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Large-scale characterization of HeLa cell nuclear phosphoproteins.


ABSTRACT: Determining the site of a regulatory phosphorylation event is often essential for elucidating specific kinase-substrate relationships, providing a handle for understanding essential signaling pathways and ultimately allowing insights into numerous disease pathologies. Despite intense research efforts to elucidate mechanisms of protein phosphorylation regulation, efficient, large-scale identification and characterization of phosphorylation sites remains an unsolved problem. In this report we describe an application of existing technology for the isolation and identification of phosphorylation sites. By using a strategy based on strong cation exchange chromatography, phosphopeptides were enriched from the nuclear fraction of HeLa cell lysate. From 967 proteins, 2,002 phosphorylation sites were determined by tandem MS. This unprecedented large collection of sites permitted a detailed accounting of known and unknown kinase motifs and substrates.

SUBMITTER: Beausoleil SA 

PROVIDER: S-EPMC514446 | biostudies-other | 2004 Aug

REPOSITORIES: biostudies-other

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Large-scale characterization of HeLa cell nuclear phosphoproteins.

Beausoleil Sean A SA   Jedrychowski Mark M   Schwartz Daniel D   Elias Joshua E JE   Villén Judit J   Li Jiaxu J   Cohn Martin A MA   Cantley Lewis C LC   Gygi Steven P SP  

Proceedings of the National Academy of Sciences of the United States of America 20040809 33


Determining the site of a regulatory phosphorylation event is often essential for elucidating specific kinase-substrate relationships, providing a handle for understanding essential signaling pathways and ultimately allowing insights into numerous disease pathologies. Despite intense research efforts to elucidate mechanisms of protein phosphorylation regulation, efficient, large-scale identification and characterization of phosphorylation sites remains an unsolved problem. In this report we desc  ...[more]

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