MGAT3 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0050890Biological processcognition
GO_0008104Biological processprotein localization
GO_0006044Biological processN-acetylglucosamine metabolic process
GO_0006487Biological processprotein N-linked glycosylation
GO_0034599Biological processcellular response to oxidative stress
GO_0030334Biological processregulation of cell migration
GO_0050435Biological processamyloid-beta metabolic process
GO_1902966Biological processpositive regulation of protein localization to early endosome
GO_1905166Biological processnegative regulation of lysosomal protein catabolic process
GO_0000139Cellular componentGolgi membrane
GO_0016020Cellular componentmembrane
GO_0003830Molecular functionbeta-1,4-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity
GO_0016757Molecular functionglycosyltransferase activity
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameMGAT3
Protein nameBeta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase (EC 2.4.1.144) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III) (GNT-III) (GlcNAc-T III) (N-acetylglucosaminyltransferase III)
Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
SynonymsGGNT3
DescriptionFUNCTION: It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate . Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location . Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation . In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage (By similarity). .

AccessionsENST00000418314.1
ENST00000429402.1
B0QY92
ENST00000341184.7
Q09327
B0QY93