PXD026730-1

PXD026730 is an original dataset announced via ProteomeXchange.

Title	Global profiling of phosphorylation-dependent changes in cysteine reactivity
Description	Proteomics 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.
HostingRepository	PRIDE
AnnounceDate	2022-03-03
AnnouncementXML	Submission_2022-03-03_03:42:07.307.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Esther Kemper
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; phosphorylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Eclipse; Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-06-15 15:43:04	ID requested
⏵ 1	2022-03-03 03:42:07	announced

Dataset with its publication pending

submitter keyword: activity-based protein profiling, chemical proteomics, TMT-ABPP, phosphorylation, cysteine, mitosis

Benjamin F. Cravatt
contact affiliation	Department of Chemistry, Scripps Research Institute, La Jolla
contact email	cravatt@scripps.edu
lab head
Esther Kemper
contact affiliation	Scripps Research Institute, Cravatt lab
contact email	ekemper@scripps.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/03/PXD026730

PRIDE project URI

• PRIDE
  1. PXD026730
     1. Label: PRIDE project
     2. Name: Global profiling of phosphorylation-dependent changes in cysteine reactivity