FUT9: Difference between revisions

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{{Infobox_gene}}
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'''Alpha-(1,3)-fucosyltransferase''' is an [[enzyme]] that in humans is encoded by the ''FUT9'' [[gene]].<ref name="pmid10386598">{{cite journal |vauthors=Kaneko M, Kudo T, Iwasaki H, Ikehara Y, Nishihara S, Nakagawa S, Sasaki K, Shiina T, Inoko H, Saitou N, Narimatsu H | title = Alpha1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX | journal = FEBS Lett | volume = 452 | issue = 3 | pages = 237–42 |date=Jul 1999 | pmid = 10386598 | pmc = | doi =10.1016/S0014-5793(99)00640-7  }}</ref><ref name="pmid10575236">{{cite journal |vauthors=Kaneko M, Kudo T, Iwasaki H, Shiina T, Inoko H, Kozaki T, Saitou N, Narimatsu H | title = Assignment of the human alpha 1,3-fucosyltransferase IX gene (FUT9) to chromosome band 6q16 by in situ hybridization | journal = Cytogenet Cell Genet | volume = 86 | issue = 3–4 | pages = 329–30 |date=Jan 2000 | pmid = 10575236 | pmc =  | doi =10.1159/000015329 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10690| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Fucosyltransferase 9 (alpha (1,3) fucosyltransferase)
| HGNCid = 4020
| Symbol = FUT9
| AltSymbols =; Fuc-TIX
| OMIM = 606865
| ECnumber =
| Homologene = 4800
| MGIid = 1330859
| GeneAtlas_image1 = PBB_GE_FUT9_207696_at_tn.png
| Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0046920 |text = alpha(1,3)-fucosyltransferase 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:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}} {{GNF_GO|id=GO:0042355 |text = L-fucose catabolic process}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10690
    | Hs_Ensembl = ENSG00000172461
    | Hs_RefseqProtein = NP_006572
    | Hs_RefseqmRNA = NM_006581
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 96570590
    | Hs_GenLoc_end = 96760477
    | Hs_Uniprot = Q9Y231
    | Mm_EntrezGene = 14348
    | Mm_Ensembl = ENSMUSG00000055373
    | Mm_RefseqmRNA = NM_010243
    | Mm_RefseqProtein = NP_034373
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 25699963
    | Mm_GenLoc_end = 25890633
    | Mm_Uniprot = Q14AE3
  }}
}}
'''Fucosyltransferase 9 (alpha (1,3) fucosyltransferase)''', also known as '''FUT9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10690| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = FUT9 is one of several alpha-3-fucosyltransferases that can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides. FUT9 synthesizes the LeX oligosaccharide (CD15), which is expressed in organ buds progressing in mesenchyma during human embryogenesis.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10690| accessdate = }}</ref>
| summary_text = FUT9 is one of several alpha-3-fucosyltransferases that can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides. FUT9 synthesizes the LeX oligosaccharide (CD15), which is expressed in organ buds progressing in mesenchyma during human embryogenesis.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10690| 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=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal  |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal  | author=Kaneko M, Kudo T, Iwasaki H, ''et al.'' |title=Alpha1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX. |journal=FEBS Lett. |volume=452 |issue= 3 |pages= 237-42 |year= 1999 |pmid= 10386598 |doi=  }}
*{{cite journal  |vauthors=Nishihara S, Iwasaki H, Kaneko M |title=Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue |journal=FEBS Lett. |volume=462 |issue= 3 |pages= 289–94 |year= 2000 |pmid= 10622713 |doi=10.1016/S0014-5793(99)01549-5 |display-authors=etal}}
*{{cite journal  | author=Kaneko M, Kudo T, Iwasaki H, ''et al.'' |title=Assignment of the human alpha 1,3-fucosyltransferase IX gene (FUT9) to chromosome band 6q16 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=86 |issue= 3-4 |pages= 329-30 |year= 2000 |pmid= 10575236 |doi= }}
*{{cite journal  |vauthors=Cailleau-Thomas A, Coullin P, Candelier JJ |title=FUT4 and FUT9 genes are expressed early in human embryogenesis |journal=Glycobiology |volume=10 |issue= 8 |pages= 789–802 |year= 2000 |pmid= 10929005 |doi=10.1093/glycob/10.8.789 |display-authors=etal}}
*{{cite journal  | author=Nishihara S, Iwasaki H, Kaneko M, ''et al.'' |title=Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue. |journal=FEBS Lett. |volume=462 |issue= 3 |pages= 289-94 |year= 2000 |pmid= 10622713 |doi=  }}
*{{cite journal  |vauthors=Nakayama F, Nishihara S, Iwasaki H |title=CD15 expression in mature granulocytes is determined by alpha 1,3-fucosyltransferase IX, but in promyelocytes and monocytes by alpha 1,3-fucosyltransferase IV |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 16100–6 |year= 2001 |pmid= 11278338 |doi= 10.1074/jbc.M007272200 |display-authors=etal}}
