PXD004445

PXD004445 is an original dataset announced via ProteomeXchange.

Title	Large scale ubiquitination in doxorubicin treated cells
Description	Protein post-translational modification (PTM) plays a central role in the DNA damage response. In particular protein phosphorylation and ubiquitination have been shown to play a major role in the signalling cascade that coordinates break repair with cell cycle progression. Here we performed large-scale quantitative proteomics to identify changes in protein ubiquitination that are induced by DNA double-strand breaks. In total we quantified >9400 ubiquitin sites, and found that the relative abundance of ~10% of these sites was altered in response to DNA double-strand breaks. Interestingly, we found a large proportion of the ribosomal proteins to be ubiquitinated after damage. These included ribosomal proteins from the 40S as well as the 60S subunit. We subsequently show that DNA damage damage leads to a transient inhibition in ribosome function in protein synthesis. Taken together, these data uncover ribosome ubiquitination as a consequence of activation of the DDR .
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:37:56.243.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Vincentius Andrianto Halim
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	ubiquitination signature dipeptidyl lysine; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2016-06-27 05:30:26	ID requested
1	2018-02-23 04:38:02	announced
⏵ 2	2024-10-22 04:37:57	announced	2024-10-22: Updated project metadata.

Halim VA, Garc, í, a-Santisteban I, Warmerdam DO, van den Broek B, Heck AJR, Mohammed S, Medema RH, Doxorubicin-induced DNA Damage Causes Extensive Ubiquitination of Ribosomal Proteins Associated with a Decrease in Protein Translation. Mol Cell Proteomics, 17(12):2297-2308(2018) [pubmed]

10.1074/mcp.ra118.000652;

curator keyword: Biomedical

submitter keyword: proteomics,DNA damage, ubiquitin, LC-MS/MS

Shabaz Mohammed
contact affiliation	Associate Professor of Proteomics Departments of Chemistry and Biochemistry | University of Oxford
contact email	shabaz.mohammed@chem.ox.ac.uk
lab head
Vincentius Andrianto Halim
contact affiliation	Faculty of Science, Utrecht University
contact email	v_halim@hotmail.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/2018/02/PXD004445

PRIDE project URI

• PRIDE
  1. PXD004445
     1. Label: PRIDE project
     2. Name: Large scale ubiquitination in doxorubicin treated cells