The database search was performed with the following parameters: a mass tolerance of 10 ppm for precursor masses; 30 ppm for MS/MS, cysteine carbamidomethylation as a fixed modification and acetylation of the N terminus of the protein, pyroglutamate formation from N terminal glutamine, and oxidation of methionine as variable modifications. A refined search was performed based on the results of this first search, correcting the systematic error of the distribution (3.65 ppm) and allowing a mass tolerance of 10 ppm for precursor masses All spectra identified as matches to peptides of a given protein were reported, and the number of spectra (Peptide Spectral Matches, PSMs) used for label free quantitation of protein abundance in the samples."],"omics_type":["Proteomics"],"labhead":["Manish K. Aghi"],"instrument_platform":[""],"labhead_affiliation":["Professor. Neurological Surgery. Tong-Po Kan Chair in Neurological Surgery. UCSF Weill Institute for Neurosciences University of California San Francisco (UCSF)"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["joses@cgl.ucsf.edu"],"publication":["Not available"],"submitter_affiliation":["UCSF"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"TurboID proximity labelling and label free proteomic analysis of AURKB and ACP1 in GBM43 human glioblastoma cells","description":"Here we are using unbiased proteomic analysis based on proximity labelling and TurboID coupled to MS to try to identify specific interactors of AURKB and ACP1 in GBM43 human glioblastoma 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