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 22.214.171.124 4 56
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 Metabolism of proteins and Transport to the Golgi and subsequent modification. Gene Ontology (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.