{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/20240523_111741_pST_TMG_OSMI_DMSO_Report_protein.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/20240523_111741_pST_TMG_OSMI_DMSO_Report_PTM.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/20240523_111741_pST_TMG_OSMI_DMSO_Report_normal.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/20240523_111741_pST_TMG_OSMI_DMSO_Report_peptide.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_Sil_pST_TiO2_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_OSMI_DIA2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_TMG_DIA1new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_TMG_DIA2new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_TMG_DIA2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_TMG_DIA3new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_OSMI_DIA3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_DMSO_DIA2new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_TMG_pST_TiO2_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_DMSO_DIA3new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_Sil_pST_TiO2_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_TMG_DIA3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_DMSO_DIA1new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_DMSO_pST_TiO2_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_DMSO_DIA1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_DMSO_DIA2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_DMSO_pST_TiO2_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_TMG_pST_TiO2_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_DMSO_DIA3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_TMG_pST_TiO2_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_OSMI_DIA1new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_Sil_pST_TiO2_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_OSMI_DIA3new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Panc1_pST_TiO2_OSMI_DIA2new.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_OSMI_DIA1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/Proteome_TMG_DIA1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070284/panc1_DMSO_pST_TiO2_01.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["Junfeng.Ma@georgetown.edu"],"submitter":["Ci Wu"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Carcinoma"],"software":[""],"submitter_keywords":["Phosphorylation crosstalk o-glcnac"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070284"],"tissue":["Permanent Cell Line Cell"],"sample_protocol":["Peptides were analyzed with a nanoAcquity UPLC system (Waters) coupled with Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher) in either data dependent acquisition (DDA) mode or data independent acquisition (DIA) mode.27,28 In brief, samples were resuspended in 0.1% FA solution and loaded onto a C18 Trap column (Waters Acquity UPLC M-Class Trap, Symmetry C18, 100 Å, 5 μm, 180 μm × 20 mm) at 10 µL/min for 4 min. Peptides were then separated with an analytical column (Waters Acquity UPLC M-Class, peptide BEH C18 column, 300 Å, 1.7 μm, 75 μm × 250 mm) which was temperature controlled at 45°C. The flow rate was set as 400 nL/min. A 150-min gradient of buffer A (2% ACN, 0.1% formic acid) and buffer B (0.1% formic acid in ACN) was used for separation: 1% buffer B at 0 min, 5% buffer B at 1 min, 22% buffer B at 105 min, 36% buffer B at 125 min, 50% buffer B at 130 min, 90% buffer B at 135 min, 90% buffer B at 145 min, 1% buffer B at 145.1 min, and 1% buffer B at 150 min."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["DDA raw files were processed in Proteome Discoverer (Thermo Fisher Scientific, version 2.4) with the Sequest HT database search engine. The SwissProt database with taxonomy as Homo sapiens (TaxID 9606) was downloaded from UniProt (Released on July 5, 2017, with 42253 protein sequences). The database searching parameters were set as below: full tryptic digestion and allowed up to two missed cleavages, the precursor mass tolerance was set at 10 ppm, whereas the fragment-mass tolerance was set at 0.02 Da. Carbamidomethylation of cysteines (+57.0215 Da) was set as a fixed modification, and variable modifications of methionine oxidation (+15.9949 Da) and acetyl (N-terminus, +42.011 Da) were allowed. The false-discovery rate (FDR) was determined by using a target-decoy search strategy. The decoy-sequence database contains each sequence in reverse orientations, enabling FDR estimation. On the peptide level, the corresponding FDR was less than 1%."],"omics_type":["Proteomics"],"labhead":["Junfeng Ma"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Georgetown University"],"species":["Homo Sapiens (human)"],"publication":["42326659 Wu C, Hou C, Wang X, Peng Y, Lin Y, Byers SW, Pei H, Ma J. Deciphering O‑GlcNAc-Dependent Signaling Via Integrated Proteomics and Phosphoproteomics. ACS Omega. 