PXD002205 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Ubiquitin S65 proteomics: Protein turnover analysis |
Description | Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology. |
HostingRepository | PRIDE |
AnnounceDate | 2015-07-11 |
AnnouncementXML | Submission_2015-07-11_00:31:24.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Danielle Swaney |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | No PTMs are included in the dataset |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2015-05-19 02:19:14 | ID requested | |
1 | 2015-07-07 11:18:09 | announced | |
⏵ 2 | 2015-07-11 00:31:25 | announced | Updated project metadata. |
Publication List
Swaney DL, Rodr, í, guez-Mias RA, Vill, é, n J, Phosphorylation of ubiquitin at Ser65 affects its polymerization, targets, and proteome-wide turnover. EMBO Rep, 16(9):1131-44(2015) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Yeast, ubiquitin, phosphorylation, orbitrap |
Contact List
Judit Villen |
contact affiliation | University of Washington |
contact email | jvillen@uw.edu |
lab head | |
Danielle Swaney |
contact affiliation | UCSF |
contact email | daniswan@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD002205
- Label: PRIDE project
- Name: Ubiquitin S65 proteomics: Protein turnover analysis