PXD013930

PXD013930 is an original dataset announced via ProteomeXchange.

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

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.

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;

submitter keyword: HeLa, nanoUHPLC-MS/MS, N-glycosylation, site-specific

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

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

• PRIDE
  1. PXD013930
     1. Label: PRIDE project
     2. Name: Site-specific N-glycosylation of HeLa cell glycoproteins