PXD071631

PXD071631 is an original dataset announced via ProteomeXchange.

Title	Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1
Description	Active cullin-RING profiling and total proteome mass spectrometry were used to uncover the inverse, cysteine-dependent, releationship between the E3 LRRC58 and its substrate CDO1.
HostingRepository	PRIDE
AnnounceDate	2026-04-29
AnnouncementXML	Submission_2026-04-29_11:46:13.130.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Gisele Andree
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	timsTOF Pro 2

Revision	Datetime	Status	ChangeLog Entry
0	2025-12-05 02:45:33	ID requested
⏵ 1	2026-04-29 11:46:13	announced

10.1038/S41467-026-72524-3;

submitter keyword: E3 ligase, cysteine metabolism

Brenda A. Schulman
contact affiliation	Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
contact email	schulman@biochem.mpg.de
lab head
Gisele Andree
contact affiliation	MPIB
contact email	andree@biochem.mpg.de
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/PXD071631

PRIDE project URI

• PRIDE
  1. PXD071631
     1. Label: PRIDE project
     2. Name: Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1