B3GNT2

B3GNT2
Identifiers
Aliases	B3GNT2, 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 IDs	OMIM: 605581 MGI: 1889505 HomoloGene: 4797 GeneCards: B3GNT2
Gene location (Human)
Chr.	Chromosome 2 (human)
End	62,224,731 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	22,810,961 bp
RNA expression pattern
	Top expressed in
	secondary oocyte; ; visceral pleura; ; germinal epithelium; ; lower lobe of lung; ; parietal pleura; ; jejunal mucosa; ; duodenum; ; gallbladder; ; bronchial epithelial cell; ; oral cavity;
	Top expressed in
	secondary oocyte; ; adrenal gland; ; proximal tubule; ; lung; ; urinary bladder; ; placenta; ; yolk sac; ; thymus; ; lip; ; kidney;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; glycosyltransferase activity; galactosyltransferase activity; N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; acetylgalactosaminyltransferase activity; protein binding;
Cellular component	integral component of membrane; Golgi apparatus; membrane; Golgi membrane; endoplasmic reticulum;
Biological process	poly-N-acetyllactosamine biosynthetic process; axon guidance; protein glycosylation; sensory perception of smell; O-glycan processing; keratan sulfate biosynthetic process; cellular response to leukemia inhibitory factor;
	Sources:Amigo / QuickGO
Orthologs
	10678
	53625
	ENSG00000170340
	ENSMUSG00000051650
	Q9NY97
	Q9Z222
	NM_006577; NM_033252; NM_001319075; NM_018554
	NM_001169114; NM_016888
	NP_001306004; NP_006568
	NP_001162585; NP_058584
	Wikidata
View/Edit Human	View/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 edit

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000170340 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000051650 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:1999PNAS...96..406Z. doi:10.1073/pnas.96.2.406. PMC 15149. PMID 9892646.
^ 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.
^ ^a ^b "Entrez Gene: B3GNT2 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2".

External links edit

Human B3GNT2 genome location and B3GNT2 gene details page in the UCSC Genome Browser.

Further reading edit

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. Bibcode:2002PNAS...9916899M. 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. S2CID 11013021.
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): 186–194. doi:10.1046/j.1432-1033.2003.03919.x. PMID 14686931. S2CID 38965439.
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. S2CID 22952647.
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.

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000170340 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000051650 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9892646-5] 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. Bibcode:1999PNAS...96..406Z. doi:10.1073/pnas.96.2.406. PMC 15149. PMID 9892646.

[pmid11042166-6] 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.

[entrez-7] "Entrez Gene: B3GNT2 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2".

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