Proteomics

Dataset Information

0

Hs_Hela_Tyr_Pervanadate


ABSTRACT: HeLa S3 cells, Tyr phosphorylation, thymidine block and nocodazole arrest, treated with pervanadate

REANALYSIS of: PXD000612

INSTRUMENT(S): QExactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Others

SUBMITTER: Mario Oroshi 

PROVIDER: PAe005300 | PeptideAtlas | 2014-12-31

REPOSITORIES: PeptideAtlas

Dataset's files

Source:
Action DRS
PAe005300_10347_tandem.params Other
PAe005300_README Other
PAe005300_Search_Results_10347_201512312023.properties Other
PAe005300_Search_Results_10347_201512312023.tar.gz Other
PAe005300_mzXML_201512312008.properties Other
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Publications

Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling.

Sharma Kirti K   D'Souza Rochelle C J RC   Tyanova Stefka S   Schaab Christoph C   WiÅ›niewski Jacek R JR   Cox Jürgen J   Mann Matthias M  

Cell reports 20140821 5


Regulatory protein phosphorylation controls normal and pathophysiological signaling in eukaryotic cells. Despite great advances in mass-spectrometry-based proteomics, the extent, localization, and site-specific stoichiometry of this posttranslational modification (PTM) are unknown. Here, we develop a stringent experimental and computational workflow, capable of mapping more than 50,000 distinct phosphorylated peptides in a single human cancer cell line. We detected more than three-quarters of ce  ...[more]

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