ST6GAL1: Difference between revisions

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{{Infobox_gene}}
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'''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>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = ST6 beta-galactosamide alpha-2,6-sialyltranferase 1
| HGNCid = 10860
| Symbol = ST6GAL1
| AltSymbols =; CD75; MGC48859; SIAT1; ST6Gal I; ST6GalI
| OMIM = 109675
| ECnumber = 
| Homologene = 2281
| MGIid = 108470
| Function = {{GNF_GO|id=GO:0003835 |text = beta-galactoside alpha-2,6-sialyltransferase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030173 |text = integral to Golgi membrane}}
| Process = {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0009311 |text = oligosaccharide metabolic process}} {{GNF_GO|id=GO:0040007 |text = growth}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6480
    | Hs_Ensembl = ENSG00000073849
    | Hs_RefseqProtein = NP_003023
    | Hs_RefseqmRNA = NM_003032
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 188131210
    | Hs_GenLoc_end = 188279035
    | Hs_Uniprot = P15907
    | Mm_EntrezGene = 20440
    | Mm_Ensembl = ENSMUSG00000022885
    | Mm_RefseqmRNA = NM_145933
    | Mm_RefseqProtein = NP_666045
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 23140096
    | Mm_GenLoc_end = 23275682
    | Mm_Uniprot = Q8BM62
  }}
}}
'''ST6 beta-galactosamide alpha-2,6-sialyltranferase 1''', also known as '''ST6GAL1''', is a human [[gene]].


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| section_title =  
| section_title =  
| 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 apparatus|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-sialyltranferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6480| accessdate = }}</ref>
| 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 apparatus|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-sialyltranferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6480| accessdate = }}</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|url=http://www.nature.com/ni/journal/v15/n10/full/ni.2983.html|display-authors=etal|pmc=4222088}}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
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| citations =  
| 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   |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 | 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   |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  | 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  | 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 | 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   |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) |issue= |pages= 1617–27 |year= 1995 |pmid= 7615680 |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  | 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  }}
*{{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   |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 |pmid= 7786324 |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  | 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 |pmid= 8144653 |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   |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 }}
*{{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   |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  | 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  | 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  }}
*{{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  | 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  }}
*{{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  | 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  | 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  | 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 }}
*{{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  | 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 }}
*{{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   |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  | 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  | 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 }}
*{{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  | 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 }}
*{{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  | 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 }}
*{{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   |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 }}
*{{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 }}
*{{cite journal   |vauthors=Szabo R, Skropeta D, etal |title=Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities. |journal=Med. Res. Rev. |volume=37 |pages= 210–270 |year= 2017 |doi= 10.1002/med.21407 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 20:54, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Wikidata
View/Edit Human

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. PMC 4222088. PMID 25173345.

Further reading



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