GAL3ST2: Difference between revisions

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{{Infobox_gene}}
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'''Galactose-3-O-sulfotransferase 2''' is an [[enzyme]] that in humans is encoded by the ''GAL3ST2'' [[gene]].<ref name="pmid11029462">{{cite journal |vauthors=Honke K, Tsuda M, Koyota S, Wada Y, Iida-Tanaka N, Ishizuka I, Nakayama J, Taniguchi N | title = Molecular cloning and characterization of a human beta-Gal-3'-sulfotransferase that acts on both type 1 and type 2 (Gal beta 1-3/1-4GlcNAc-R) oligosaccharides | journal = J Biol Chem | volume = 276 | issue = 1 | pages = 267–74 |date=Feb 2001 | pmid = 11029462 | pmc =  | doi = 10.1074/jbc.M005666200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GAL3ST2 galactose-3-O-sulfotransferase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64090| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Galactose-3-O-sulfotransferase 2
| HGNCid = 24869
| Symbol = GAL3ST2
| AltSymbols =; GAL3ST-2; GP3ST
| OMIM = 608237
| ECnumber = 
| Homologene = 41471
| MGIid = 2685834
| GeneAtlas_image1 = PBB_GE_GAL3ST2_gnf1h00397_at_tn.png
| Function = {{GNF_GO|id=GO:0001733 |text = galactosylceramide sulfotransferase activity}} {{GNF_GO|id=GO:0008146 |text = sulfotransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0009058 |text = biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 64090
    | Hs_Ensembl = ENSG00000154252
    | Hs_RefseqProtein = NP_071417
    | Hs_RefseqmRNA = NM_022134
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 242364913
    | Hs_GenLoc_end = 242399076
    | Hs_Uniprot = Q9H3Q3
    | Mm_EntrezGene = 381334
    | Mm_Ensembl = ENSMUSG00000034005
    | Mm_RefseqmRNA = XM_001006077
    | Mm_RefseqProtein = XP_001006077
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 95682898
    | Mm_GenLoc_end = 95706900
    | Mm_Uniprot = 
  }}
}}
'''Galactose-3-O-sulfotransferase 2''', also known as '''GAL3ST2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAL3ST2 galactose-3-O-sulfotransferase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64090| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a member of the galactose-3-O-sulfotransferase protein family. The product of this gene catalyzes sulfonation by transferring a sulfate group to the hydroxyl at C-3 of nonreducing beta-galactosyl residues, and it can act on both type 1 and type 2 (Galbeta 1-3/1-4GlcNAc-R) oligosaccharides with similar efficiencies, and on core 1 glycans. This enzyme has been implicated in tumor metastasis processes. This gene is different from the GAL3ST3 gene located on chromosome 11, which has also been referred to as GAL3ST2 and encodes a related enzyme with distinct tissue distribution and substrate specificities, compared to galactose-3-O-sulfotransferase 2.<ref name="entrez">{{cite web | title = Entrez Gene: GAL3ST2 galactose-3-O-sulfotransferase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64090| accessdate = }}</ref>
| summary_text = This gene encodes a member of the galactose-3-O-sulfotransferase protein family. The product of this gene catalyzes sulfonation by transferring a sulfate group to the hydroxyl at C-3 of nonreducing beta-galactosyl residues, and it can act on both type 1 and type 2 (Galbeta 1-3/1-4GlcNAc-R) oligosaccharides with similar efficiencies, and on core 1 glycans. This enzyme has been implicated in tumor metastasis processes. This gene is different from the GAL3ST3 gene located on chromosome 11, which has also been referred to as GAL3ST2 and encodes a related enzyme with distinct tissue distribution and substrate specificities, compared to galactose-3-O-sulfotransferase 2.<ref name="entrez">{{cite web | title = Entrez Gene: GAL3ST2 galactose-3-O-sulfotransferase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64090| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Honke K, Tsuda M, Koyota S, ''et al.'' |title=Molecular cloning and characterization of a human beta-Gal-3'-sulfotransferase that acts on both type 1 and type 2 (Gal beta 1-3/1-4GlcNAc-R) oligosaccharides. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 267-74 |year= 2001 |pmid= 11029462 |doi= 10.1074/jbc.M005666200 }}
*{{cite journal  |vauthors=Venter JC, Adams MD, Myers EW |title=The sequence of the human genome. |journal=Science |volume=291 |issue= 5507 |pages= 1304–51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 |display-authors=etal}}
*{{cite journal  | author=Venter JC, Adams MD, Myers EW, ''et al.'' |title=The sequence of the human genome. |journal=Science |volume=291 |issue= 5507 |pages= 1304-51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 }}
*{{cite journal  |vauthors=Suzuki A, Hiraoka N, Suzuki M |title=Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 24388–95 |year= 2001 |pmid= 11323440 |doi= 10.1074/jbc.M103135200 |display-authors=etal}}
*{{cite journal  | author=Suzuki A, Hiraoka N, Suzuki M, ''et al.'' |title=Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 24388-95 |year= 2001 |pmid= 11323440 |doi= 10.1074/jbc.M103135200 }}
