PXD015216

PXD015216 is an original dataset announced via ProteomeXchange.

Title	Asparagine hydroxylation of the UBA domain in Cezanne (OTUD7B)
Description	by DUBs need to be tightly controlled. Here, we identify asparagine hydroxylation as a novel posttranslational modification involved in the regulation of Cezanne (OTUD7B), a DUB that controls key cellular functions and signaling pathways. We demonstrate that Cezanne is a substrate for FIH1- and oxygen-dependent asparagine hydroxylation. FIH1 modifies Asn35 within the uncharacterized N-terminal ubiquitin-associated (UBA)-like domain of Cezanne (UBACez), which lacks conserved UBA domain properties. We show for the first time that UBACez binds Lys11-, Lys48-, Lys63- and Met1-linked ubiquitin chains in vitro, and thereby establish UBACez as a functional ubiquitin-binding domain. We reveal that interaction of UBACez with ubiquitin is mediated via a non-canonical surface, and that hydroxylation of Asn35 inhibits ubiquitin binding. Recently, it has been suggested that recruitment of Cezanne to specific target proteins depends on UBACez. Our data show that UBACez can indeed fulfil this role as regulatory domain by binding differently linked ubiquitin chains and that this interaction with ubiquitin, and thus modified substrates, can be modulated by asparagine hydroxylation.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:57:40.836.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Florian Bonn
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	hydroxylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-08-29 05:37:17	ID requested
1	2020-01-24 00:25:47	announced
⏵ 2	2024-10-22 04:57:48	announced	2024-10-22: Updated project metadata.

10.1074/jbc.ra119.010315;

Mader J, Huber J, Bonn F, D, ö, tsch V, Rogov VV, Bremm A, Oxygen-dependent asparagine hydroxylation of the ubiquitin-associated (UBA) domain in Cezanne regulates ubiquitin binding. J Biol Chem, 295(8):2160-2174(2020) [pubmed]

submitter keyword: OTU7B, Deubiquitinases,Hydroxylation, Cezanne

Anja Bremm
contact affiliation	Institute of Biochemistry II, University Hospital, Goethe University, Frankfurt, Germany
contact email	bremm@em.uni-frankfurt.de
lab head
Florian Bonn
contact affiliation	University of Frankfurt
contact email	flobonn@gmail.com
dataset submitter

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/2020/01/PXD015216

PRIDE project URI

• PRIDE
  1. PXD015216
     1. Label: PRIDE project
     2. Name: Asparagine hydroxylation of the UBA domain in Cezanne (OTUD7B)