ST6GAL1

ST6 beta-galactosamide alpha-2,6-sialyltranferase 1
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4JS1​, 4JS2​
Identifiers
Symbols	ST6GAL1 ; SIAT1; ST6GalI; ST6N
External IDs	OMIM: 109675 MGI: 108470 HomoloGene: 2281 GeneCards: ST6GAL1 Gene
EC number	2.4.99.1
Gene ontology Molecular function • beta-galactoside alpha-2,6-sialyltransferase activity • protein binding • sialyltransferase activity Cellular component • Golgi membrane • integral component of Golgi membrane • Golgi cisterna membrane • extracellular exosome Biological process • N-acetylneuraminate metabolic process • dolichol-linked oligosaccharide biosynthetic process • protein O-linked glycosylation • humoral immune response • O-glycan processing • protein N-linked glycosylation via asparagine • post-translational protein modification • cellular protein metabolic process • sialylation Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6480	20440
Ensembl	ENSG00000073849	ENSMUSG00000022885
UniProt	P15907	Q64685
RefSeq (mRNA)	NM_003032	NM_001252505
RefSeq (protein)	NP_003023	NP_001239434
Location (UCSC)	Chr 3: 186.93 – 187.08 Mb	Chr 16: 23.22 – 23.36 Mb
PubMed search

Beta-galactoside alpha-2,6-sialyltransferase 1 is an enzyme that in humans is encoded by the ST6GAL1 gene.^[1]

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.^[2]

Transcripts of ST6GAL1 are found in mouse high endothelial cells of mesenteric lymph node and Peyer's patches, and it could be involved in the B cell homing to Peyer's patches.^[3]

References

1. Grundmann U, Nerlich C, Rein T, Zettlmeissl G (Apr 1990). "Complete cDNA sequence encoding human beta-galactoside alpha-2,6-sialyltransferase". Nucleic Acids Res 18 (3): 667. doi:10.1093/nar/18.3.667. PMC 333489. PMID 2408023.
2. "Entrez Gene: ST6GAL1 ST6 beta-galactosamide alpha-2,6-sialyltranferase 1".
3. Lee; et al. (Oct 2014). "Transcriptional programs of lymphoid tissue capillary and high endothelium reveal control mechanisms for lymphocyte homing". Nature Immunology 15 (10): 982–995. doi:10.1038/ni.2983. PMID 25173345.

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. doi:10.1083/jcb.116.2.423. PMC 2289289. 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. doi:10.1084/jem.172.2.641. PMC 2188328. PMID 2373995.
• 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. doi:10.1016/0006-291X(89)91706-3. 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. doi:10.1074/jbc.270.22.13524. 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. doi:10.1111/j.1432-1033.1993.tb17783.x. 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. doi:10.1074/jbc.271.31.18803. 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. doi:10.1093/glycob/6.3.271. 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. doi:10.1006/bbrc.1996.1670. PMID 8920923.
• Tsuji S, Datta AK, Paulson JC (1997). "Systematic nomenclature for sialyltransferases.". Glycobiology 6 (7): v–vii. doi:10.1093/glycob/6.7.647. 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. doi:10.1074/jbc.272.1.672. PMID 8995311.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. 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. doi:10.1093/glycob/9.9.907. PMID 10460832.
• Laroy W, Ameloot P, Contreras R (2001). "Characterization of sialyltransferase mutants using surface plasmon resonance.". Glycobiology 11 (3): 175–82. doi:10.1093/glycob/11.3.175. 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. PMC 139241. PMID 12477932.