PXD031976

PXD031976 is an original dataset announced via ProteomeXchange.

Title	Quantitative chemoproteomic identification of lysine carboxylation in proteins
Description	Carbon dioxide is an abundant biological gas that drives adaptive physiological responses within organisms from all domains. The basic biochemical mechanisms by which proteins serve as sensors of CO2 are, therefore, of great interest. CO2 is a potent electrophilic, and thus one way it can modulate protein biochemistry is by carboxylation of the primary amines group of lysines. However, the resulting cabamates spontaneously decompose, giving off CO2, which makes studying this modification notoriously challenging. Here we describe a chemoproteomic method to stably mimic CO2-carboxylated lysine residues in proteins by reacting them with OCNH. We leverage this method to develop a competition based strategy to quantitatively identify CO2-carboxylatedlysines of proteins and use it to explore the lysine ‘carboxylome’.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:05:13.357.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Dustin King
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Synechocystis sp.; NCBI TaxID: 1143;
ModificationList	carbamoylated residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2022-03-01 10:31:19	ID requested
1	2023-09-09 14:46:30	announced
⏵ 2	2023-11-14 09:05:23	announced	2023-11-14: Updated project metadata.

King DT, Zhu S, Hardie DB, Serrano-Negr, ó, n JE, Madden Z, Kolappan S, Vocadlo DJ, -dependent lysine carboxylation in proteins. Nat Chem Biol, 18(7):782-791(2022) [pubmed]

submitter keyword: CO2, lysine carboxylation, chemoproteomics, homocitrulline

David Vocadlo
contact affiliation	Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6, Canada Department of Chemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6, Canada
contact email	dvocadlo@sfu.ca
lab head
Dustin King
contact affiliation	Simon Fraser University
contact email	dustink@sfu.ca
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/2023/09/PXD031976

PRIDE project URI

• PRIDE
  1. PXD031976
     1. Label: PRIDE project
     2. Name: Quantitative chemoproteomic identification of lysine carboxylation in proteins