{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/StudyDescription_HEK293T_Pervanadate_C6-CysPAT.xlsx"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/241024_CysPAT_Per15_eclipse_OxC.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/241024_CysPAT_Per15_eclipse_input.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/241024_CysPAT_Per15_eclipse_input_OxC.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/241024_CysPAT_Per15_eclipse.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_08_Per15_CysPAT_Phos_enriched_fraction8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_03_Per15_CysPAT_Phos_enriched_fraction3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_01_Per15_CysPAT_Phos_enriched_fraction1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_06_Per15_CysPAT_Phos_enriched_fraction6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_05_Per15_CysPAT_Phos_enriched_fraction5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_10_Per15_CysPAT_Phos_input_preenrichment.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_07_Per15_CysPAT_Phos_enriched_fraction7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_02_Per15_CysPAT_Phos_enriched_fraction2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_04_Per15_CysPAT_Phos_enriched_fraction4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/Ref_1084_09_Per15_CysPAT_Phos_enriched_fraction9.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/241024_CysPAT_Per15_eclipse.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059503/241024_CysPAT_Per15_eclipse_OxC.pdResult"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Hayley.Sharpe@babraham.ac.uk"],"submitter":["Harvey Johnston"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Cysteine","Hek293t","Phosphoproteomics","Pervanadate","Redox","C6-cpt","C6-cyspat"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD059503"],"tissue":["Permanent Cell Line Cell","Cell Culture"],"sample_protocol":["Plated HEK293T cells, treated with 100uM pervanadate for 0, 5 and 15 minutes, were aspirated of media, then washed 4 times in ice cold phosphate buffered saline. Cells were lysed on ice in 300 µl of chilled ‘SP3 lysis buffer’ (50 mM HEPES pH 8.0, 150 mM NaCl, 1% SDS, 1% Triton X-100, 1% IGEPAL CA-630, 1% Tween 20, 1% sodium deoxycholate, 1 × cOmpleteTM protease inhibitors EDTA-free, PhosSTOP (Roche), 1 mM PMSF) supplemented with either 40 mM NEM (blocking buffer) or 5 mM C6-CPT (labelling buffer), collected and sonicated on ice. For each condition, untreated (UT), 5- and 15-minute pervanadate (P5 and P15) three plates were lysed with blocking (for oxidised Cys samples, OxC) and labelling (for total Cys samples, Tot) buffer in parallel. The initial alkylation reaction was incubated on a thermomixer at 1200 rpm for 20 mins at 25 °C and protected from light. ~300 µg protein was cleaned by SP4 (6) using four volumes of acetonitrile and glass beads and washed 4 times with 500 µl of 80% ethanol. For all samples, cleaned precipitated proteins were resolubilised in 300 µl of labelling buffer (containing 5 mM C6-CPT), in addition to 2% SDS to aid solubilisation, and 5 mM TCEP to reduce oxidised Cys residues, and incubated on a thermomixer at 1200 rpm for 20 mins at 25 °C and protected from light.       Proteins were cleaned with a further round of SP4, as before, but with no further glass beads added, with the resulting pellet digested overnight at 37 °C in 200 µl of 50 mM HEPES pH 8 with 1:100 trypsin and 1:200 Lys-C (enzyme:protein). Peptide concentration was assessed BCA assay (Thermo Fisher Scientific) and adjusted to 1 µg/µl. 200 µg of peptides per sample were labelled with a 2.5:1 ratio of TMT 18-plex:peptides as follows: UT Tot (126C, 127C, 128C), P5 Tot (129C, 130C, 131C), P15 Tot (132C, 133C, 134C), UT OxC (127N, 128N, 129N), P5 OxC (130N, 131N, 132N), and P15 OxC (133N, 134N, 135N) on a thermomixer at 800 rpm for 1 h at 25 °C. Reactions were quenched with 20 µl 5% hydroxylamine for 15 mins and pooled. A 50 µg aliquot was taken for whole proteome analysis and cleaned by C18.       Peptides were adjusted to 80% ACN, 5% TFA, 1M glycolic acid and incubated with vigorous shaking (~1000 rpm) with 24 mg of TitanSphereTM Phos-TiO beads (GL Sciences Inc.) for 20 mins. The beads were aspirated and washed twice with 4 ml of 80% ACN, 5% TFA, 1M glycolic acid, with 2 mL 80% ACN, 1% TFA, then 2 ml 20% ACN, 0.2% TFA and beads dried for 10 min. Phospho- and C6-CPT-peptides were eluted in 300 µl of 1% Ammonium Hydroxide for 10 min with the beads washed in a further 150 µl and sequentially loaded all onto a prepared HpH spin fractionation column (Thermo Fisher Scientific). Peptides were washed and eluted in 10, 12, 14, 16, 18, 20, 24, 28, and 40% ACN in 0.1% TEA. Fractions, and the cleaned input peptides, were dried in a vacuum concentrator and resuspended in 30 µl 2% ACN, 0.1% formic acid.      Peptides were analysed by nanoLC-MS/MS on a Dionex Ultimate 3000 LC, interfaced to an Orbitrap Eclipse mass spectrometer (Thermo Fisher Scientific). Samples were loaded onto a Pepmap C18 trap (20 x 0.1mm) and separated on a Pepmap C18 column (500 x .075mm), with a 3hr gradient of 2-35% acetonitrile (containing 0.1% formic acid) at 300nL/min. The Eclipse was fitted with a FAIMS interface, which was cycled through four compensation voltages (-45V, -55V, -65V, -75V; 2s each) throughout each run. For each compensation voltage the scan cycle consisted of a MS1 scan at 120k resolution and MS2 scans of peptide ions (+2 to +5 charge states) isolated with a 0.7Th window and fragmented by HCD with 35% relative collision energy. MS2 spectra were recorded with resolution set to 30k, with TMT resolution enhancement."