PXD009994-2

PXD009994 is an original dataset announced via ProteomeXchange.

Title	Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
Description	Lysine acetylation is a reversible posttranslational modification that occurs at thousands of sites on human proteins. However, the stoichiometry of acetylation remains poorly characterized, and is important for understanding acetylation-dependent mechanisms of protein regulation. Here we provide accurate, validated measurements of acetylation stoichiometry at 6,829 sites on 2,535 proteins in human cervical cancer (HeLa) cells. Most acetylation occurs at very low stoichiometry (median 0.02%), whereas high stoichiometry acetylation occurs on nuclear proteins involved in gene transcription and on acetyltransferases. Analysis of acetylation copy number shows that histones harbor the majority of acetylated lysine residues in human cells. Class I deacetylases target a greater proportion of high stoichiometry acetylation compared to SIRT1 and HDAC6. The acetyltransferases CBP and p300 catalyze a majority (65%) of high stoichiometry acetylation, yet also target sites with low stoichiometry. This resource dataset provides valuable information for understanding the impact of individual acetylation sites on protein function.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:08:20.193.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Brian Weinert
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-06-01 01:48:34	ID requested
1	2019-03-11 20:26:56	announced
⏵ 2	2024-10-22 04:08:21	announced	2024-10-22: Updated project metadata.

10.1038/s41467-019-09024-0;

Hansen BK, Gupta R, Baldus L, Lyon D, Narita T, Lammers M, Choudhary C, Weinert BT, Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation. Nat Commun, 10(1):1055(2019) [pubmed]

curator keyword: Biological

submitter keyword: acetylation, acetylome, human, HeLa, stoichiometry

Brian Tate Weinert
contact affiliation	University of Copenhagen The Novo Nordisk Foundation Center for Protein Research Blegdamsvej 3B, 6.1 DK-2200 Copenhagen N Denmark
contact email	brtw@cpr.ku.dk
lab head
Brian Weinert
contact affiliation	Proteomics
contact email	brtw@cpr.ku.dk
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/2019/03/PXD009994

PRIDE project URI

• PRIDE
  1. PXD009994
     1. Label: PRIDE project
     2. Name: Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation