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B4GALT1Processed beta-1,4-galactosyltransferase 1; The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. (398 aa)    
Predicted Functional Partners:
LALBA
Alpha-lactalbumin; Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N- acetylglucosamine of the oligosaccharide chains in glycoproteins; Belongs to the glycosyl hydrolase 22 family.
    
 0.998
FUT6
Alpha-(1,3)-fucosyltransferase 6; Enzyme involved in the biosynthesis of the E-Selectin ligand, sialyl-Lewis X. Catalyzes the transfer of fucose from GDP-beta-fucose to alpha-2,3 sialylated substrates.
   
 
 0.984
B3GALT1
Beta-1,3-galactosyltransferase 1; Beta-1,3-galactosyltransferase that transfers galactose from UDP-alpha-D-galactose to substrates with a terminal beta-N- acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N-acetylglucosamine (alpha- GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues.
   
 
 0.984
ST6GAL1
Beta-galactoside alpha-2,6-sialyltransferase 1; Transfers sialic acid from CMP-sialic acid to galactose- containing acceptor substrates.
     
 0.980
B3GALT2
Beta-1,3-galactosyltransferase 2; Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N- acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha- GalNAc) residues.
   
 
 0.973
FUT8
Alpha-(1,6)-fucosyltransferase; Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. Belongs to the glycosyltransferase 23 family.
   
 
 0.971
FUT5
Alpha-(1,3)-fucosyltransferase 5; May catalyze alpha-1,3 glycosidic linkages involved in the expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens.
   
 
 0.969
B3GNT2
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2; Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors. Probably constitutes the main polylactosamine synthase. Belongs to the glycosyltransferase 31 family.
   
 
 0.967
ST3GAL3
CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase; Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4- GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal- beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta- 1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc. Belongs to the glycosyltransferase 29 family.
     
 0.957
ST3GAL6
Type 2 lactosamine alpha-2,3-sialyltransferase; Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3- sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1; Belongs to the glycosyltransferase 29 family.
     
 0.954
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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