ST6GAL1

{{cs1 config|name-list-style=vanc}} {{Infobox_gene}} '''Beta-galactoside alpha-2,6-sialyltransferase 1''' is an enzyme that in humans is encoded by the ''ST6GAL1'' gene.<ref name="pmid2408023">{{cite journal | vauthors = 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 |date=Apr 1990 | pmid = 2408023 | pmc = 333489 | doi =10.1093/nar/18.3.667 }}</ref>

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.<ref name="entrez">{{cite web | title = Entrez Gene: ST6GAL1 ST6 beta-galactosamide alpha-2,6-sialyltransferase 1| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=6480}}</ref>

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.<ref>{{cite journal|last1=Lee|title=Transcriptional programs of lymphoid tissue capillary and high endothelium reveal control mechanisms for lymphocyte homing|journal=Nature Immunology|date=Oct 2014|volume=15|issue=10|pages=982–995|doi=10.1038/ni.2983|pmid=25173345|display-authors=etal|pmc=4222088}}</ref> ST6GAL1 expression has also shown to be upregulated in several types of cancers and has been shown to haves roles in cancer survival and metastasis.<ref>{{cite journal |last1=Garnham |first1=Rebecca |last2=Scott |first2=Emma |last3=Livermore |first3=Karen |last4=Munkley |first4=Jennifer |title=ST6GAL1: A key player in cancer |journal=Oncology Letters |date=August 2019 |volume=18 |issue=2 |pages=983–989 |doi=10.3892/ol.2019.10458 |pmid=31423157 |pmc=6607188 |doi-access=free }}</ref>

==References== {{reflist}}

==Further reading== {{refbegin}} *{{cite journal |vauthors=Bast BJ, Zhou LJ, Freeman GJ, etal |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=10.1083/jcb.116.2.423 | pmc=2289289 }} *{{cite journal |vauthors=Stamenkovic I, Asheim HC, Deggerdal A, etal |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=10.1084/jem.172.2.641 | pmc=2188328 }} *{{cite journal | vauthors=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=10.1016/0006-291X(89)91706-3 }} *{{cite journal |vauthors=Rabouille C, Hui N, Hunte F, etal |title=Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. | series=108 |journal=J. Cell Sci. |volume=( Pt 4) |pages= 1617–27 |year= 1995 |issue=4 |doi=10.1242/jcs.108.4.1617 |pmid= 7615680 }} *{{cite journal | vauthors=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=10.1074/jbc.270.22.13524 |doi-access=free }} *{{cite journal |vauthors=Wang X, Vertino A, Eddy RL, etal |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 |doi=10.1016/S0021-9258(18)53617-6 |pmid= 7786324 |doi-access=free }} *{{cite journal | vauthors=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 |doi=10.1016/S0021-9258(17)34107-8 |pmid= 8144653 |doi-access=free }} *{{cite journal |vauthors=Aasheim HC, Aas-Eng DA, Deggerdal A, etal |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=10.1111/j.1432-1033.1993.tb17783.x |doi-access= }} *{{cite journal |vauthors=Andersson B, Wentland MA, Ricafrente JY, etal |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 | vauthors=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=10.1074/jbc.271.31.18803 |doi-access=free }} *{{cite journal | vauthors=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=10.1093/glycob/6.3.271 |doi-access=free }} *{{cite journal | vauthors=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=10.1006/bbrc.1996.1670 }} *{{cite journal | vauthors=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= 10.1093/glycob/6.7.647 |doi-access= free }} *{{cite journal | vauthors=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=10.1074/jbc.272.1.672 |doi-access=free }} *{{cite journal |vauthors=Yu W, Andersson B, Worley KC, etal |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi= 10.1101/gr.7.4.353| pmc=139146 }} *{{cite journal | vauthors=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=10.1093/glycob/9.9.907 |doi-access=free }} *{{cite journal | vauthors=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=10.1093/glycob/11.3.175 |doi-access=free }} *{{cite journal | vauthors=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 |doi-access= free }} *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }} *{{cite journal |vauthors=Szabo R, Skropeta D, etal |title=Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities. |journal=Med. Res. Rev. |volume=37 |issue=2 |pages= 210–270 |year= 2017 |doi= 10.1002/med.21407 |pmid=27678392 |s2cid=26280291 |url=http://ro.uow.edu.au/cgi/viewcontent.cgi?article=5226&context=smhpapers }} {{refend}}