PXD062628
PXD062628 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Quantification and site-specific analysis of co-occupied N- and O-glycopeptides |
Description | Protein glycosylation is a complex post-translational modification that is generally classified as N- or O-linked. Site-specific analysis of glycopeptides is accomplished with a variety of fragmentation methods, depending on the type of glycosylation being investigated and the instrumentation available. For instance, collisional dissociation methods are frequently used for N-glycoproteomic analysis with the assumption that one N-sequon exists per tryptic peptide. Alternatively, electron-based methods are indispensable for O-glycosite localization. However, the presence of simultaneously N- and O-glycosylated peptides could suggest the necessity of electron-based fragmentation methods for N-glycoproteomics, which is not commonly performed. Thus, we quantified the prevalence of N- and O-glycopeptides in mucins and other glycoproteins. A much higher frequency of co-occupancy within mucins was detected whereas only a negligible occurrence occurred within non-mucin glycoproteins. This was demonstrated from analyses of recombinant and/or purified proteins, as well as more complex samples. Where co-occupancy occurred, O-glycosites were frequently localized to the Ser/Thr within the N-sequon. Additionally, we found that O-glycans in close proximity to the occupied Asn were predominantly unelaborated core 1 structures, while those further away were more extended. Overall, we demonstrate electron-based methods are required for robust site-specific analysis of mucins, wherein co-occupancy is more prevalent. Conversely, collisional methods are generally sufficient for analyses of other types of glycoproteins. |
HostingRepository | PRIDE |
AnnounceDate | 2025-04-08 |
AnnouncementXML | Submission_2025-04-08_12:44:04.376.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Joann Chongsaritsinsuk |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | complex glycosylation |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2025-04-04 13:15:06 | ID requested | |
⏵ 1 | 2025-04-08 12:44:05 | announced |
Publication List
10.1021/ACS.JPROTEOME.4C00574; |
10.1021/acs.jproteome.4c00574; |
Chongsaritsinsuk J, Rangel-Angarita V, Lucas TM, Mahoney KE, Enny OM, Katemauswa M, Malaker SA, Quantification and Site-Specific Analysis of Co-occupied N- and O-Glycopeptides. J Proteome Res, 23(12):5449-5461(2024) [pubmed] |
Keyword List
submitter keyword: mucin, glycoproteomics, O-glycosylation,glycosylation, N-glycosylation |
Contact List
Stacy Malaker | |
---|---|
contact affiliation | Yale University, Department of Chemistry |
contact email | stacy.malaker@yale.edu |
lab head | |
Joann Chongsaritsinsuk | |
contact affiliation | Yale University |
contact email | joann.chongsaritsinsuk@yale.edu |
dataset submitter |
Full Dataset Link List
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PRIDE project URI |
Repository Record List
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