PXD021286-1

PXD021286 is an original dataset announced via ProteomeXchange.

Title	Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler
Description	Virtually all aspects of cell biology are regulated by a ubiquitin code where distinct ubiquitin chain architectures guide the binding events and itineraries of modified substrates. Various combinations of E2 and E3 enzymes accomplish chain formation by forging isopeptide bonds between the C-terminus of their transiently-linked donor ubiquitin and a specific nucleophilic amino acid on the acceptor ubiquitin, yet it is unknown whether the fundamental feature of most acceptors - the lysine side-chain - affects catalysis. Here, use of synthetic ubiquitins with non-natural acceptor site replacements reveals that the aliphatic side-chain specifying reactive amine geometry is a determinant of the ubiquitin code, through unanticipated and complex reliance of many distinct ubiquitin carrying enzymes on a canonical acceptor lysine.
HostingRepository	PRIDE
AnnounceDate	2020-09-09
AnnouncementXML	Submission_2020-09-08_23:09:13.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Mario Oroshi
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	ubiquitinylated lysine
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2020-09-03 01:40:26	ID requested
⏵ 1	2020-09-08 23:09:13	announced
2	2024-10-22 05:11:59	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: ubiquitin, proteomics

Matthias Mann
contact affiliation	Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried
contact email	mmann@biochem.mpg.de
lab head
Mario Oroshi
contact affiliation	Proteomics
contact email	oroshi@biochem.mpg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD021286
     1. Label: PRIDE project
     2. Name: Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler