PXD013930 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Site-specific N-glycosylation of HeLa cell glycoproteins |
Description | HeLa 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. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:56:56.394.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Lilla Turiák |
SpeciesList | scientific name: Bos taurus (Bovine); NCBI TaxID: 9913; scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | deaminated residue; monohydroxylated residue; complex glycosylation; iodoacetamide derivatized residue |
Instrument | maXis |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-05-20 03:51:45 | ID requested | |
1 | 2019-10-21 14:25:23 | announced | |
2 | 2019-10-25 03:54:07 | announced | 2019-10-25: Updated publication reference for PubMed record(s): 31616032. |
3 | 2019-11-15 00:03:06 | announced | 2019-10-25: Updated publication reference for PubMed record(s): 31616032.
2019-11-15: Updated publication reference for PubMed record(s): 31616032, 31697861. |
⏵ 4 | 2024-10-22 04:57:07 | announced | 2024-10-22: 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 affiliation | MS Proteomics Research Group, Institute of Organic Chemistry, Hungarian Academy of Sciences Research Centre for Natural Sciences, Hungary |
contact email | drahos.laszlo@ttk.mta.hu |
lab head | |
Lilla Turiák |
contact affiliation | RCNS HAS, MS Proteomics Research Group |
contact email | liliat7@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD013930
- Label: PRIDE project
- Name: Site-specific N-glycosylation of HeLa cell glycoproteins