MGAT2

Protein-coding gene in the species Homo sapiens

MGAT2

Identifiers

Aliases

MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase, alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

External IDs

OMIM: 602616; MGI: 2384966; HomoloGene: 1806; GeneCards: MGAT2; OMA:MGAT2 - orthologs

Gene location (Human)

Chr.	Chromosome 14 (human)^[1]

Band	14q21.3	Start	49,620,799 bp^[1]
Band	14q21.3	End	49,623,481 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 12 (mouse)^[2]

Band	12\|12 C2	Start	69,230,931 bp^[2]
Band	12\|12 C2	End	69,233,544 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

jejunal mucosa

mucosa of sigmoid colon

decidua

periodontal fiber

corpus epididymis

caput epididymis

bronchial epithelial cell

tail of epididymis

seminal vesicula

skin of hip

Top expressed in

parotid gland

seminal vesicula

epithelium of stomach

decidua

calvaria

right kidney

gastrula

medullary collecting duct

transitional epithelium of urinary bladder

pyloric antrum

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity carbohydrate binding glycosyltransferase activity manganese ion binding protein homodimerization activity metal ion binding
Cellular component	integral component of membrane Golgi membrane Golgi stack Golgi apparatus membrane
Biological process	protein glycosylation oligosaccharide biosynthetic process protein N-linked glycosylation oligosaccharide metabolic process protein N-linked glycosylation via asparagine
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


4247


217664

Ensembl


ENSG00000168282


ENSMUSG00000043998

UniProt


Q10469


Q921V5

RefSeq (mRNA)


NM_002408 NM_001015883


NM_146035

RefSeq (protein)


NP_002399


NP_666147

Location (UCSC)

Chr 14: 49.62 – 49.62 Mb

Chr 12: 69.23 – 69.23 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT2 gene.^[5]^[6]

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.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000168282 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000043998 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Tan J, D'Agostaro AF, Bendiak B, Reck F, Sarkar M, Squire JA, Leong P, Schachter H (Sep 1995). "The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein". Eur J Biochem. 231 (2): 317–28. doi:10.1111/j.1432-1033.1995.tb20703.x. PMID 7635144.
^ ^a ^b "Entrez Gene: MGAT2 mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase".

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Pal R, Hoke GM, Sarngadharan MG (1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 86 (9): 3384–8. Bibcode:1989PNAS...86.3384P. doi:10.1073/pnas.86.9.3384. PMC 287137. PMID 2541446.
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Blough HA, Pauwels R, De Clercq E, et al. (1987). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.
Montefiori DC, Robinson WE, Mitchell WM (1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9248–52. Bibcode:1988PNAS...85.9248M. doi:10.1073/pnas.85.23.9248. PMC 282716. PMID 3264072.
D'Agostaro GA, Zingoni A, Moritz RL, et al. (1995). "Molecular cloning and expression of cDNA encoding the rat UDP-N-acetylglucosamine:alpha-6-D-mannoside beta-1,2-N-acetylglucosaminyltransferase II". J. Biol. Chem. 270 (25): 15211–21. doi:10.1074/jbc.270.25.15211. PMID 7797505.
Fenouillet E, Jones I, Powell B, et al. (1993). "Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain". J. Virol. 67 (1): 150–60. doi:10.1128/jvi.67.1.150-160.1993. PMC 237347. PMID 8093218.
Yeh JC, Seals JR, Murphy CI, et al. (1993). "Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system". Biochemistry. 32 (41): 11087–99. doi:10.1021/bi00092a019. PMID 8218172.
Bolmstedt A, Sjölander S, Hansen JE, et al. (1996). "Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12 (3): 213–20. doi:10.1097/00042560-199607000-00001. PMID 8673525.
Tan J, Dunn J, Jaeken J, Schachter H (1996). "Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disease with defective brain development". Am. J. Hum. Genet. 59 (4): 810–7. PMC 1914797. PMID 8808595.
Hu H, Shioda T, Moriya C, et al. (1996). "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface". J. Virol. 70 (11): 7462–70. doi:10.1128/jvi.70.11.7462-7470.1996. PMC 190813. PMID 8892864.
Papandreou MJ, Fenouillet E (1997). "Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation". FEBS Lett. 406 (1–2): 191–5. doi:10.1016/S0014-5793(97)00273-1. PMID 9109416. S2CID 17660.