{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/FBXO7delNdelC_TMTchannel_summary.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/sa05138.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/sa05141.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/sa05139.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/sa05142.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/36575_sa05138_O7delNdelC.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/36578_sa05142_O7delNdelC.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/36577_sa05141_O7delNdelC.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/36576_sa05139_O7delNdelC.mzid"],"Mzxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/sa05138_O7delNdelC.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/sa05142_O7delNdelC.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/sa05139_O7delNdelC.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077028/sa05141_O7delNdelC.mzXML"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["wade_harper@hms.harvard.edu"],"submitter":["Ellen Goodall"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Human","Parkinson's disease","Ip-ms","Fbxo7"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077028"],"tissue":["Cell Culture"],"sample_protocol":["HEK293T FBXO7-/- PSMF1-/- cells expressing FLAG-HA-FBXO7 constructs were seeded into 150 mm plates with one plate per replicate and performed in triplicate. Once plates reached confluency, or approximately 20 x 10^6 cells per replicate, cells were scraped in ice cold phosphate buffered saline, pelleted at 500 x g and snap frozen in liquid nitrogen. To begin the immunoprecipitation, all cell pellets were thawed on ice and each mixed end-over-end with lysis buffer (50 mM HEPES pH 7.6, 140 mM NaCl, 0.5% IGEPAL-CA630 (v/v), protease inhibitors: 1 mM PMSF, 10 µM leupeptin, 1.5 µM pepstatin A, 5 µg/mL aprotinin and Benzonase nuclease (Novagen)) for 30 minutes at 4˚C.  Lysates were clarified by centrifugation at 21 000 x g for 30 minutes at 4˚C followed by total protein quantification using Pierce BCA (cat#: 23250). Normalized protein inputs were incubated with 20 µL of prewashed anti-FLAG M2 magnetic beads (Sigma cat#: M8823) for 3 hours, mixing on orbital plate mixer at 800 rpm at 4˚C.  Using a Kingfisher Flex (Thermo, RRID:SCR_027576) samples were washed first with 500 µL with low detergent buffer (50 mM HEPES pH 7.6, 140 mM NaCl, 0.1% IGEPAL-CA630 (v/v)), followed by three washes, each of 500 µL of wash buffer (50 mM HEPES pH 7.6, 140 mM NaCl). Finally, beads were eluted with mixing in 75 µL of elution buffer (50 mM HEPES pH 7.6, 140 mM NaCl 0.15 mg/mL, 0.15 mg/mL FLAG peptide). Immunoprecipitations were reduced with 5 mM TCEP for 15 minutes, alkylated with 10 mM iodoacetamide for 20 minutes in the dark, quenching the reaction with 15 mM DTT. Following reduction and alkylation, peptide digestion was performed on beads following buffer exchange using SP3 method [Hughes et al. 2019] adapted for the Kingfisher Flex. Each sample was incubated with 28 µL of a 1:1 mixture carboxylate modified, magnetic SpeedBeads of 1µm average and 0.7-1.10 µm average diameter (Cytiva cat #:65152105050250 and cat #:45152105050250) as a 5% slurry. After incubating these samples for 5 minutes, samples were mixed with an equal volume of pure ethanol, then washed three times, each with 200 µL of 80% ethanol before digestion overnight at 37˚C with agitation on a microplate mixer with sequencing grade modified trypsin (Thermo Scientific, cat#: 90059) and Lys-c (Fujifilm Wako cat#: NC9242798).  Following digestion, peptide-containing buffer was transferred to a fresh plate for labeling with TMTpro 18 reagents (Thermo), removing the remaining SpeedBeads and incubated for 90 minutes hour at 25˚C in a solution containing 30% (v/v) acetonitrile. Following labeling each sample was quenched with 0.5% hydroxylamine (w/v), pooled in equal ratios, diluted to a final concentration of 5% acetonitrile and acidified with formic acid. The pooled sample was desalted using a C18 StageTip [Rappsilber, Mann, and Ishihama 2007] , dried in a vacuum centrifuge and resuspended in 5% formic acid, 5% acetonitrile for analysis by liquid chromatography and tandem mass spectrometry (LC-MS). Mass spectrometric data were collected on an Orbitrap Ascend MultiOmics mass spectrometer coupled to a Vanquish Neo UHPLC. Approximately 1 µg of peptide was separated at a flow rate of 300 nL/min on a 100 µm capillary column that was packed with 35 cm of Accucore 150 resin (2.6 μm, 150Å; ThermoFisher Scientific). The gradient was 7-25% Buffer B (95% acetonitrile, 0.125% formic acid) which was mixed into buffer A (5% acetonitrile, 0.125% formic acid) over a 135 min gradient. The scan sequence began with an MS1 spectrum (Orbitrap analysis, resolution 60,000, 350-1350 Th, automatic gain control (AGC) target is set to 100%, maximum injection time set to 50ms, RF lens was set to 30%). The hrMS2 stage consisted of fragmentation by higher energy collisional dissociation (HCD, normalized collision energy 36%) and analysis using the Orbitrap (AGC 200%, maximum injection time 120 ms, isolation window 0.7 Th, resolution 45,000 with TurboTMT activated). Data were acquired using the FAIMSpro interface the dispersion voltage (DV) set to 5,000V, the compensation voltages (CVs) were set at -30V, -50V, and -70V. The sample was analyzed twice with the second acquisition using a different set of CV (-40V, -60V, and -80V). The number of dependent scans was set to 25 scans per MS1 per CV. Dynamic exclusion list (duration=120s) was shared among CVs."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Peptides from each sample were analyzed using an in-house pipeline. Briefly, .raw files are converted to .mzml files using MSConvert [Chambers 2012] and assigned using Comet [JK Eng 2013] with a sequence database containing the canonical human proteome (Uniprot Reference proteome: HUMAN_UP000005640), modified to include eGFP, common sample prep contaminants, FLAG epitope tag, and decoy peptides consisting of reverse sequences [Elias 2007]. Peptide mass tolerance and fragment ion tolerance were set to 50ppm and 0.02 Da, respectively. Peptide modifications included: TMTpro labels as fixed modification +304.207 Da on lysines and peptide N-termini, carboxyamidomethylation as fixed modification +57.021 Da on cysteine, and oxidation as variable modification on methionine +15.995 Da. Peptide-spectrum matches were filtered by LDA [Huttlin 2010] to 1% false discovery rate(FDR) [Elias and Gygi 2007]. TMT-reporter ions were quantified and corrected for isotopic impurity."],"omics_type":["Proteomics"],"labhead":["J. Wade Harper"],"instrument_platform":[""],"labhead_affiliation":["Harvard Medical School Cell Biology Department"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"publication":["10.64898/2026.05.28.728263"],"submitter_mail":["ellen_goodall@hms.harvard.edu"],"submitter_affiliation":["Harvard Medical School"],"submitter_country":["United States"],"doi":["10.6019/PXD077028"],"additional_accession":[]},"is_claimable":false,"name":"FLAG-IP, FLAG-FBXO7 samples with domain deletions of FBXO7 variants, with or without FBXO7","description":"Triplicate FLAG-Immunoprecipitations of FLAG-tagged FBXO7 constructs (full length (1-522), ∆N (169-522), ∆C (1-406), and ∆N∆C (169-406)) overexpressed in FBXO7-/- PSMF1-/- HEK293T cells. FBXO7∆N∆C co-overexpressed with full length PI31(1-271) is also included. Parental cells lacking tagged FBXO7 are included as a negative control for non-specific binding in the IP. Identities of each sample and their layout by TMT channel are included as 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