Search results for MGAT3

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Species

Types

Compartments

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Protein (1 results from a total of 1)

Identifier: R-HSA-975897
Species: Homo sapiens
Compartment: Golgi membrane
Primary external reference: UniProt: MGAT3: Q09327

Reaction (2 results from a total of 2)

Identifier: R-HSA-975926
Species: Homo sapiens
Compartment: Golgi lumen, Golgi membrane
The addition of a bisecting GlcNAc to a complex N-glycan by MGAT3 is one of the most important regulatory steps in N-glycosylation, directing the pathway toward the synthesis of complex and hybrid N-glycans. This addition changes the structure of the N-glycan and inhibits further modification by MGAT2, MGAT4, MGAT5A/B and FUT8. Defects in MGAT3 have been shown to be associated with predisposition to cancer and several developmental defects (Song et al 2010; Stanley 2002).
Identifier: R-HSA-975916
Species: Homo sapiens
Compartment: Golgi membrane, Golgi lumen
N-acetylglucosaminyltransferase (GnT)-V catalyzes the addition of GlcNAc beta 1,4 on the GlcNAc beta1,2 Man,alpha1,6 arm of complex type N-Glycans (Park C et al, 1999; Granowski M et al, 2000; Wang L et al, 2007). The activity of MGAT5 competes with MGAT3 (Pinho SS et al, 2009) and is associated with gastric cancer (Tian H et al, 2008) and multiple sclerosis (Brynedal B et al, 2010).

Pathway (2 results from a total of 2)

Identifier: R-HSA-975578
Species: Homo sapiens
If MAN2 acts before MGAT3, the pathway progresses to complex N-glycans, because MAN2 is not able to operate on bisected oligosaccharides (11421343, page 5). The expression of MAN2 over MGAT3 in a tissue can regulate the synthesis of hybrid or complex N-glycans.
Identifier: R-HSA-975574
Species: Homo sapiens
The transfer of a bisecting GlcNAc by MGAT3 commits the pathway toward the synthesis of hybrid glycans, because MAN2 is not able to operate on bisected oligosaccharides (Schachter et al 2000, Priatel JJ et al, 1997). The expression of MGAT3 over MGAT2 in a tissue can regulate the synthesis of hybrid toward complex N-glycans. The addition of a GlcNAc between the two arms also prevents the action of MGAT4, MGAT5 and FUT8.
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