2026 11(23):34373-34384 10.1021/acsomega.6c02310"],"submitter_mail":["wuci1111@126.com"],"submitter_affiliation":["Research specialist"],"submitter_country":["China"],"pubmed_abstract":["Post-translational modifications (PTMs) on proteins play crucial roles in various biological processes. Two highly dynamic modifications, phosphorylation and O-linked N-acetylglucosamine modification (O-GlcNAcylation), are essential for cellular physiology and pathology. Emerging evidence suggests intimate crosstalk between phosphorylation and O-GlcNAcylation on multiple proteins. However, the precise nature of their crosstalk remains largely unknown. In this study, we explored the crosstalk between phosphorylation and O-GlcNAcylation using the pancreatic ductal cell line PANC-1 as a model. Proteome and phosphoproteome changes were measured for cells treated with OSMI-1, a specific inhibitor of O-GlcNAc transferase, and Thiamet G, a specific inhibitor of O-GlcNAcase. Among the 8938 phosphorylation sites quantified, 2289 phosphosites on 1225 proteins and 2201 phosphosites on 1199 proteins were significantly altered by OSMI-1 and TMG treatment, respectively, demonstrating extensive crosstalk between O-GlcNAcylation and phosphorylation. Further analysis revealed widespread phosphorylation changes of the kinome and phosphatome, even after a short-term perturbation with inhibitors to O-GlcNAc cycling enzymes. Moreover, phosphoproteomic profiling, kinase inhibition experiments, and in vitro kinase assays identified that phosphorylation of OGA itself at S364 is specifically mediated by casein kinase 2 α (CK2α). These results uncover glycosylation-dependent cellular signaling through the potentially multilayer crosstalk between phosphorylation and O-GlcNAcylation."],"pubmed_title":["Deciphering O‑GlcNAc-Dependent Signaling Via Integrated Proteomics and Phosphoproteomics."],"pubmed_authors":["Wu Ci C, Hou Chunyan C, Wang Xinyue X, Peng Yihan Y, Lin Yao Y, Byers Stephen W SW, Pei Huadong H, Ma Junfeng J"],"additional_accession":[]},"is_claimable":false,"name":"Dissecting the Molecular Crosstalk between O-GlcNAcylation and Phosphorylation via Quantitative Proteomics and Phosphoproteomics","description":"In this study, we explored the cross-talk between phosphorylation and O-GlcNAcylation using the pancreatic ductal cell line PANC-1 as a model. Proteome and phosphoproteome changes were measured for cells treated with OSMI-1, a specific inhibitor to O-GlcNAc transferase (OGT)  and Thiamet G, a specific inhibitor to O-GlcNAcase (OGA). Among the 8938 phosphorylation sites quantified, 1399 phosphosites on 870 proteins and 1480 phosphosites on 896 proteins were significantly altered by OSMI-1 and TMG treatment, respectively, demonstrating extensive cross-talk between O-GlcNAcylation and phosphorylation. In-depth analysis revealed widespread phosphorylation changes of the kinome and phosphatome, even after a short-term perturbation with inhibitors to O-GlcNAc cycling enzymes. Notably, we identified that phosphorylation of OGA at S364 is specifically mediated by casein kinase 2 alpha (CK2α), which was supported by phosphoproteomic profiling, kinase inhibition experiments, and in vitro kinase assays. These results uncover a regulatory mechanism underlying glycosylation-dependent cellular signaling through the interplay of phosphorylation and O-GlcNAcylation.","dates":{"publication":"2026-06-29","submission":"2025-11-04"},"accession":"PXD070284","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:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:112509","NEWT:475174","NEWT:111205","NEWT:1599","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","NEWT:1748418","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:381198","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:1562698","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:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","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:200795","NEWT:37919","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","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:3715","NEWT:1538","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:9006","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:2709072","NEWT:2499525","NEWT:2853422","NEWT:1122984","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:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","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:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","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:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:10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