*{{cite journal  |vauthors=Seko A, Hara-Kuge S, Yamashita K |title=Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1-->3galNAc residue in O-glycans. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 25697–704 |year= 2001 |pmid= 11333265 |doi= 10.1074/jbc.M101558200 }}
*{{cite journal  | author=Seko A, Hara-Kuge S, Yamashita K |title=Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1-->3galNAc residue in O-glycans. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 25697-704 |year= 2001 |pmid= 11333265 |doi= 10.1074/jbc.M101558200 }}
*{{cite journal  |vauthors=Ikeda N, Eguchi H, Nishihara S |title=A remodeling system of the 3'-sulfo-Lewis a and 3'-sulfo-Lewis x epitopes. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 38588–94 |year= 2001 |pmid= 11504739 |doi= 10.1074/jbc.M107390200 |display-authors=etal}}
*{{cite journal  | author=Ikeda N, Eguchi H, Nishihara S, ''et al.'' |title=A remodeling system of the 3'-sulfo-Lewis a and 3'-sulfo-Lewis x epitopes. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 38588-94 |year= 2001 |pmid= 11504739 |doi= 10.1074/jbc.M107390200 }}
*{{cite journal  |vauthors=Koma M, Miyagawa S, Honke K |title=The possibility of reducing xenoantigen levels with a novel gal 3'-sulfotransferase (GP3ST). |journal=J. Biochem. |volume=131 |issue= 4 |pages= 517–22 |year= 2002 |pmid= 11926988 |doi=  10.1093/oxfordjournals.jbchem.a003129|display-authors=etal}}
*{{cite journal  | author=Koma M, Miyagawa S, Honke K, ''et al.'' |title=The possibility of reducing xenoantigen levels with a novel gal 3'-sulfotransferase (GP3ST). |journal=J. Biochem. |volume=131 |issue= 4 |pages= 517-22 |year= 2002 |pmid= 11926988 |doi=  }}
*{{cite journal  |vauthors=Seko A, Nagata K, Yonezawa S, Yamashita K |title=Down-regulation of Gal 3-O-sulfotransferase-2 (Gal3ST-2) expression in human colonic non-mucinous adenocarcinoma. |journal=Jpn. J. Cancer Res. |volume=93 |issue= 5 |pages= 507–15 |year= 2003 |pmid= 12036446 |doi=  10.1111/j.1349-7006.2002.tb01285.x}}
*{{cite journal  | author=Seko A, Nagata K, Yonezawa S, Yamashita K |title=Down-regulation of Gal 3-O-sulfotransferase-2 (Gal3ST-2) expression in human colonic non-mucinous adenocarcinoma. |journal=Jpn. J. Cancer Res. |volume=93 |issue= 5 |pages= 507-15 |year= 2003 |pmid= 12036446 |doi=  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal}}
*{{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=Chandrasekaran EV, Lakhaman SS, Chawda R |title=Identification of physiologically relevant substrates for cloned Gal: 3-O-sulfotransferases (Gal3STs): distinct high affinity of Gal3ST-2 and LS180 sulfotransferase for the globo H backbone, Gal3ST-3 for N-glycan multiterminal Galbeta1, 4GlcNAcbeta units and 6-sulfoGalbeta1, 4GlcNAcbeta, and Gal3ST-4 for the mucin core-2 trisaccharide. |journal=J. Biol. Chem. |volume=279 |issue= 11 |pages= 10032–41 |year= 2004 |pmid= 14701868 |doi= 10.1074/jbc.M311989200 |display-authors=etal}}
*{{cite journal  | author=Chandrasekaran EV, Lakhaman SS, Chawda R, ''et al.'' |title=Identification of physiologically relevant substrates for cloned Gal: 3-O-sulfotransferases (Gal3STs): distinct high affinity of Gal3ST-2 and LS180 sulfotransferase for the globo H backbone, Gal3ST-3 for N-glycan multiterminal Galbeta1, 4GlcNAcbeta units and 6-sulfoGalbeta1, 4GlcNAcbeta, and Gal3ST-4 for the mucin core-2 trisaccharide. |journal=J. Biol. Chem. |volume=279 |issue= 11 |pages= 10032-41 |year= 2004 |pmid= 14701868 |doi= 10.1074/jbc.M311989200 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Shi BZ, Hu P, Geng F |title=Gal3ST-2 involved in tumor metastasis process by regulation of adhesion ability to selectins and expression of integrins. |journal=Biochem. Biophys. Res. Commun. |volume=332 |issue= 4 |pages= 934–40 |year= 2005 |pmid= 15921657 |doi= 10.1016/j.bbrc.2005.05.040 |display-authors=etal}}
*{{cite journal  | author=Shi BZ, Hu P, Geng F, ''et al.'' |title=Gal3ST-2 involved in tumor metastasis process by regulation of adhesion ability to selectins and expression of integrins. |journal=Biochem. Biophys. Res. Commun. |volume=332 |issue= 4 |pages= 934-40 |year= 2005 |pmid= 15921657 |doi= 10.1016/j.bbrc.2005.05.040 }}
*{{cite journal  |vauthors=Seko A, Sumiya J, Yamashita K |title=Porcine, mouse and human galactose 3-O-sulphotransferase-2 enzymes have different substrate specificities; the porcine enzyme requires basic compounds for its catalytic activity. |journal=Biochem. J. |volume=391 |issue= Pt 1 |pages= 77–85 |year= 2006 |pmid= 15926885 |doi= 10.1042/BJ20050362 | pmc=1237141 }}
*{{cite journal  | author=Seko A, Sumiya J, Yamashita K |title=Porcine, mouse and human galactose 3-O-sulphotransferase-2 enzymes have different substrate specificities; the porcine enzyme requires basic compounds for its catalytic activity. |journal=Biochem. J. |volume=391 |issue= Pt 1 |pages= 77-85 |year= 2006 |pmid= 15926885 |doi= 10.1042/BJ20050362 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 08:37, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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Wikidata
View/Edit Human

