<<< Full experiment listing


PXD009994 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleAnalysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation
DescriptionLysine 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.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterBrian Weinert
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListacetylated residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02018-06-01 01:48:34ID requested
12019-03-11 20:26:56announced
Publication List
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]
Keyword List
curator keyword: Biological
submitter keyword: acetylation, stoichiometry, HeLa, human, acetylome
Contact List
Brian Tate Weinert
contact affiliationUniversity of Copenhagen The Novo Nordisk Foundation Center for Protein Research Blegdamsvej 3B, 6.1 DK-2200 Copenhagen N Denmark
contact emailbrtw@cpr.ku.dk
lab head
Brian Weinert
contact affiliationProteomics
contact emailbrtw@cpr.ku.dk
dataset submitter
Full Dataset Link List
Dataset FTP location
PRIDE project URI
Repository Record List
[ + ]