MGAT2

The product of this gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in this gene may lead to carbohydrate-deficient glycoprotein syndrome, type II. The coding region of this gene is intronless. Transcript variants with a spliced 5' UTR may exist, but their biological validity has not been determined. [provided by RefSeq]

mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase

Plays an essential role in protein N-glycosylation. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal mannose moiety in the core structure of the nascent N-linked glycan chain, giving rise to the second branch in complex glycans.

Oligosaccharide biosynthetic process Source: InterPro
Protein N-linked glycosylation Source: GO_Central
Protein N-linked glycosylation via asparagine Source: UniProtKB
Viral protein processing Source: Reactome

Golgi apparatus membrane

Congenital disorder of glycosylation 2A (CDG2A):
A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.

Cytoplasmic: 1-9
Helical: 10-29
Lumenal: 30-447