Proteomics

Dataset Information

0

Hs_Hela_Tyr_Mitosis


ABSTRACT: HeLa S3 cells, Tyr phosphorylation, double thymidine block and nocodazole arrest

REANALYSIS of: PXD000612

INSTRUMENT(S): QExactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Others

SUBMITTER: Mario Oroshi 

PROVIDER: PAe005270 | PeptideAtlas | 2014-12-31

REPOSITORIES: PeptideAtlas

Dataset's files

Source:
Action DRS
PAe005270_10293_tandem.params Other
PAe005270_README Other
PAe005270_Search_Results_10293_201512312008.properties Other
PAe005270_Search_Results_10293_201512312008.tar.gz Other
PAe005270_mzXML_201512312007.properties Other
Items per page:
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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   Wiśniewski 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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