Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation.
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The human MGAT1 gene was identified by complementation of the N-glycosylation defect of the Lec1 CHO mutant, and the cloned full-length cDNA encodes an active GlcNAc-TI (EC 2.4.1.101); the 445-aa protein is a type II Golgi transferase.
"full-length cDNA encoding human GlcNAc-TI activity. The overall features of the cDNA and deduced protein sequence (445 amino acids) are typical of other Golgi transferases that are type II transmembrane proteins."
Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells.
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Live-cell BiFC shows MGAT1 (GnTI) forms Golgi-localized homodimers and a functionally relevant medial-Golgi heterodimer with MGAT2 (GnTII); BiFC signal was detected only in the Golgi membranes.
"the BiFC signal with GnTI was detected only in the Golgi membranes of live cells"
A universal glycoenzyme biosynthesis pipeline that enables efficient cell-free remodeling of glycans.
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A SIMPLEx-based platform produced ~98 difficult-to-express glycosyltransferases (predominantly human) as water-soluble, catalytically active enzymes for cell-free glycan remodeling, including complex-type N-glycan synthesis; UniProt cites this work as experimental evidence for MGAT1 catalytic activity.
"facile production of 98 difficult-to-express GTs, predominantly of human origin"
Identification of IFITM3 and MGAT1 as novel interaction partners of BRI3 by yeast two-hybrid screening.
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MGAT1 was identified and confirmed (Y2H, co-IP, confocal colocalization) as an interaction partner of BRI3 (stronger with BRI3 isoform a/1), colocalizing in the perinuclear region.
"intense colocalization of BRI3 with MGAT1, especially in the perinuclear area of Huh7 cells"
Proteomic analysis of cerebrospinal fluid extracellular vesicles: a comprehensive dataset.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Defining the membrane proteome of NK cells.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
Addition of GlcNAc to the glycan on the A arm
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Reactome reaction for the MGAT1-catalyzed first committed step in complex and hybrid N-glycan synthesis, modeled at the ER-Golgi intermediate compartment / Golgi membrane.
"This is the first committed step in the synthesis of complex and hybrid N-glycans"
Spike trimer glycoside chains are extended
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Reactome reaction in which GlcNAc-TI (MGAT1) adds a GlcNAc residue to high-mannose chains of the SARS-CoV spike glycoprotein during its N-glycan maturation.
"The N-acetylglucosaminyltransferase called GlcNAc-TI (MGAT1) adds a GlcNAc residue in the core of some high-mannose chains"
Maturation of spike protein
Maturation of spike protein
Spike trimer glycoside chains are extended
FutureHouse Falcon deep-research report for MGAT1
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Deep-research synthesis: MGAT1/GnT-I is a Golgi type II GT13 glycosyltransferase that catalyzes the first committed step of complex/hybrid N-glycan synthesis (UDP-GlcNAc to alpha-1,3-Man arm of Man5GlcNAc2; Mn2+-dependent); its many developmental/immune/cancer phenotypes are indirect, substrate-mediated consequences of altered N-glycans and should not be annotated as direct MGAT1 functions.
"A key annotation risk is conflating the pleiotropic consequences of altered N-glycan structures on substrate glycoproteins with direct MGAT1 molecular activities."