Aliases for MGAT4B Gene
- Mannosyl (Alpha-1,3-)-Glycoprotein Beta-1,4-N-Acetylglucosaminyltransferase, Isozyme B 2 3 5
- UDP-N-Acetylglucosamine: Alpha-1,3-D-Mannoside Beta-1,4-N-Acetylglucosaminyltransferase IVb 3 4
- Mannosyl (Alpha-1,3-)-Glycoprotein Beta-1,4-N-Acetylglucosaminyltransferase, Isoenzyme B 2 3
- N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase IVb 3 4
- N-Acetylglucosaminyltransferase IVb 3 4
- GlcNAc-T IVb 3 4
- EC 188.8.131.52 4 61
External Ids for MGAT4B Gene
Previous GeneCards Identifiers for MGAT4B Gene
This gene encodes a key glycosyltransferase that regulates the formation of tri- and multiantennary branching structures in the Golgi apparatus. The encoded protein, in addition to the related isoenzyme A, catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc in a beta-1,4 linkage to the Man-alpha-1,3-Man-beta-1,4-GlcNAc arm of R-Man-alpha-1,6(GlcNAc-beta-1,2-Man-alpha-1,3)Man-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1-Asn. The encoded protein may play a role in regulating the availability of serum glycoproteins, oncogenesis, and differentiation. [provided by RefSeq, Jul 2008]
GeneCards Summary for MGAT4B Gene
MGAT4B (Mannosyl (Alpha-1,3-)-Glycoprotein Beta-1,4-N-Acetylglucosaminyltransferase, Isozyme B) is a Protein Coding gene. Among its related pathways are Transport to the Golgi and subsequent modification and N-glycan antennae elongation in the medial/trans-Golgi. GO annotations related to this gene include transferase activity, transferring hexosyl groups and alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity. An important paralog of this gene is MGAT4A.
UniProtKB/Swiss-Prot for MGAT4B Gene
Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N-glycan biosynthesis.