PXD011533

PXD011533 is an original dataset announced via ProteomeXchange.

Title	Glycoproteomics with AI-ETD
Description	Protein glycosylation is a highly important, yet a poorly understood protein post-translational modification. Thousands of possible glycan structures and compositions create potential for tremendous site heterogeneity and analytical challenge. A lack of suitable analytical methods for large-scale analyses of intact glycopeptides has ultimately limited our abilities to both address the degree of heterogeneity across the glycoproteome and to understand how it contributes biologically to complex systems. Here we show that N-glycoproteome site-specific microheterogeneity can be captured at a global level via glycopeptide profiling with activated ion electron transfer dissociation (AI-ETD), enabling characterization of nearly 2,100 N-glycosites (> 7,500 unique N-glycopeptides) from mouse brain tissue. Moreover, we have used this unprecedented scale of glycoproteomic data to develop several new visualizations that will prove useful for analyzing intact glycopeptides in future studies. Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein.
HostingRepository	PRIDE
AnnounceDate	2019-04-02
AnnouncementXML	Submission_2019-04-02_07:51:07.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nicholas Riley
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	complex glycosylation; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2018-10-30 09:13:30	ID requested
⏵ 1	2019-04-02 07:51:09	announced

Riley NM, Hebert AS, Westphall MS, Coon JJ, Capturing site-specific heterogeneity with large-scale N-glycoproteome analysis. Nat Commun, 10(1):1311(2019) [pubmed]

submitter keyword: electron transfer dissociation, glycosylation, glycopeptides

Joshua J. Coon
contact affiliation	University of Wisconsin, Departments of Chemistry and Biomolecular Chemistry Morgridge Institute for Research
contact email	jcoon@chem.wisc.edu
lab head
Nicholas Riley
contact affiliation	Stanford University
contact email	riley.nicholasm@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/2019/04/PXD011533

PRIDE project URI

• PRIDE
  1. PXD011533
     1. Label: PRIDE project
     2. Name: Glycoproteomics with AI-ETD