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PXD002277

PXD002277 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleLysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation
DescriptionRecent 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.
HostingRepositoryPRIDE
AnnounceDate2015-06-02
AnnouncementXMLSubmission_2015-06-02_03:01:03.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterBrian 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;
ModificationListacetylated residue; N6-succinyl-L-lysine
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02015-06-01 02:32:57ID requested
12015-06-02 03:01:05announced
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 affiliationThe NNF Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark
contact emailchuna.choudhary@cpr.ku.dk
lab head
Brian Weinert
contact affiliationProteomics
contact emailbrtw@cpr.ku.dk
dataset submitter
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