B3GNT2

B3GNT2
Identifiers
AliasesB3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGNT2, BGnT-2, 3-Gn-T1, 3-Gn-T2, beta-1, beta3Gn-T1, beta3Gn-T2, UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2
External IDsMGI: 1889505 HomoloGene: 4797 GeneCards: B3GNT2
Gene location (Human)
Chr.Chromosome 2 (human)[1]
Band2p15Start62,196,113 bp[1]
End62,224,731 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

10678

53625

Ensembl

ENSG00000170340

ENSMUSG00000051650

UniProt

Q9NY97

Q9Z222

RefSeq (mRNA)

NM_006577
NM_033252
NM_001319075
NM_018554

NM_001169114
NM_016888

RefSeq (protein)

NP_001306004
NP_006568

NP_001162585
NP_058584

Location (UCSC)Chr 2: 62.2 – 62.22 MbChr 11: 22.76 – 22.86 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 is an enzyme that in humans is encoded by the B3GNT2 gene.[5][6][7]

This gene encodes a member of the beta-1,3-N-acetylglucosaminyltransferase family. This enzyme is a type II transmembrane protein. It prefers the substrate of lacto-N-neotetraose, and is involved in the biosynthesis of poly-N-acetyllactosamine chains.[7]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000170340 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000051650 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Zhou D, Dinter A, Gutierrez Gallego R, Kamerling JP, Vliegenthart JF, Berger EG, Hennet T (Mar 1999). "A β-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine synthase activity is structurally related to β-1,3-galactosyltransferases". Proc Natl Acad Sci U S A. 96 (2): 406–11. doi:10.1073/pnas.96.2.406. PMC 15149. PMID 9892646.
  6. ↑ Shiraishi N, Natsume A, Togayachi A, Endo T, Akashima T, Yamada Y, Imai N, Nakagawa S, Koizumi S, Sekine S, Narimatsu H, Sasaki K (May 2001). "Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family". J Biol Chem. 276 (5): 3498–507. doi:10.1074/jbc.M004800200. PMID 11042166.
  7. 1 2 "Entrez Gene: B3GNT2 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2".

Further reading

  • Amado M, Almeida R, Schwientek T, Clausen H (2000). "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions". Biochim. Biophys. Acta. 1473 (1): 35–53. doi:10.1016/S0304-4165(99)00168-3. PMID 10580128.
  • Ju T, Cummings RD (2003). "A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16613–8. doi:10.1073/pnas.262438199. PMC 139192. PMID 12464682.
  • 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. PMC 139241. PMID 12477932.
  • Isshiki S, Kudo T, Nishihara S, et al. (2003). "Lewis type 1 antigen synthase (beta3Gal-T5) is transcriptionally regulated by homeoproteins". J. Biol. Chem. 278 (38): 36611–20. doi:10.1074/jbc.M302681200. PMID 12855703.
  • Hayashi N, Nakamori S, Okami J, et al. (2004). "Association between expression levels of CA 19-9 and N-acetylglucosamine-beta;1,3-galactosyltransferase 5 gene in human pancreatic cancer tissue". Pathobiology. 71 (1): 26–34. doi:10.1159/000072959. PMID 14555842.
  • Mare L, Trinchera M (2004). "Suppression of beta 1,3galactosyltransferase beta 3Gal-T5 in cancer cells reduces sialyl-Lewis a and enhances poly N-acetyllactosamines and sialyl-Lewis x on O-glycans". Eur. J. Biochem. 271 (1): 186–94. doi:10.1046/j.1432-1033.2003.03919.x. PMID 14686931.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Zheng H, Li Y, Ji C, et al. (2005). "Characterization of a cDNA encoding a protein with limited similarity to beta1, 3-N-acetylglucosaminyltransferase". Mol. Biol. Rep. 31 (3): 171–5. doi:10.1023/B:MOLE.0000043552.32411.67. PMID 15560372.
  • Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human Plasma N-Glycoproteome Analysis by Immunoaffinity Subtraction, Hydrazide Chemistry, and Mass Spectrometry". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.


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