PXD009731 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | O-GlcNAc pattern of sOGT regulates its substrate selectivity and function |
Description | O-GlcNAcylation occurs on thousands of proteins involved in various cellular events. O-GlcNAc transferase (OGT), one of the enzymes responsible for protein O-GlcNAcylation, is known to be auto-O-GlcNAcylated at multiple sites. However, the role of O-GlcNAcylation on OGT is still unknown. Here, we report the role of O-GlcNAcylation on short form OGT (sOGT). By LC-ETD-MS analysis and western blot, we show that sOGT was mainly O-GlcNAcylated in the tetratricopeptide repeat (TPR) motifs with T12 and S56 being two “key” sites. T12 was a predominant O-GlcNAcylation site and the absence of S56 O-GlcNAcylation enhanced sOGT O-GlcNAcylation level. We found that O-GlcNAcylation of sOGT did not affect the enzyme activity but increased its binding to substrate proteins. S56A bound to and hence glycosylated more proteins, while T12A associated with fewer substrates. Proteomic studies combined with cell proliferation/cell cycle analyses indicated that S56A substantially enhanced cell proliferation, while T12A reduced it, and T12A led to a G2/M cell cycle arrest, due to O-GlcNAcylation of diverse proteins. These findings demonstrate that the O-GlcNAc pattern on sOGT modulates its function in cells by targeting different proteins. |
HostingRepository | PRIDE |
AnnounceDate | 2019-09-16 |
AnnouncementXML | Submission_2019-09-25_04:12:32.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Yong Zhang |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-05-09 09:33:34 | ID requested | |
1 | 2019-09-16 00:39:28 | announced | |
⏵ 2 | 2019-09-25 04:12:33 | announced | 2019-09-25: Updated publication reference for PubMed record(s): 31527085. |
Publication List
Liu L, Li L, Ma C, Shi Y, Liu C, Xiao Z, Zhang Y, Tian F, Gao Y, Zhang J, Ying W, Wang PG, Zhang L, -GlcNAc transferase (sOGT) regulates its substrate selectivity. J Biol Chem, 294(45):16620-16633(2019) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: O-GlcNAc pattern;sOGT;site mapping;functional regulation |
Contact List
Lianwen zhang |
contact affiliation | college of pharmacy, Nankai university,Tianjin, 300353, China |
contact email | lianwen@nankai.edu.cn |
lab head | |
Yong Zhang |
contact affiliation | Beijing Proteome Research Center |
contact email | nankai1989@foxmail.com |
dataset submitter | |
Full Dataset Link List
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/2019/09/PXD009731 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD009731
- Label: PRIDE project
- Name: O-GlcNAc pattern of sOGT regulates its substrate selectivity and function