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PXD014731 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleAspartate residues far from the active site drive O-GlcNAc transferase substrate selection
DescriptionHere we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection. Changing these residues to alanines alters substrate selectivity and unexpectedly increases rates of protein glycosylation. Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues Cterminal to the glycosite. In addition to guiding design of inhibitors that target OGT’s TPR domain, this information will inform efforts to engineer substrates to explore biological functions.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterChristina Woo
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListNo PTMs are included in the dataset
InstrumentLTQ Orbitrap
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-07-24 06:14:10ID requested
12019-07-26 03:29:25announced
22019-08-08 03:22:10announcedUpdated publication reference for PubMed record(s): 31373491.
Publication List
Joiner CM, Levine ZG, Aonbangkhen C, Woo CM, Walker S, Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection. J Am Chem Soc, 141(33):12974-12978(2019) [pubmed]
Keyword List
submitter keyword: glycoproteomics, O-glcNAc
Contact List
Christina Woo and Suzanne Walker
contact affiliationChemistry & Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138 and Department of Microbiology, Harvard Medical School, 4 Blackfan Circle, Boston, MA 02115
contact emailcwoo@chemistry.harvard.edu
lab head
Christina Woo
contact affiliationHarvard University
contact emailcwoo@chemistry.harvard.edu
dataset submitter
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