{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP.msfView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P.msfView"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP-8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP-7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P-8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P-7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP-4.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-P.pdResultView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD076568/BASP1-CP.pdResultView"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["moumj@zju.edu.cn"],"submitter":["Minjie Mou"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Breast Cancer"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076568"],"tissue":["Permanent Cell Line Cell","Cell Culture"],"sample_protocol":["The cells used for chemoproteomic experiments involving IDRB-Probe-1 and IDRB-CRP was MCF-7 cell line. All cells were passaged using the corresponding complete culture medium in an incubator set at 37 °C with 5% CO2 and saturated humidity. All cells used in chemoproteomic experiments were grown in 10-cm cell culture dishes to ∼90% confluence at the time of probe treatment. All dishes were washed twice with sterilized PBS and switched to serum-free DMEM. Probes were added to the cells at concentrations indicated in figures and mixed well before incubation for 1 h. For concentration-dependent experiments, two groups were established: (1) the probe group, treated with IDRB-Probe-1; and (2) the control group, treated with the control reference probe (IDRB-CRP) at the same concentration as the probe, serving as a null diazirine control. Following probe treatment, cells were pre-cooled to 4 °C and irradiated for 10 minutes at 365 nm to induce probe-protein crosslinking. Irradiated cells were washed twice with pre-chilled PBS and collected by scraping on ice. Cells were immediately lysed using lysis buffer (1×PBS, 1% Triton X-100 (v/v), 0.5% SDS (w/v), 1 × protease inhibitor cocktails) or stored at -80 °C until future use. Following cell lysis, the protein concentration was determined by BCA assay (BCA protein assay kit, catalog no. C503021, Sangon Biotech). Protein concentrations were adjusted to 2 mg/ml, and 1 mg of proteome was aliquoted in lysis buffer for further processing. Click reaction was performed by pre-mixing and adding the following reagents (per 500 µL sample): 10 µL Tris(3-hydroxypropyltriazolylmethyl)amine (THPTA) (5 mM in DMSO, final concentration 100 µM), 2.5 µL CuSO4 (200 mM in H2O, final concentration 1 mM), 2.5 µL fresh prepared sodium ascorbate (400 mM in H2O, final concentration 2 mM), and 1 µL Biotin-PEG3-Azide (50 mM in DMSO, final concentration 100 µM). For gel-based analysis, 1 µL TAMRA-Azide was used instead of Biotin-PEG3-Azide. The samples were then mixed well and incubated at room temperature with gentle rotation for 3 h. To remove excess click reagents, proteins were precipitated with methanol precipitation. Briefly, 2.5 mL of pre-chilled methanol was added to 500 µL of sample and incubated overnight at -20 °C. The protein pellets were then washed twice with 500 µL of pre-chilled methanol and resuspended in 250 µL resuspension buffer (1×PBS, 1% Triton X-100 (v/v), 0.5% SDS (w/v)). Subsequently, 3.2 µL of 5-Tris(2-carboxyethyl) phosphine hydrochloride (TCEP) (400 mM TCEP in 100 mM triethylammonium bicarbonate (TEAB) buffer, final concentration 5 mM) was added for the reduction of disulfide bond at 50 °C for 1 h, and 4.2 µL iodoacetamide (600 mM IAA in 100 mM TEAB buffer, final concentration 10 mM) was added for thiol alkylation at 37 °C in the dark for 30 minutes. Following reduction and alkylation, samples were added to prewashed streptavidin agarose beads (30 µL per sample) and incubated for protein enrichment at room temperature with gentle rotation for 4 h. Agarose beads were precipitated using Pierce centrifuge columns, washed three times with 600 µL 6M urea, three times with PBS, and three times with TEAB. Following washing, enriched proteins were digested using 1.5 µg trypsin overnight at 37 °C with gentle shaking. The next day, digested peptides were collected by centrifugation. The beads were further washed twice with 100 µL 50 mM TEAB pH 8.5 and once with 200 µL 50% ACN in water. For each sample, the flow-through and wash solutions were combined and evaporated to dryness for downstream TMTpro labeling. Collected peptides were resuspended in 10 µL 50 mM TEAB buffer and labeled with TMTpro reagents according to the manufacturer’s instructions. The reaction was quenched by incubation with 2 µL 5% hydroxylamine for 15 minutes. All TMTpro-labeled samples were pooled, dried and evaporated to dryness. The proteome was