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- Table of Contents
Facts about Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase.
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 as it's unable to utilize the bisected oligosaccharide as a substrate (PubMed:19403558).
Human | |
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Gene Name: | MGAT3 |
Uniprot: | Q09327 |
Entrez: | 4248 |
Belongs to: |
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glycosyltransferase 17 family |
beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase; EC 2.4.1.144; FLJ43371; GGNT3; GlcNAc-T III; GNT3; GNT-III; GNT-IIIMGC142278; mannosyl (beta-1,4-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase; MGAT3; MGC141943; N-acetylglucosaminyltransferase III; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
Mass (kDA):
61.313 kDA
Human | |
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Location: | 22q13.1 |
Sequence: | 22; NC_000022.11 (39457012..39492194) |
Golgi apparatus membrane; Single-pass type II membrane protein.
PMID: 8370666 by Ihara Y., et al. cDNA cloning, expression, and chromosomal localization of human N- acetylglucosaminyltransferase III (GnT-III).
PMID: 19403558 by Pinho S.S., et al. The role of N-acetylglucosaminyltransferase III and V in the post- transcriptional modifications of E-cadherin.