*{{cite journal  | author=Cailleau-Thomas A, Coullin P, Candelier JJ, ''et al.'' |title=FUT4 and FUT9 genes are expressed early in human embryogenesis. |journal=Glycobiology |volume=10 |issue= 8 |pages= 789-802 |year= 2000 |pmid= 10929005 |doi=  }}
*{{cite journal  |vauthors=Roos C, Kolmer M, Mattila P, Renkonen R |title=Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3168–75 |year= 2002 |pmid= 11698403 |doi= 10.1074/jbc.M107927200 }}
*{{cite journal  | author=Nakayama F, Nishihara S, Iwasaki H, ''et al.'' |title=CD15 expression in mature granulocytes is determined by alpha 1,3-fucosyltransferase IX, but in promyelocytes and monocytes by alpha 1,3-fucosyltransferase IV. |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 16100-6 |year= 2001 |pmid= 11278338 |doi= 10.1074/jbc.M007272200 }}
*{{cite journal  |vauthors=Toivonen S, Nishihara S, Narimatsu H |title=Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor- and site-specificity profile |journal=Glycobiology |volume=12 |issue= 6 |pages= 361–8 |year= 2003 |pmid= 12107078 |doi=10.1093/glycob/12.6.361 |display-authors=etal}}
*{{cite journal  | author=Roos C, Kolmer M, Mattila P, Renkonen R |title=Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3168-75 |year= 2002 |pmid= 11698403 |doi= 10.1074/jbc.M107927200 }}
*{{cite journal  |vauthors=Li H, Kong Y, Yan B |title=[Regulation by ovarian hormones of alpha 1,3-fucosyltransferase gene (FUT9) expression in human endometrium] |journal=Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao |volume=34 |issue= 6 |pages= 775–9 |year= 2003 |pmid= 12417923 |doi=  }}
*{{cite journal  | author=Toivonen S, Nishihara S, Narimatsu H, ''et al.'' |title=Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor- and site-specificity profile. |journal=Glycobiology |volume=12 |issue= 6 |pages= 361-8 |year= 2003 |pmid= 12107078 |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=Li H, Kong Y, Yan B |title=[Regulation by ovarian hormones of alpha 1,3-fucosyltransferase gene (FUT9) expression in human endometrium] |journal=Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao |volume=34 |issue= 6 |pages= 775-9 |year= 2003 |pmid= 12417923 |doi=  }}
*{{cite journal  |vauthors=Nishihara S, Iwasaki H, Nakajima K |title=Alpha1,3-fucosyltransferase IX (Fut9) determines Lewis X expression in brain |journal=Glycobiology |volume=13 |issue= 6 |pages= 445–55 |year= 2004 |pmid= 12626397 |doi= 10.1093/glycob/cwg048 |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=Mungall AJ, Palmer SA, Sims SK |title=The DNA sequence and analysis of human chromosome 6 |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 |display-authors=etal}}
*{{cite journal  | author=Nishihara S, Iwasaki H, Nakajima K, ''et al.'' |title=Alpha1,3-fucosyltransferase IX (Fut9) determines Lewis X expression in brain. |journal=Glycobiology |volume=13 |issue= 6 |pages= 445-55 |year= 2004 |pmid= 12626397 |doi= 10.1093/glycob/cwg048 }}
*{{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=Mungall AJ, Palmer SA, Sims SK, ''et al.'' |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805-11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 }}
*{{cite journal  |vauthors=Bogoevska V, Horst A, Klampe B |title=CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues |journal=Glycobiology |volume=16 |issue= 3 |pages= 197–209 |year= 2006 |pmid= 16282604 |doi= 10.1093/glycob/cwj057 |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  | author=Bogoevska V, Horst A, Klampe B, ''et al.'' |title=CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues. |journal=Glycobiology |volume=16 |issue= 3 |pages= 197-209 |year= 2006 |pmid= 16282604 |doi= 10.1093/glycob/cwj057 }}
}}
}}
{{refend}}
{{refend}}


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{{Glycosyltransferases}}
 
 
{{gene-6-stub}}

Latest revision as of 04:59, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT9 gene.[1][2][3]

FUT9 is one of several alpha-3-fucosyltransferases that can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides. FUT9 synthesizes the LeX oligosaccharide (CD15), which is expressed in organ buds progressing in mesenchyma during human embryogenesis.[supplied by OMIM][3]

References

  1. ↑ Kaneko M, Kudo T, Iwasaki H, Ikehara Y, Nishihara S, Nakagawa S, Sasaki K, Shiina T, Inoko H, Saitou N, Narimatsu H (Jul 1999). "Alpha1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX". FEBS Lett. 452 (3): 237–42. doi:10.1016/S0014-5793(99)00640-7. PMID 10386598.
  2. ↑ Kaneko M, Kudo T, Iwasaki H, Shiina T, Inoko H, Kozaki T, Saitou N, Narimatsu H (Jan 2000). "Assignment of the human alpha 1,3-fucosyltransferase IX gene (FUT9) to chromosome band 6q16 by in situ hybridization". Cytogenet Cell Genet. 86 (3–4): 329–30. doi:10.1159/000015329. PMID 10575236.
  3. ↑ 3.0 3.1 "Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase)".

Further reading



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