Galactose-3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the GAL3ST2 gene.[1][2]

This gene encodes a member of the galactose-3-O-sulfotransferase protein family. The product of this gene catalyzes sulfonation by transferring a sulfate group to the hydroxyl at C-3 of nonreducing beta-galactosyl residues, and it can act on both type 1 and type 2 (Galbeta 1-3/1-4GlcNAc-R) oligosaccharides with similar efficiencies, and on core 1 glycans. This enzyme has been implicated in tumor metastasis processes. This gene is different from the GAL3ST3 gene located on chromosome 11, which has also been referred to as GAL3ST2 and encodes a related enzyme with distinct tissue distribution and substrate specificities, compared to galactose-3-O-sulfotransferase 2.[2]

References

  1. ↑ Honke K, Tsuda M, Koyota S, Wada Y, Iida-Tanaka N, Ishizuka I, Nakayama J, Taniguchi N (Feb 2001). "Molecular cloning and characterization of a human beta-Gal-3'-sulfotransferase that acts on both type 1 and type 2 (Gal beta 1-3/1-4GlcNAc-R) oligosaccharides". J Biol Chem. 276 (1): 267–74. doi:10.1074/jbc.M005666200. PMID 11029462.
  2. ↑ 2.0 2.1 "Entrez Gene: GAL3ST2 galactose-3-O-sulfotransferase 2".

Further reading



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