ST6GAL1
| ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 | |||||||||||
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| Identifiers | |||||||||||
| Symbols | ST6GAL1 ; CD75; MGC48859; SIAT1; ST6Gal I; ST6GalI | ||||||||||
| External IDs | Template:OMIM5 Template:MGI HomoloGene: 2281 | ||||||||||
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| Template:GNF Ortholog box | |||||||||||
| Species | Human | Mouse | |||||||||
| Entrez | n/a | n/a | |||||||||
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| RefSeq (mRNA) | n/a | n/a | |||||||||
| RefSeq (protein) | n/a | n/a | |||||||||
| Location (UCSC) | n/a | n/a | |||||||||
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ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, also known as ST6GAL1, is a human gene.
The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein, which is normally found in the Golgi but which can be proteolytically processed to a soluble form, is involved in the generation of the cell-surface carbohydrate determinants and differentiation antigens HB-6, CDw75, and CD76. This protein is a member of glycosyltransferase family 29. Three transcript variants encoding two different isoforms have been found for this gene.[1]
References
Further reading
- Bast BJ, Zhou LJ, Freeman GJ; et al. (1992). "The HB-6, CDw75, and CD76 differentiation antigens are unique cell-surface carbohydrate determinants generated by the beta-galactoside alpha 2,6-sialyltransferase". J. Cell Biol. 116 (2): 423–35. PMID 1730763.
- Stamenkovic I, Asheim HC, Deggerdal A; et al. (1990). "The B cell antigen CD75 is a cell surface sialytransferase". J. Exp. Med. 172 (2): 641–3. PMID 2373995.
- Grundmann U, Nerlich C, Rein T, Zettlmeissl G (1990). "Complete cDNA sequence encoding human beta-galactoside alpha-2,6-sialyltransferase". Nucleic Acids Res. 18 (3): 667. PMID 2408023.
- Lance P, Lau KM, Lau JT (1989). "Isolation and characterization of a partial cDNA for a human sialyltransferase". Biochem. Biophys. Res. Commun. 164 (1): 225–32. PMID 2803295.
- Rabouille C, Hui N, Hunte F; et al. (1995). "Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides". J. Cell. Sci. 108 ( Pt 4): 1617–27. PMID 7615680.
- Bruneau N, Lombardo D (1995). "Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase". J. Biol. Chem. 270 (22): 13524–33. PMID 7768954.
- Wang X, Vertino A, Eddy RL; et al. (1993). "Chromosome mapping and organization of the human beta-galactoside alpha 2,6-sialyltransferase gene. Differential and cell-type specific usage of upstream exon sequences in B-lymphoblastoid cells". J. Biol. Chem. 268 (6): 4355–61. PMID 7786324.
- Hanasaki K, Varki A, Stamenkovic I, Bevilacqua MP (1994). "Cytokine-induced beta-galactoside alpha-2,6-sialyltransferase in human endothelial cells mediates alpha 2,6-sialylation of adhesion molecules and CD22 ligands". J. Biol. Chem. 269 (14): 10637–43. PMID 8144653.
- Aasheim HC, Aas-Eng DA, Deggerdal A; et al. (1993). "Cell-specific expression of human beta-galactoside alpha 2,6-sialyltransferase transcripts differing in the 5' untranslated region". Eur. J. Biochem. 213 (1): 467–75. PMID 8477718.
- Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- Sgroi D, Nocks A, Stamenkovic I (1996). "A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the I-type lectins CD22 and CD33". J. Biol. Chem. 271 (31): 18803–9. PMID 8702538.
- Lo NW, Lau JT (1996). "Transcription of the beta-galactoside alpha 2,6-sialyltransferase gene in B lymphocytes is directed by a separate and distinct promoter". Glycobiology. 6 (3): 271–9. PMID 8724135.
- Lo NW, Lau JT (1996). "Novel heterogeneity exists in the 5'-untranslated region of the beta-galactoside alpha 2,6-sialytransferase mRNAs in the human B-lymphoblastoid cell line, louckes". Biochem. Biophys. Res. Commun. 228 (2): 380–5. PMID 8920923.
- Tsuji S, Datta AK, Paulson JC (1997). "Systematic nomenclature for sialyltransferases". Glycobiology. 6 (7): v–vii. PMID 8953271.
- Ma J, Qian R, Rausa FM, Colley KJ (1997). "Two naturally occurring alpha2,6-sialyltransferase forms with a single amino acid change in the catalytic domain differ in their catalytic activity and proteolytic processing". J. Biol. Chem. 272 (1): 672–9. PMID 8995311.
- Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.
- Lo NW, Lau JT (1999). "Transcription of the beta-galactoside alpha2,6-sialyltransferase gene (SIAT1) in B-lymphocytes: cell type-specific expression correlates with presence of the divergent 5'-untranslated sequence". Glycobiology. 9 (9): 907–14. PMID 10460832.
- Laroy W, Ameloot P, Contreras R (2001). "Characterization of sialyltransferase mutants using surface plasmon resonance". Glycobiology. 11 (3): 175–82. PMID 11320056.
- Qian R, Chen C, Colley KJ (2001). "Location and mechanism of alpha 2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing". J. Biol. Chem. 276 (31): 28641–9. doi:10.1074/jbc.M103664200. PMID 11356854.
- 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.
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