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PXD026730-1

PXD026730 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleGlobal profiling of phosphorylation-dependent changes in cysteine reactivity
DescriptionProteomics has revealed that the ~20,000 human genes engender a far greater number of proteins, or proteoforms, that are diversified in large part by post-translational modifications (PTMs). How such PTMs affect protein structure and function is an active area of research but remains technically challenging to assess on a proteome-wide scale. Here, we describe a chemical proteomic method to quantitatively relate serine/threonine phosphorylation to changes in the reactivity of cysteine residues, a parameter that can affect the potential for cysteines to be post-translationally modified or engaged by covalent drugs. Leveraging the extensive high-stoichiometry phosphorylation occurring in mitotic cells, we discover numerous cysteines that exhibit phosphorylation-dependent changes in reactivity on diverse proteins enriched in cell cycle regulatory pathways. The discovery of bidirectional changes in cysteine reactivity often occurring in proximity to serine/threonine phosphorylation events points to the broad impact of phosphorylation on the chemical reactivity of proteins and the future potential to create small-molecule probes that differentially target PTM-modified proteoforms.
HostingRepositoryPRIDE
AnnounceDate2022-03-03
AnnouncementXMLSubmission_2022-03-03_03:42:07.307.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterEsther Kemper
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListTMT6plex-126 reporter+balance reagent acylated residue; phosphorylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Eclipse; Orbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-06-15 15:43:04ID requested
12022-03-03 03:42:07announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: activity-based protein profiling, chemical proteomics, TMT-ABPP, phosphorylation, cysteine, mitosis
Contact List
Benjamin F. Cravatt
contact affiliationDepartment of Chemistry, Scripps Research Institute, La Jolla
contact emailcravatt@scripps.edu
lab head
Esther Kemper
contact affiliationScripps Research Institute, Cravatt lab
contact emailekemper@scripps.edu
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
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