PXD004995

PXD004995 is an original dataset announced via ProteomeXchange.

Title	Sites of aspirin-mediated lysine acetylation in HeLa cells, part 2
Description	Aspirin, or acetylsalicylic acid is widely used to control pain, inflammation and fever. Important to this function is its ability to irreversibly acetylate cyclooxygenases at active site serines. Aspirin has the potential to acetylate other amino-acid side-chains, leading to speculation that aspirin-mediated lysine acetylation could explain some of its drug actions or side-effects. Using a labeled form of aspirin, aspirin-d3, we identified over 12000 sites of lysine acetylation from cultured human cells. Although aspirin amplifies acetylation signals at thousands of sites, cells tolerate aspirin mediated acetylation very well unless endogenous deacetylases are inhibited. Apart from a limited number of cellular proteins that are substantially acetylated under endogenous conditions, aspirin mediated acetylation leads to a large increase in the acetylation of many proteins even although they remain at very low stoichiometry. This reinforces the idea that a major function of cellular deacetylases is the suppression of non-specific or non-enzymatic protein acetylation.
HostingRepository	PRIDE
AnnounceDate	2017-10-24
AnnouncementXML	Submission_2017-10-24_04:02:48.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Mike Tatham
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-09-19 03:25:28	ID requested
1	2016-12-23 22:09:06	announced
2	2017-06-21 00:31:16	announced	Updated project metadata.
⏵ 3	2017-10-24 04:02:49	announced	Updated project metadata.

Tatham MH, Cole C, Scullion P, Wilkie R, Westwood NJ, Stark LA, Hay RT, A Proteomic Approach to Analyze the Aspirin-mediated Lysine Acetylome. Mol Cell Proteomics, 16(2):310-326(2017) [pubmed]

curator keyword: Biomedical

submitter keyword: Aspirin, lysine acetylation, Hela,

Ronald Thomas Hay
contact affiliation	Centre for Gene Regulation and Expression, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH. UK.
contact email	r.t.hay@dundee.ac.uk
lab head
Mike Tatham
contact affiliation	University of Dundee
contact email	m.tatham@dundee.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/2016/12/PXD004995

PRIDE project URI

• PRIDE
  1. PXD004995
     1. Label: PRIDE project
     2. Name: Sites of aspirin-mediated lysine acetylation in HeLa cells, part 2