Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity.
Large-scale mapping of human protein-protein interactions by mass spectrometry.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.
Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are enzymatically active.
Comparative Proteomics Reveals Important Viral-Host Interactions in HCV-Infected Human Liver Cells.
Bi-allelic UGGT1 variants cause a congenital disorder of glycosylation.
UGGT1,2 transfers glucose from DbGP to (un)folded protein:(GlcNAc)2 (Man)8b
ER Quality Control Compartment (ERQC)
Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint.
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UGGT1 has a seven-domain topology with four N-terminal thioredoxin-like domains (TRXL1-4) arranged in an arc, two beta-sandwich domains, and a C-terminal GT24 catalytic domain
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Interdomain conformational flexibility is required for activity; engineered interdomain disulfides that rigidify UGGT reduce catalytic function
ER chaperones use a protein folding and quality control glyco-code.
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UGGT1-mediated reglucosylation writes a programmable glyco-code that determines which ER chaperones engage substrates at specific glycosylation sites
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UGGT1 deletion reduces monoglucosylated AAT by more than half; UGGT1/2 double deletion abolishes glucosylation
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UGGT preferentially modifies particular glycosylation sites (e.g., AAT N247 more than N83), supporting positional logic in the glyco-code
UGGT1-mediated reglucosylation of <i>N</i> -glycan competes with ER-associated degradation of unstable and misfolded glycoproteins
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UGGT1 delays degradation of misfolded glycoproteins in a tug-of-war between reglucosylation/refolding and EDEM-mediated mannose trimming that commits substrates to ERAD
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UGGT2 protein levels are ~6.9% (HCT116) and ~29.8% (HeLa) of UGGT1, establishing UGGT1 as the dominant mammalian reglucosyltransferase
Insights into the interaction between UGGT, the gatekeeper of folding in the ER, and its partner, the selenoprotein SEP15.
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AlphaFold-multimer predicts a specific UGGT1/SEP15 complex with SEP15 selenocysteine positioned proximal to UGGT1 catalytic region
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About 27% of expressed SEP15 co-occurs with UGGT1; interface mutants reduce binding to ~3.8-6.5%
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SEP15 affects a subset of UGGT1 clients rather than globally shifting all UGGT activity (26 proteins with significantly altered glucosylation in SELENOF-null cells)
UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum.
Quantitative glycoproteomics reveals cellular substrate selectivity of the ER protein quality control sensors UGGT1 and UGGT2.