ST6GAL1

From Wikipedia, the free encyclopedia

ST6 beta-galactosamide alpha-2,6-sialyltranferase 1

Identifiers

ST6GAL1; CD75; MGC48859; SIAT1; ST6Gal I; ST6GalI

External IDs

OMIM: 109675 MGI: 108470 HomoloGene: 2281

Gene ontology
Molecular Function:	• beta-galactoside alpha-2,6-sialyltransferase activity
Cellular Component:	• membrane • integral to membrane • integral to Golgi membrane
Biological Process:	• protein amino acid glycosylation • humoral immune response • multicellular organismal development • oligosaccharide metabolic process • growth

Orthologs

Human

Mouse

Refseq

NM_003032 (mRNA)
NP_003023 (protein)

NM_145933 (mRNA)
NP_666045 (protein)

Location

Chr 3: 188.13 - 188.28 Mb

Chr 16: 23.14 - 23.28 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ Entrez Gene: ST6GAL1 ST6 beta-galactosamide alpha-2,6-sialyltranferase 1.

[edit] 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.