{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD060554/Appendix.xlsx"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD060554/20221018RJCF_Fehls_Peptide4_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD060554/20221018RJCF_Fehls_Peptide6_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD060554/20221018RJCF_Fehls_Peptide5_1.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["zhengping.yi@wayne.edu"],"submitter":["Zhengping Yi"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Disease Of Metabolism"],"software":["Not available"],"submitter_keywords":["Glycoproteomics","Mouse quadriceps","O-glcnac","Tissue atlas","Skeletal muscle"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD060554"],"tissue":["Skeletal Muscle","Skeletal Muscle Cell"],"sample_protocol":["Mouse muscle tissues were homogenized in RIPA buffer using a Precellys bead homogenizer, for 3x5000 rpm, 5 second bursts. Soluble proteins were isolated by centrifuging the samples for 7000 x g for 10 minutes at 4C, collecting the supernatant, and a second spin at 10,000 x g for 15 min at 4C. Proteins were extracted in RIPA buffer with protease inhibitor cocktail. Muscle protein extracts were subjected to chemoenzymatic O-GlcNAc glycoprotein labeling following the methods describe by the Hsieh-Wilson group.Briefly, the engineered Y289L mutant bovine galactosyltransferase (GalT) enzyme was produced in Escherichia coli strain BL21(DE3) following the reported method30 with just one modification, where bacteria were lysed using a French press device rather than by sonication. Our purified GalT matched the expected size by SDS-PAGE analysis and was sufficiently pure. Positive and negative controls using the known O-GlcNAcylated protein-crystallin confirmed activity of the construct. Muscle protein extracts were incubated with GalT and the azide-labeled uridine diphosphate N-acetylgalactosamine donor sugar to selectively install an azide tag on O-GlcNAc sites. The reported methods were followed exactly, substituting our muscle protein extracts instead of protein extracts from cell culture as described in the former report.30 Following O-GlcNAc chemoenzymatic azide-tagging, the tagged proteins were labeled with biotin-alkyne following the reported method with no changes. Labeled proteins were precipitated from methanol/chloroform/H2O to remove unreacted alkyne reagents. Protein pellets were stored at -80C until proteomic preparation. Following biotin labeling, proteins were resuspended in 500 µL RIPA buffer. To enrich biotinylated proteins, samples containing 400 µg total protein were incubated with streptavidin-coated magnetic beads overnight at 4C. Beads were washed with RIPA buffer, wash buffer (50 mM Tris, pH 7.2, 2% SDS), and twice more with RIPA buffer. The beads were then resuspended in DTT in PBS and were then treated with iodoacetamide. The beads were then washed with mass spectrometry grade water and 50% acetonitrile/50% water, then were resuspended in MS grade 50% acetonitrile/50% water. The samples were digested with Lys-C protease for 16 hours at 37 °C and with Solu- for 1 hour (47°C) then for 4 hours (37°C). The supernatants were quenched with formic acid and the magnetic beads were removed. Samples were dried via vacuum centrifugation and stored at -80°C. Each peptide sample was solubilized in 0.1% TFA, purified using C18 ziptips and subjected to LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Statistics and graphics were performed in GraphPad Prism. Gene ontology (GO) was conducted with CLUE-GO50 in Cytoscape.69 The functional analysis mode was used with “GO: biological processes” with “Evidence: All_Experimental” as ontology terms, with Network Specificity set to “Detailed”. Interactome and protein localization analyses were performed with the StringApp70 using the STRING-db46 dataset in Cytoscape.69. Enrichment and over-representation test were applied to annotate the functional differences between labeled proteomics data in PANTHER.71 Plots were generated in Perseus and PRISM. Databases used in this study include UniprotKB (https://www.uniprot.org), the O-GlcNAc Database (https://www.oglcnac.mcw.edu) and the O-GlcNAcATLAS (https://www.oglcnac.org/atlas). O-GlcNAc overlap with performed by comparing the UniprotIDs in the O-GlcNAc Database and the O-GlcNAcATLAS with the majority UniprotID’s for MS hits."],"omics_type":["Proteomics"],"labhead":["Zhengping Yi"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Pharmaceutical Science, EACPHS,Wayne State University,Detroit, MI, USA"],"species":["Mus Musculus (mouse)"],"publication":["39927985 Jaiswal R, Liu Y, Petriello M, Zhang X, Yi Z, Fehl C. A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice. Glycobiology. 