B4GALT1

UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1
PDB rendering based on 1nf5.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1nf5​, 1nhe​, 1nkh​, 1nmm​, 1nqi​, 1nwg​, 1o0r​, 1o23​, 1oqm​, 2ae7​, 2aec​, 2aes​, 2agd​, 2ah9​, 2fy7​, 2fya​, 2fyb​
Identifiers
Symbols	B4GALT1 ; GTB; B4GAL-T1; DKFZp686N19253; GGTB2; GT1; MGC50983; beta4Gal-T1
External IDs	Template:OMIM5 Template:MGI HomoloGene: 20378
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1, also known as B4GALT1, is a human gene.

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. This gene is unique among the beta4GalT genes because it encodes an enzyme that participates both in glycoconjugate and lactose biosynthesis. For the first activity, the enzyme adds galactose to N-acetylglucosamine residues that are either monosaccharides or the nonreducing ends of glycoprotein carbohydrate chains. The second activity is restricted to lactating mammary tissues where the enzyme forms a heterodimer with alpha-lactalbumin to catalyze UDP-galactose + D-glucose <=> UDP + lactose. The two enzymatic forms result from alternate transcription initiation sites and post-translational processing. Two transcripts, which differ only at the 5' end, with approximate lengths of 4.1 kb and 3.9 kb encode the same protein. The longer transcript encodes the type II membrane-bound, trans-Golgi resident protein involved in glycoconjugate biosynthesis. The shorter transcript encodes a protein which is cleaved to form the soluble lactose synthase.

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.CS1 maint: Multiple names: authors list (link)
• Gerber AC, Kozdrowski I, Wyss SR, Berger EG (1979). "The charge heterogeneity of soluble human galactosyltransferases isolated from milk, amniotic fluid and malignant ascites". Eur. J. Biochem. 93 (3): 453–60. PMID 33805.CS1 maint: Multiple names: authors list (link)
• Uejima T, Uemura M, Nozawa S, Narimatsu H (1992). "Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies". Cancer Res. 52 (22): 6158–63. PMID 1384956.CS1 maint: Multiple names: authors list (link)
• Lopez LC, Youakim A, Evans SC, Shur BD (1991). "Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase". J. Biol. Chem. 266 (24): 15984–91. PMID 1714903.CS1 maint: Multiple names: authors list (link)
• Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC (1991). "Genomic structure and expression of human beta-1,4-galactosyltransferase". Biochem. Biophys. Res. Commun. 176 (3): 1269–76. PMID 1903938.CS1 maint: Multiple names: authors list (link)
• Aoki D, Appert HE, Johnson D; et al. (1990). "Analysis of the substrate binding sites of human galactosyltransferase by protein engineering". EMBO J. 9 (10): 3171–8. PMID 2120039.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Watzele G, Berger EG (1991). "Near identity of HeLa cell galactosyltransferase with the human placental enzyme". Nucleic Acids Res. 18 (23): 7174. PMID 2124683.
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Appert HE, Rutherford TJ, Tarr GE; et al. (1986). "Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence". Biochem. Biophys. Res. Commun. 138 (1): 224–9. PMID 3091013.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Appert HE, Rutherford TJ, Tarr GE; et al. (1986). "Isolation of a cDNA coding for human galactosyltransferase". Biochem. Biophys. Res. Commun. 139 (1): 163–8. PMID 3094506.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Furukawa K, Roth S, Sawicki J (1987). "Several galactosyltransferase activities are associated with mouse chromosome 17". Genetics. 114 (3): 983–91. PMID 3098628.CS1 maint: Multiple names: authors list (link)
• Masri KA, Appert HE, Fukuda MN (1989). "Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase)". Biochem. Biophys. Res. Commun. 157 (2): 657–63. PMID 3144273.CS1 maint: Multiple names: authors list (link)
• Roth J, Lentze MJ, Berger EG (1985). "Immunocytochemical demonstration of ecto-galactosyltransferase in absorptive intestinal cells". J. Cell Biol. 100 (1): 118–25. PMID 3917437.CS1 maint: Multiple names: authors list (link)
• Roth J, Berger EG (1982). "Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae". J. Cell Biol. 93 (1): 223–9. PMID 6121819.
• Chatterjee SK, Mukerjee S, Tripathi PK (1995). "Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones". Int. J. Biochem. Cell Biol. 27 (3): 329–36. PMID 7540104.CS1 maint: Multiple names: authors list (link)
• Kudo T, Narimatsu H (1995). "The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells". Glycobiology. 5 (4): 397–403. PMID 7579794.