MGAT4B

From Wikipedia, the free encyclopedia


Mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme B
Identifiers
Symbol(s) MGAT4B; GNT-IV; GNT-IVB
External IDs OMIM: 604561 MGI2143974 HomoloGene8611
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 11282 103534
Ensembl ENSG00000161013 ENSMUSG00000036620
Refseq NM_014275 (mRNA)
NP_055090 (protein)
NM_145926 (mRNA)
NP_666038 (protein)
Location Chr 5: 179.16 - 179.17 Mb Chr 11: 50.07 - 50.08 Mb
Pubmed search [1] [2]

Mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme B, also known as MGAT4B, is a human gene.[1]

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.[1]

[edit] References

[edit] Further reading

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  • Dedera DA, Gu RL, Ratner L (1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function.". Virology 187 (1): 377–82. PMID 1736542. 
  • Kalyanaraman VS, Rodriguez V, Veronese F, et al. (1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1.". AIDS Res. Hum. Retroviruses 6 (3): 371–80. PMID 2187500. 
  • 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. PMID 2541446. 
  • Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport.". J. Virol. 63 (6): 2452–6. PMID 2542563. 
  • Kozarsky K, Penman M, Basiripour L, et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein.". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9. PMID 2649653. 
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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. 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. PMID 3264072. 
  • 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. PMID 8093218. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298. 
  • 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. PMID 8673525. 
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  • Yoshida A, Minowa MT, Takamatsu S, et al. (1999). "A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment.". Glycoconj. J. 15 (12): 1115–23. PMID 10372966. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309. 
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