PXD035902

PXD035902 is an original dataset announced via ProteomeXchange.

Title	Functional analysis of O-GlcNAcylation by networking of OGT interactors and substrates
Description	The post-translational modification (PTM) of proteins by O-linked β-N-acetyl-D-glucosamine (O-GlcNAcylation) is widely found across the proteome and regulates diverse cellular processes, from transcription and translation to signal transduction and metabolism. However, most functional studies to date have focused on individual modifications, overlooking other simultaneous O-GlcNAcylation events that work together to coordinate cellular activities. Here we describe networking of O-GlcNAc transferase interactors and substrates (NOTISE), a systems-level approach that monitors O-GlcNAcylation rapidly and comprehensively across the proteome to reveal important functional and regulatory relationships. The NOTISE method integrates affinity purification–mass spectrometry and site-specific chemoproteomic technologies with network generation to connect putative upstream regulators and downstream targets of O-GlcNAcylation. The resulting data-rich networks identify critical conserved activities of O-GlcNAcylation and tissue-specific functions. This holistic and unbiased approach provides a broadly applicable framework to catalyze investigations into the functional roles of coordinated, multisubstrate PTMs in specific cellular and physiological contexts.
HostingRepository	PRIDE
AnnounceDate	2026-04-03
AnnouncementXML	Submission_2026-04-03_10:42:52.684.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	John Thompson
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606; scientific name: Mus musculus (Mouse); NCBI TaxID: NEWT:10090;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; O-(N-acetylamino)glucosyl-L-threonine; O-(N-acetylamino)glucosyl-L-serine; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF; Orbitrap Fusion; LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2022-08-08 10:45:52	ID requested
⏵ 1	2026-04-03 10:42:53	announced

10.1038/S41589-025-02108-7;

submitter keyword: None

Linda Hsieh-Wilson
contact affiliation	Milton and Rosalind Chang Professor of Chemistry, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA
contact email	lhw@caltech.edu
lab head
John Thompson
contact affiliation	Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA
contact email	jthompso@caltech.edu
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/2026/04/PXD035902

PRIDE project URI

• PRIDE
  1. PXD035902
     1. Label: PRIDE project
     2. Name: Functional analysis of O-GlcNAcylation by networking of OGT interactors and substrates