PXD009994 is an
original dataset announced via ProteomeXchange.
Dataset Summary
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 | 2019-03-12 |
AnnouncementXML | Submission_2019-03-11_20:26:54.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 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-06-01 01:48:34 | ID requested | |
⏵ 1 | 2019-03-11 20:26:56 | announced | |
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 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 | |
Full Dataset Link List
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 |
Repository Record List
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[ - ]
- PRIDE
- PXD009994
- Label: PRIDE project
- Name: Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation