FUT9: Difference between revisions

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Latest revision as of 04:59, 31 August 2017

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

↑ 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.
↑ 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.
↑ ^3.0 ^3.1 "Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase)".

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Nishihara S, Iwasaki H, Kaneko M, et al. (2000). "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". FEBS Lett. 462 (3): 289–94. doi:10.1016/S0014-5793(99)01549-5. PMID 10622713.
Cailleau-Thomas A, Coullin P, Candelier JJ, et al. (2000). "FUT4 and FUT9 genes are expressed early in human embryogenesis". Glycobiology. 10 (8): 789–802. doi:10.1093/glycob/10.8.789. PMID 10929005.
Nakayama F, Nishihara S, Iwasaki H, et al. (2001). "CD15 expression in mature granulocytes is determined by alpha 1,3-fucosyltransferase IX, but in promyelocytes and monocytes by alpha 1,3-fucosyltransferase IV". J. Biol. Chem. 276 (19): 16100–6. doi:10.1074/jbc.M007272200. PMID 11278338.
Roos C, Kolmer M, Mattila P, Renkonen R (2002). "Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism". J. Biol. Chem. 277 (5): 3168–75. doi:10.1074/jbc.M107927200. PMID 11698403.
Toivonen S, Nishihara S, Narimatsu H, et al. (2003). "Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor- and site-specificity profile". Glycobiology. 12 (6): 361–8. doi:10.1093/glycob/12.6.361. PMID 12107078.
Li H, Kong Y, Yan B (2003). "[Regulation by ovarian hormones of alpha 1,3-fucosyltransferase gene (FUT9) expression in human endometrium]". Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao. 34 (6): 775–9. PMID 12417923.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Nishihara S, Iwasaki H, Nakajima K, et al. (2004). "Alpha1,3-fucosyltransferase IX (Fut9) determines Lewis X expression in brain". Glycobiology. 13 (6): 445–55. doi:10.1093/glycob/cwg048. PMID 12626397.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Bogoevska V, Horst A, Klampe B, et al. (2006). "CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues". Glycobiology. 16 (3): 197–209. doi:10.1093/glycob/cwj057. PMID 16282604.

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

[pmid10386598-1] 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.

[pmid10575236-2] 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.

[entrez-3] 3.0 ^3.1 "Entrez Gene: FUT9 fucosyltransferase 9 (alpha (1,3) fucosyltransferase)".

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
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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>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | 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==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | 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}}
-{{protein-stub}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
-{{WikiDoc Sources}}
+{{PBB_Controls
+| update_page = yes
+| require_manual_inspection = no
+| update_protein_box = yes
+| update_summary = yes
+| update_citations = yes
+}}
+{{Glycosyltransferases}}
+{{gene-6-stub}}

FUT9: Difference between revisions

Latest revision as of 04:59, 31 August 2017

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