2025 35(3):cwaf005 10.1093/glycob/cwaf005"],"submitter_mail":["zhengping.yi@wayne.edu"],"curator_keywords":["Human proteome project","Biology/disease-driven human proteome project (b/d-hpp)","Skeletal muscle proteome (b/d-hpp)","Glycoproteomics (b/d-hpp)"],"submitter_affiliation":["Wayne State University"],"submitter_country":["United States"],"pubmed_abstract":["A key nutrient sensing process in all animal tissues is the dynamic attachment of O-linked N-acetylglucosamine (O-GlcNAc). Determining the targets and roles of O-GlcNAc glycoproteins has the potential to reveal insights into healthy and diseased metabolic states. In cell studies, thousands of proteins are known to be O-GlcNAcylated, but reference datasets for most tissue types in animals are lacking. Here, we apply a chemoenzymatic labeling study to compile a high coverage dataset of quadriceps skeletal muscle O-GlcNAc glycoproteins from mice. Our dataset contains over 550 proteins, and > 80% of the dataset matched known O-GlcNAc proteins. This dataset was further annotated via bioinformatics, revealing the distribution, protein interactions, and gene ontology (GO) functions of these skeletal muscle proteins. We compared these quadriceps glycoproteins with a high-coverage O-GlcNAc enrichment profile from mouse hearts and describe the key overlap and differences between these tissue types. Quadriceps muscles can be used for biopsies, so we envision this dataset to have potential biomedical relevance in detecting aberrant glycoproteins in metabolic diseases and physiological studies. This new knowledge adds to the growing collection of tissues with high-coverage O-GlcNAc profiles, which we anticipate will further the systems biology of O-GlcNAc mechanisms, functions, and roles in disease."],"pubmed_title":["A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice."],"pubmed_authors":["Jaiswal Ruchi R, Liu Yimin Y, Petriello Michael M, Zhang Xiangmin X, Yi Zhengping Z, Fehl Charlie C"],"additional_accession":[]},"is_claimable":false,"name":"A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice","description":"A key nutrient sensing process in all animal tissues is the dynamic attachment of O-linked N-acetylglucosamine (O-GlcNAc). Determining the targets and roles of O-GlcNAc glycoproteins has the potential to reveal insights into healthy and diseased metabolic states. In cell studies, thousands of proteins are known to be O-GlcNAcylated, but reference datasets for most tissue types in animals are lacking. Here, we apply a chemoenzymatic labeling study to compile a high coverage dataset of quadriceps skeletal muscle O-GlcNAc glycoproteins from mice. Our dataset contains over 550 proteins, and >80% of the dataset matched known O-GlcNAc proteins. This dataset was further annotated via bioinformatics, revealing the distribution, protein interactions, and gene ontology (GO) functions of these skeletal muscle proteins. We compared these quadriceps glycoproteins with a high-coverage O-GlcNAc enrichment profile from mouse hearts and describe the key overlap and differences between these tissue types. Quadriceps muscles can be used for biopsies, so we envision this dataset to have potential biomedical relevance in detecting aberrant glycoproteins in metabolic diseases and physiological studies. This new knowledge adds to the growing collection of tissues with high-coverage O-GlcNAc profiles, which we anticipate will further the systems biology of O-GlcNAc mechanisms, functions, and roles in disease.","dates":{"publication":"2026-07-21","submission":"2025-02-06"},"accession":"PXD060554","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:112509","NEWT:475174","NEWT:111205","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","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: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:160621","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","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: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: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:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","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: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:906914","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:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","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: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:595495","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEW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