B4GALT2

From Wikipedia, the free encyclopedia

UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 2

Identifiers

B4GALT2; B4Gal-T2; B4Gal-T3; beta4Gal-T2

External IDs

OMIM: 604013 MGI: 1858493 HomoloGene: 2804

Gene ontology
Molecular Function:	• beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity • N-acetyllactosamine synthase activity • lactose synthase activity • galactosyltransferase activity • transferase activity, transferring glycosyl groups • manganese ion binding • metal ion binding
Cellular Component:	• membrane • integral to membrane
Biological Process:	• carbohydrate metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001005417 (mRNA)
NP_001005417 (protein)

XM_987031 (mRNA)
XP_992125 (protein)

Location

Chr 1: 44.22 - 44.23 Mb

Chr 4: 117.37 - 117.38 Mb

Pubmed search

[1]

[2]

UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 2, also known as B4GALT2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: B4GALT2 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 2.

[edit] 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. 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. 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.
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. PMID 2829950.
Almeida R, Amado M, David L, et al. (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. PMID 9405390.
Lo NW, Shaper JH, Pevsner J, Shaper NL (1998). "The expanding beta 4-galactosyltransferase gene family: messages from the databanks.". Glycobiology 8 (5): 517–26. PMID 9597550.
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. 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. doi:10.1073/pnas.242603899. 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. 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. 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. 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.