ST6GAL1

ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, also known as ST6GAL1, is a human gene.

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: ST6GAL1 ST6 beta-galactosamide alpha-2,6-sialyltranferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6480| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Bast BJ, Zhou LJ, Freeman GJ, "et al." |title=The HB-6, CDw75, and CD76 differentiation antigens are unique cell-surface carbohydrate determinants generated by the beta-galactoside alpha 2,6-sialyltransferase. |journal=J. Cell Biol. |volume=116 |issue= 2 |pages= 423–35 |year= 1992 |pmid= 1730763 |doi=
*cite journal | author=Stamenkovic I, Asheim HC, Deggerdal A, "et al." |title=The B cell antigen CD75 is a cell surface sialytransferase. |journal=J. Exp. Med. |volume=172 |issue= 2 |pages= 641–3 |year= 1990 |pmid= 2373995 |doi=
*cite journal | author=Grundmann U, Nerlich C, Rein T, Zettlmeissl G |title=Complete cDNA sequence encoding human beta-galactoside alpha-2,6-sialyltransferase. |journal=Nucleic Acids Res. |volume=18 |issue= 3 |pages= 667 |year= 1990 |pmid= 2408023 |doi=
*cite journal | author=Lance P, Lau KM, Lau JT |title=Isolation and characterization of a partial cDNA for a human sialyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=164 |issue= 1 |pages= 225–32 |year= 1989 |pmid= 2803295 |doi=
*cite journal | author=Rabouille C, Hui N, Hunte F, "et al." |title=Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. |journal=J. Cell. Sci. |volume=108 ( Pt 4) |issue= |pages= 1617–27 |year= 1995 |pmid= 7615680 |doi=
*cite journal | author=Bruneau N, Lombardo D |title=Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13524–33 |year= 1995 |pmid= 7768954 |doi=
*cite journal | author=Wang X, Vertino A, Eddy RL, "et al." |title=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. |journal=J. Biol. Chem. |volume=268 |issue= 6 |pages= 4355–61 |year= 1993 |pmid= 7786324 |doi=
*cite journal | author=Hanasaki K, Varki A, Stamenkovic I, Bevilacqua MP |title=Cytokine-induced beta-galactoside alpha-2,6-sialyltransferase in human endothelial cells mediates alpha 2,6-sialylation of adhesion molecules and CD22 ligands. |journal=J. Biol. Chem. |volume=269 |issue= 14 |pages= 10637–43 |year= 1994 |pmid= 8144653 |doi=
*cite journal | author=Aasheim HC, Aas-Eng DA, Deggerdal A, "et al." |title=Cell-specific expression of human beta-galactoside alpha 2,6-sialyltransferase transcripts differing in the 5' untranslated region. |journal=Eur. J. Biochem. |volume=213 |issue= 1 |pages= 467–75 |year= 1993 |pmid= 8477718 |doi=
*cite journal | author=Andersson B, Wentland MA, Ricafrente JY, "et al." |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138
*cite journal | author=Sgroi D, Nocks A, Stamenkovic I |title=A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the I-type lectins CD22 and CD33. |journal=J. Biol. Chem. |volume=271 |issue= 31 |pages= 18803–9 |year= 1996 |pmid= 8702538 |doi=
*cite journal | author=Lo NW, Lau JT |title=Transcription of the beta-galactoside alpha 2,6-sialyltransferase gene in B lymphocytes is directed by a separate and distinct promoter. |journal=Glycobiology |volume=6 |issue= 3 |pages= 271–9 |year= 1996 |pmid= 8724135 |doi=
*cite journal | author=Lo NW, Lau JT |title=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. |journal=Biochem. Biophys. Res. Commun. |volume=228 |issue= 2 |pages= 380–5 |year= 1996 |pmid= 8920923 |doi=
*cite journal | author=Tsuji S, Datta AK, Paulson JC |title=Systematic nomenclature for sialyltransferases. |journal=Glycobiology |volume=6 |issue= 7 |pages= v-vii |year= 1997 |pmid= 8953271 |doi=
*cite journal | author=Ma J, Qian R, Rausa FM, Colley KJ |title=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. |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 672–9 |year= 1997 |pmid= 8995311 |doi=
*cite journal | author=Yu W, Andersson B, Worley KC, "et al." |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=
*cite journal | author=Lo NW, Lau JT |title=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. |journal=Glycobiology |volume=9 |issue= 9 |pages= 907–14 |year= 1999 |pmid= 10460832 |doi=
*cite journal | author=Laroy W, Ameloot P, Contreras R |title=Characterization of sialyltransferase mutants using surface plasmon resonance. |journal=Glycobiology |volume=11 |issue= 3 |pages= 175–82 |year= 2001 |pmid= 11320056 |doi=
*cite journal | author=Qian R, Chen C, Colley KJ |title=Location and mechanism of alpha 2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 28641–9 |year= 2001 |pmid= 11356854 |doi= 10.1074/jbc.M103664200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899

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