PXD046990

PXD046990 is an original dataset announced via ProteomeXchange.

Dataset Summary

Title	Mechanism of 60S ribosomal subunit recognition and UFMylation by the UFM1 E3 ligase complex
Description	During co-translational translocation at the endoplasmic reticulum (ER), ribosomes can stall and become covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit RPL26 (uL24). This process, known as UFMylation, is mediated by the UFM1 Ribosome E3 Ligase (UREL) complex, comprised of UFL1, UFBP1, and CDK5RAP3. However, the functional consequences of UFMylation and catalytic mechanisms of UREL are unknown. Here, we present crosslinking-mass spectrometry (XL-MS) data of UREL bound to 60S ribosomes.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:34:23.758.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Antonio Calabrese
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Eclipse

Dataset History

Revision	Datetime	Status	ChangeLog Entry
0	2023-11-15 07:23:24	ID requested
1	2024-03-22 01:38:14	announced
⏵ 2	2024-10-22 06:34:24	announced	2024-10-22: Updated project metadata.

Publication List

10.1038/s41586-024-07093-w;
Makhlouf L, Peter JJ, Magnussen HM, Thakur R, Millrine D, Minshull TC, Harrison G, Varghese J, Lamoliatte F, Foglizzo M, Macartney T, Calabrese AN, Zeqiraj E, Kulathu Y, The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons. Nature, 627(8003):437-444(2024) [pubmed]

10.1038/s41586-024-07093-w;

Makhlouf L, Peter JJ, Magnussen HM, Thakur R, Millrine D, Minshull TC, Harrison G, Varghese J, Lamoliatte F, Foglizzo M, Macartney T, Calabrese AN, Zeqiraj E, Kulathu Y, The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons. Nature, 627(8003):437-444(2024) [pubmed]

Keyword List

submitter keyword: ribosome, XL-MS,UFM

submitter keyword: ribosome, XL-MS,UFM

Contact List

Antonio Calabrese
contact affiliation	Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, United Kingdom
contact email	a.calabrese@leeds.ac.uk
lab head
Antonio Calabrese
contact affiliation	School of Molecular and Cellular Biology, University of Leeds
contact email	a.calabrese@leeds.ac.uk
dataset submitter

Full Dataset Link List

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PRIDE project URI

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/2024/03/PXD046990

PRIDE project URI

Repository Record List

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