dissolved in 300 µL 0.1% trifluoroacetic acid (TFA) in HPLC grade water and then fractionated using the Pierce high pH reversed-phase peptide fractionation kit according to the manufacturer’s instructions. The lyophilized fractions were dissolved in 10 µL of 0.1% formic acid (FA) in MS grade water and stored at -80 °C before LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["All MS data were acquired using an Orbitrap Fusion Lumos mass spectrometer in line with a Dionex UltiMate™ 3000 RSLCnano system. Solvent A was 0.1% formic acid in MS water, while solvent B was 0.1% formic acid in 98% acetonitrile. Peptides were separated on an NTC C18 Plus column (1.7 µm 250 mm x 75 µm, catalog number 26350-4-25S) using a 130-minute gradient of 5-27% buffer B over 91 minutes, 27%-98% buffer B over 24 minutes, 98% buffer B for 5 minutes, 98%-2% buffer B over 1 minute, and 2% buffer B for 9 minutes, at a flow rate of 350 nL/min. The eluted peptides were directly introduced into the Thermo Fisher Orbitrap Fusion Lumos MS system for data-dependent MS/MS analysis for TMTpro quantification. The MS full scans were acquired in an m/z range of 375 to 1650 in profile mode, with the AGC target set at 4E6, dynamic exclusion of 60 seconds, and the maximum injection time set at 50 ms. The resolution of the full MS scan was set to 120,000 in the Orbitrap. For the subsequent MS2 analysis, the 15 most intense ions with charge states between 2+ and 7+ were selected. The AGC target of MS2 analysis was set to 7.5E4 with a quadruple isolation window width of 0.5 m/z. The peptide ions were fragmented using higher energy collision dissociation (HCD) at a NCE of 34, and the resolution of the MS2 scan was set to 50,000 in the Orbitrap. All acquired MS raw data were searched utilizing Proteome Discoverer v.2.5 from Thermo Fisher Scientific. For all experiments, spectral data were searched against a custom FASTA-formatted database that included common contaminants and Homo sapiens proteome data (UniProt reviewed sequences, downloaded in 2023) with the following parameters: sequence database search engine SEQUEST-HT, 10 ppm precursor mass tolerance, 0.1 Da fragment mass tolerance, fully tryptic peptides, two maximum cleavages, carbamidomethylation of cysteine residues (+57.0214 Da) and TMTpro tags (+304.207 Da) on lysine and peptide N-termini set as static modifications, while oxidation of methionine residues (+15.9949 Da) was set as a dynamic modification. Peptide spectral matches were filtered to achieve a peptide false discovery rate (FDR) of 1%. For TMTpro quantification, only PSMs with an average signal-to-noise (S:N) ratio of >3 ions matched to the identified peptide sequence were retained. Additionally, only proteins identified by at least two unique peptides were retained. Processed proteomic data were exported from Proteome Discoverer and further analyzed using Python."],"omics_type":["Proteomics"],"labhead":["Minjie Mou"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Zhejiang University, China"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["moumj@zju.edu.cn"],"submitter_affiliation":["Zhejiang University"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"The raw data of chemoproteomics related to IDRB-Probe-1 for validating the effectiveness of iTarget.","description":"The eight raw files starting with 'BASP1-P' represent the chemoproteomic experiment of multiple concentrations of IDRB-Probe-1 in MCF-7. Each concentration includes three measurements taken from distinct samples.126, 127N and 127C represent the data of 0.5 μM IDRB-Probe-1. 128N, 128C and 129N represent the data of 1.5 μM IDRB-Probe-1. 129C, 130N and 130C represent the data of 5 μM IDRB-Probe-1. 131N, 131C and 132N represent the data of 15 μM IDRB-Probe-1. 132C, 133N and 133C represent the data of 50 μM IDRB-Probe-1. 134N, 134C and 135N represent the data of 100 μM IDRB-Probe-1. The eight raw files starting with 'BASP1-CP' represent the chemoproteomic experiment of multiple concentrations of IDRB-CRP in MCF-7. Each concentration includes three measurements taken from distinct samples. 134N, 134C and 135N represent the data of 0.5 μM IDRB-CRP. 132C, 133N and 133C represent the data of 1.5 μM IDRB-CRP. 131N, 131C and 132N represent the data of 5 μM IDRB-CRP. 129C, 130N and 130C represent the data of 15 μM IDRB-CRP. 128N, 128C and 129N represent the data of 50 μM IDRB-CRP. 126, 127N and 127C represent the data of 100 μM IDRB-CRP.","dates":{"publication":"2026-05-06","submission":"2026-04-03"},"accession":"PXD076568","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:11294","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:487521","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:2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