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PXD034098-1

PXD034098 is an original dataset announced via ProteomeXchange.

Dataset Summary
Title  Cyclin A and Cks1 promote kinase consensus switching to non-proline directed CDK1 phosphorylation
DescriptionOrdered protein phosphorylation by CDKs is a key mechanism for regulating the cell cycle. How temporal order is enforced in mammalian cells remains unclear. Using a fixed cell kinase assay and phosphoproteomics, we studied how CDK1 activity and non-catalytic CDK1 subunits contribute to the choice of substrate and phosphorylation site. Increases in CDK1 activity alters substrate choice, with intermediate and low sensitivity CDK1 substrates enriched in DNA replication and mitotic functions, respectively. This activity dependence was shared between Cyclin A- and Cyclin B-CDK1. Cks1 has a proteome-wide role as an enhancer of multisite CDK1 phosphorylation. Contrary to the model of CDK1 as an exclusively proline-directed kinase, we show that Cyclin A and Cks1 promote non-proline directed phosphorylation, preferably on sites with a +3 lysine residue. Indeed, 70% of cell cycle regulated phosphorylations, where the kinase carrying out this modification has not been identified, are non-proline directed CDK1 sites.
HostingRepositoryPRIDE
AnnounceDate2023-02-17
AnnouncementXMLSubmission_2023-02-17_05:39:42.908.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterTonyLy
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListphosphorylated residue
InstrumentOrbitrap Fusion Lumos; Orbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-05-25 03:10:31ID requested
12023-02-17 05:39:43announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: cell cycle, cdk1, kinase, phosphoproteomics
Contact List
TonyLy
contact affiliationCentre for Gene Regulation and Expression University of Dundee
contact emailtly@dundee.ac.uk
lab head
TonyLy
contact affiliationUniversity of Dundee
contact emailtly@dundee.ac.uk
dataset submitter
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