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MS raw files were processed with Proteome DiscovererTM 2.5 using Sequest HT (2.0.0.24, x64), Percolator (3.05.0), and IMP-ptmRS (1.0.0.0) searching against UniProt Human Swissprot (UniProtKB v2024-10-02) and a PD contaminant list (2015_5). Default settings were used, allowing 2 missed tryptic cleavages, with N-ethylmaleimide and C6-CPT (C, variable), phospho (S/T/Y, variable) oxidation (M, variable), acetyl, Met-loss, and Met-loss+acetyl (protein N-term, variable), TMTpro (K, peptide N-term, fixed). FTMS spectra were searched with 0.02 Da fragment mass tolerances. Proteome DiscovererTM was used to determine peptide identifications (q < 0.01) and TMT values. All raw intensities were converted to Log Intensities using log2(raw intensity+1). The input samples were used to calculate global correction factors for differences in amounts of starting material in each sample.  The mean log intensity (MLI) for each sample across all peptides was calculated, and then the per sample correction value was defined as the MLI per sample minus the median MLI across all samples.  For CPT all peptides annotated with a CPT modification were retained, peptides containing a mix of CPT and Phosphorylation were removed.  For phosphorylation analysis peptides containing CPT were discarded.  The remaining peptides were classified based on the phosphorylated resides (Ser, Thr or Tyr) which were observed in each peptide.  Peptides containing more than one type of phosphorylated amino acid were removed.  In both analyses, global Log Intensities per sample were corrected by subtracting the correction value calculated from the corresponding input sample.  Peptides which were not observed in all replicates were removed.  Differential abundance was assessed using an ANOVA test on the Corrected Log Intensities, across the Untreated, 5 min and 15 min timepoints.  Raw p-values were adjusted for multiple testing using Benjamini and Hochberg multiple testing correction.  Differences were calculated as the differences in mean Log Intensity between the treated samples and the untreated controls."],"omics_type":["Proteomics"],"labhead":["Hayley Sharpe"],"instrument_platform":[""],"labhead_affiliation":["Hayley Sharpe, Signalling, Babraham Institute, Cambridge, UK"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["harvey.johnston@babraham.ac.uk"],"publication":["41557758 Mulholland KE, Bourguet M, Cheng N, Rahman O, Ezeriņa D, Daly LA, Lai T, Aldaz Casanova S, Featherston T, Creixell P, Eyers CE, Messens J, Eyers PA, Byrne DP, Sharpe HJ. Pervanadate-induced oxidation relieves autoinhibition of the protein tyrosine kinase SRC. Sci Signal. 2026 19(921):eady9437 10.1126/scisignal.ady9437"],"submitter_affiliation":["The Babraham Institute"],"submitter_country":["United Kingdom"],"pubmed_abstract":["Dynamic regulation of protein tyrosine phosphorylation (pTyr) by kinases and phosphatases enables cells to sense and respond to environmental changes. The widely used chemical pervanadate induces the accumulation of pTyr in mammalian cell lines. This effect is primarily attributed to its inhibition of protein tyrosine phosphatases (PTPs), leading to the assertion that PTPs are master gatekeepers of intracellular pTyr homeostasis. Here, we used several approaches to reveal that pervanadate disrupted cellular redox homeostasis and directly activated tyrosine kinases of the SRC family through the oxidation of specific cysteine residues. Mass spectrometry and biophysical approaches showed that pervanadate-induced oxidation of cysteine-188 and cysteine-280 activated SRC by disrupting autoinhibitory intramolecular interactions between the catalytic domain and the SH2/SH3 domains and by impairing SH2 domain binding to phosphopeptides, including the regulatory carboxyl-terminal tail phosphotyrosine-530. Redox-sensitive cysteine residues were essential for SRC to promote the overgrowth of mouse fibroblasts. Our findings call for a reevaluation of pervanadate-based experiments and demonstrate that SRC cysteines control its oncogenic properties."],"pubmed_title":["Pervanadate-induced oxidation relieves autoinhibition of the protein tyrosine kinase SRC."],"pubmed_authors":["Mulholland Katie E KE, Bourguet Maxime M, Cheng Nuo N, Rahman Oisharja O, Ezeriņa Daria D, Daly Leonard A LA, Lai Tiffany T, Aldaz Casanova Silvia S, Featherston Therese T, Creixell Pau P, Eyers Claire E CE, Messens Joris J, Eyers Patrick A PA, Byrne Dominic P DP, Sharpe Hayley J HJ"],"additional_accession":[]},"is_claimable":false,"name":"Combined cysteine oxidation (C6-CPT/CysPAT) proteomics and phosphoproteomics of pervanadate-treated of HEK293T cells","description":"HEK293T cells were treated with pervanadate for 0, 5 or 15 minutes to evaluate the effects on the phosphorylation and cysteine oxidation status across the proteome. Samples were labelled withTMT 18plex and C6-CPT/CysPAT labelling was used to allow the simultaneous enrichment of both the phosphoproteome and total vs. oxidised cysteine proteome.","dates":{"publication":"2026-06-22","submission":"2025-01-07"},"accession":"PXD059503","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT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