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PXD010173 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleO-GlcNAc pattern of sOGT regulates its substrate selectivity and function
DescriptionO-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.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterYong Zhang
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListO-(N-acetylamino)glucosyl-L-threonine; O-(N-acetylamino)glucosyl-L-serine; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue; deamidated residue
InstrumentLTQ Orbitrap Elite
Dataset History
RevisionDatetimeStatusChangeLog Entry
02018-06-20 07:27:09ID requested
12019-09-16 00:40:53announced
22019-09-25 02:49:17announced2019-09-25: 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 affiliationcollege of pharmacy, Nankai university,Tianjin, 300353, China
contact emaillianwen@nankai.edu.cn
lab head
Yong Zhang
contact affiliationBeijing Proteome Research Center
contact emailnankai1989@foxmail.com
dataset submitter
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