PXD002687

PXD002687 is an original dataset announced via ProteomeXchange.

Title	Co-translational and Post-translational protein myristoylation in HeLa cells
Description	Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. In E. Thinon, R. A. Serwa, et al., Nature Communications 2014, doi:10.1038/ncomms5919, we report the global N-myristoylated proteome in human cells determined using quantitative chemical proteomics combined with potent and specific human N-myristoyltransferase (NMT) inhibition. Global quantification of N-myristoylation during normal growth or apoptosis allowed the identification of >100 N-myristoylated proteins, >95% of which are identified for the first time at endogenous levels. Furthermore, quantitative dose response for inhibition of N-myristoylation is determined for >70 substrates simultaneously across the proteome. Small-molecule inhibition through a conserved substrate-binding pocket is also demonstrated by solving the crystal structures of inhibitor-bound NMT1 and NMT2. The presented data substantially expand the known repertoire of co- and post-translational N-myristoylation in addition to validating tools for the pharmacological inhibition of NMT in living cells.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_03:59:09.129.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Remigiusz Serwa
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	myristoylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2015-08-10 01:53:31	ID requested
1	2018-07-31 03:44:15	announced
⏵ 2	2024-10-22 03:59:13	announced	2024-10-22: Updated project metadata.

Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW, Global profiling of co- and post-translationally N-myristoylated proteomes in human cells. Nat Commun, 5():4919(2014) [pubmed]

10.1038/ncomms5919;

curator keyword: Biomedical

submitter keyword: Co-translational modification, Post-translational modification, Apoptosis,Protein myristoylation

Edward W. Tate
contact affiliation	Department of Chemistry, Imperial College London
contact email	e.tate@imperial.ac.uk
lab head
Remigiusz Serwa
contact affiliation	Imperial College London
contact email	r.serwa@imperial.ac.uk
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/2018/07/PXD002687

PRIDE project URI

• PRIDE
  1. PXD002687
     1. Label: PRIDE project
     2. Name: Co-translational and Post-translational protein myristoylation in HeLa cells