PXD000612 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling |
Description | Regulatory protein phosphorylation controls nearly every normal and pathophysiological signaling system in eukaryotic cells. Despite great advances in mass spectrometry based-proteomics, the total number, localization and site-specific stoichiometry of this post-translational modification (PTM) are unknown. Here we develop stringent experimental and computational workflow, capable of mapping more than 50,000 distinct phosphorylated peptides in a single human cancer cell line. Label-free quantitation determined very high stoichiometries in mitosis or growth factor signaling and more than three-quarters of cellular proteins were detected as phosphoproteins. The proportion of phospho-Tyr drastically decreases as coverage of the phosphoproteome increases, whereas Ser/Thr sites only saturate for technical reasons. Tyrosine phosphorylation is maintained at especially low stoichiometric levels in the absence of specific signaling events. Unexpectedly, it is statistically enriched on higher abundance proteins and this correlates with the substrate Km values of tyrosine kinases. Our data suggests that P-Tyr should be considered a functionally separate PTM of eukaryotic proteomes. |
HostingRepository | PRIDE |
AnnounceDate | 2014-08-06 |
AnnouncementXML | Submission_2014-08-06_11:22:01.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Mario Oroshi |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | phosphorylated residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2013-12-02 02:12:12 | ID requested | |
⏵ 1 | 2014-08-06 11:22:01 | announced | |
2 | 2014-08-07 00:30:31 | announced | Updated project metadata. |
3 | 2014-09-04 03:48:18 | announced | Updated project metadata. |
4 | 2014-10-23 02:50:05 | announced | Updated project metadata. |
5 | 2024-10-22 04:21:23 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: HeLa, Ultradeep phosphoproteome, Mitosis, EGF |
Contact List
Matthias Mann |
contact affiliation | Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry |
contact email | mmann@biochem.mpg.de |
lab head | |
Mario Oroshi |
contact affiliation | Proteomics |
contact email | oroshi@biochem.mpg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD000612
- Label: PRIDE project
- Name: Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling