B4GALT2

Beta-1,4-galactosyltransferase 2 is an enzyme that in humans is encoded by the B4GALT2 gene.[5][6][7]

B4GALT2
Identifiers
Aliases	B4GALT2, B4Gal-T2, B4Gal-T3, beta4Gal-T2, beta-1,4-galactosyltransferase 2
External IDs	OMIM: 604013 MGI: 1858493 HomoloGene: 2804 GeneCards: B4GALT2
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p34.1 Start 43,978,943 bp[1] End 43,991,170 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D2.1 Start 117,869,260 bp[2] End 117,883,487 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • N-acetyllactosamine synthase activity • galactosyltransferase activity • lactose synthase activity • metal ion binding • transferase activity, transferring glycosyl groups • beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Cellular component • integral component of membrane • Golgi cisterna membrane • Golgi membrane • membrane • nucleoplasm • Golgi apparatus • intracellular membrane-bounded organelle Biological process • protein glycosylation • keratan sulfate biosynthetic process • memory • locomotory behavior • visual learning • cerebellar Purkinje cell layer development • brain development • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8704	53418
Ensembl	ENSG00000117411	ENSMUSG00000028541
UniProt	O60909	Q9Z2Y2
RefSeq (mRNA)	NM_030587 NM_001005417 NM_003780	NM_001253381 NM_017377
RefSeq (protein)	NP_001005417 NP_003771 NP_085076	NP_001240310 NP_059073
Location (UCSC)	Chr 1: 43.98 – 43.99 Mb	Chr 4: 117.87 – 117.88 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. The enzyme encoded by this gene synthesizes N-acetyllactosamine in glycolipids and glycoproteins. Its substrate specificity is affected by alpha-lactalbumin but it is not expressed in lactating mammary tissue. Two transcript variants encoding the same protein have been found for this gene.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000117411 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028541 - 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.
5. Almeida R, Amado M, David L, Levery SB, Holmes EH, Merkx G, van Kessel AG, Rygaard E, Hassan H, Bennett E, Clausen H (Jan 1998). "A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3". J Biol Chem. 272 (51): 31979–91. doi:10.1074/jbc.272.51.31979. PMID 9405390.
6. Lo NW, Shaper JH, Pevsner J, Shaper NL (Aug 1998). "The expanding beta 4-galactosyltransferase gene family: messages from the databanks". Glycobiology. 8 (5): 517–26. doi:10.1093/glycob/8.5.517. PMID 9597550.
7. "Entrez Gene: B4GALT2 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 2".

External links

• Human B4GALT2 genome location and B4GALT2 gene details page in the UCSC Genome Browser.

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.
• 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. doi:10.1089/aid.1990.6.371. 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. Bibcode:1989PNAS...86.3384P. doi:10.1073/pnas.86.9.3384. PMC 287137. 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. doi:10.1128/jvi.63.6.2452-2456.1989. PMC 250699. 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.
• Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID 2829950.
• Guo S, Sato T, Shirane K, Furukawa K (2002). "Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells". Glycobiology. 11 (10): 813–20. doi:10.1093/glycob/11.10.813. PMID 11588157.
• 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.
• 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.
• 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.
• Ben-Mahmud BM, Mann GE, Datti A, et al. (2005). "Tumor necrosis factor-alpha in diabetic plasma increases the activity of core 2 GlcNAc-T and adherence of human leukocytes to retinal endothelial cells: significance of core 2 GlcNAc-T in diabetic retinopathy". Diabetes. 53 (11): 2968–76. doi:10.2337/diabetes.53.11.2968. PMID 15504978.
• Sasaki N, Manya H, Okubo R, et al. (2005). "beta4GalT-II is a key regulator of glycosylation of the proteins involved in neuronal development". Biochem. Biophys. Res. Commun. 333 (1): 131–7. doi:10.1016/j.bbrc.2005.05.082. PMID 15939404.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
• Jiang J, Zhou J, Wei Y, et al. (2007). "beta4GalT-II increases cisplatin-induced apoptosis in HeLa cells depending on its Golgi localization". Biochem. Biophys. Res. Commun. 358 (1): 41–6. doi:10.1016/j.bbrc.2007.04.044. PMID 17470362.