PXD015216 is an
original dataset announced via ProteomeXchange.
Dataset Summary
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 |
Dataset History
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. |
Publication List
10.1074/jbc.ra119.010315; |
Mader J, Huber J, Bonn F, D, รถ, 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] |
Keyword List
submitter keyword: OTU7B, Deubiquitinases,Hydroxylation, Cezanne |
Contact List
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 | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD015216
- Label: PRIDE project
- Name: Asparagine hydroxylation of the UBA domain in Cezanne (OTUD7B)