PXD002277 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation |
Description | Recent studies have shown that lysines can be posttranslationally modified by various types of acylations. However, except for acetylation, very little is known about their scope and cellular distribution. We mapped thousands of succinylation sites in bacteria (E. coli), yeast (S. cerevisiae), human (HeLa) cells, and mouse liver tissue, demonstrating widespread succinylation in diverse organisms. A majority of succinylation sites in bacteria, yeast, and mouse liver were acetylated at the same position. Quantitative analysis of succinylation in yeast showed that succinylation was globally altered by growth conditions and mutations that affected succinyl-coenzyme A (succinyl-CoA) metabolism in the tricarboxylic acid cycle, indicating that succinylation levels are globally affected by succinyl-CoA concentration. We preferentially detected succinylation on abundant proteins, suggesting that succinylation occurs at a low level and that many succinylation sites remain unidentified. These data provide a systems-wide view of succinylation and its dynamic regulation and show its extensive overlap with acetylation. |
HostingRepository | PRIDE |
AnnounceDate | 2015-06-02 |
AnnouncementXML | Submission_2015-06-02_03:01:03.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Brian Weinert |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Homo sapiens (Human); NCBI TaxID: 9606; scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | acetylated residue; N6-succinyl-L-lysine |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2015-06-01 02:32:57 | ID requested | |
⏵ 1 | 2015-06-02 03:01:05 | announced | |
Publication List
Weinert BT, Sch, รถ, lz C, Wagner SA, Iesmantavicius V, Su D, Daniel JA, Choudhary C, Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep, 4(4):842-51(2013) [pubmed] |
Keyword List
ProteomeXchange project tag: PRIME-XS Project |
curator keyword: Biological |
submitter keyword: Succinylation, Acetylation, bacteria, yeast, human, liver, mouse |
Contact List
Brian Weinert, Chunaram Choudhary |
contact affiliation | The NNF Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark |
contact email | chuna.choudhary@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
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD002277
- Label: PRIDE project
- Name: Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation