⮝ Full datasets listing

PXD013930

PXD013930 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleSite-specific N-glycosylation of HeLa cell glycoproteins
DescriptionHeLa cell line is frequently used in biomedical research, however little is known about N-glycan structures expressed on individual glycoproteins of this complex sample. We characterized site-specific N-glycosylation of HeLa N-glycoproteins using a complex workflow based on high and low energy tandem mass spectrometry experiments and rigorous data evaluation. The analyses revealed high amount of bovine serum contaminants compromising previous results focusing on released glycan analysis. We reliably identified 43 (human) glycoproteins, 69 N-glycosylation sites and 178 glycopeptides following an acetone precipitation based sample enrichment step. HeLa glycoproteins were found to be highly fucosylated and in several cases localization of the fucose (core or antenna) could also be determined based on low energy tandem mass spectra. High-mannose sugars were expressed in high amounts as expected in case of a cancer cell line. Our method enabled the detailed characterization of site-specific N-glycosylation of several glycoproteins expressed in HeLa. Furthermore, we were the first to experimentally prove the existence of 31 glycosylation sites, where previously presence of glycosylation was only predicted based on the existence of the consensus sequon.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_04:56:56.394.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterLilla Turiák
SpeciesList scientific name: Bos taurus (Bovine); NCBI TaxID: 9913; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListdeaminated residue; monohydroxylated residue; complex glycosylation; iodoacetamide derivatized residue
InstrumentmaXis
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-05-20 03:51:45ID requested
12019-10-21 14:25:23announced
22019-10-25 03:54:07announced2019-10-25: Updated publication reference for PubMed record(s): 31616032.
32019-11-15 00:03:06announced2019-10-25: Updated publication reference for PubMed record(s): 31616032.
2019-11-15: Updated publication reference for PubMed record(s): 31616032, 31697861.
42024-10-22 04:57:07announced2024-10-22: Updated project metadata.
Publication List
Turi, á, k L, Sug, á, r S, Á, cs A, T, ó, th G, G, ö, m, ö, ry Á, Telekes A, V, é, key K, Drahos L, Site-specific N-glycosylation of HeLa cell glycoproteins. Sci Rep, 9(1):14822(2019) [pubmed]
Sug, á, r S, Turi, á, k L, V, é, key K, Drahos L, Widespread presence of bovine proteins in human cell lines. J Mass Spectrom, 55(7):e4464(2020) [pubmed]
10.1038/s41598-019-51428-x;
10.1002/jms.4464;
Keyword List
submitter keyword: HeLa, nanoUHPLC-MS/MS, N-glycosylation, site-specific
Contact List
Laszlo Drahos
contact affiliationMS Proteomics Research Group, Institute of Organic Chemistry, Hungarian Academy of Sciences Research Centre for Natural Sciences, Hungary
contact emaildrahos.laszlo@ttk.mta.hu
lab head
Lilla Turiák
contact affiliationRCNS HAS, MS Proteomics Research Group
contact emailliliat7@gmail.com
dataset submitter
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/10/PXD013930
PRIDE project URI
Repository Record List
[ + ]