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{{Infobox_gene}}
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'''Alpha-(1,6)-fucosyltransferase''' is an [[enzyme]] that in humans is encoded by the ''FUT8'' [[gene]].<ref name="pmid9368041">{{cite journal |vauthors=Costache M, Apoil PA, Cailleau A, Elmgren A, Larson G, Henry S, Blancher A, Iordachescu D, Oriol R, Mollicone R | title = Evolution of fucosyltransferase genes in vertebrates | journal = J Biol Chem | volume = 272 | issue = 47 | pages = 29721–8 |date=Dec 1997 | pmid = 9368041 | pmc =  | doi =10.1074/jbc.272.47.29721 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FUT8 fucosyltransferase 8 (alpha (1,6) fucosyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2530| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_FUT8_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2de0.
| PDB = {{PDB2|2de0}}
| Name = Fucosyltransferase 8 (alpha (1,6) fucosyltransferase)
| HGNCid = 4019
| Symbol = FUT8
| AltSymbols =; MGC26465
| OMIM = 602589
| ECnumber = 
| Homologene = 9650
| MGIid = 1858901
| GeneAtlas_image1 = PBB_GE_FUT8_203988_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008424 |text = glycoprotein 6-alpha-L-fucosyltransferase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| 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:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0006491 |text = N-glycan processing}} {{GNF_GO|id=GO:0007179 |text = transforming growth factor beta receptor signaling pathway}} {{GNF_GO|id=GO:0007585 |text = respiratory gaseous exchange}} {{GNF_GO|id=GO:0009312 |text = oligosaccharide biosynthetic process}} {{GNF_GO|id=GO:0042355 |text = L-fucose catabolic process}} {{GNF_GO|id=GO:0043112 |text = receptor metabolic process}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2530
    | Hs_Ensembl = ENSG00000033170
    | Hs_RefseqProtein = NP_004471
    | Hs_RefseqmRNA = NM_004480
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 64947063
    | Hs_GenLoc_end = 65279714
    | Hs_Uniprot = Q9BYC5
    | Mm_EntrezGene = 53618
    | Mm_Ensembl = ENSMUSG00000021065
    | Mm_RefseqmRNA = NM_016893
    | Mm_RefseqProtein = NP_058589
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 78156965
    | Mm_GenLoc_end = 78394827
    | Mm_Uniprot = Q3UYN7
  }}
}}
'''Fucosyltransferase 8 (alpha (1,6) fucosyltransferase)''', also known as '''FUT8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FUT8 fucosyltransferase 8 (alpha (1,6) fucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2530| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This enzyme belongs to the family of fucosyltransferases. The product of this gene catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha1-3, and alpha1-4 fucose addition. The expression of this gene may contribute to the malignancy of cancer cells and to their invasive and metastatic capabilities. Alternatively spliced variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: FUT8 fucosyltransferase 8 (alpha (1,6) fucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2530| accessdate = }}</ref>
| summary_text = This enzyme belongs to the family of fucosyltransferases. The product of this gene catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha1-3, and alpha1-4 fucose addition. The expression of this gene may contribute to the malignancy of cancer cells and to their invasive and metastatic capabilities. Alternatively spliced variants encoding different isoforms have been identified.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Miyoshi E, Noda K, Yamaguchi Y, ''et al.'' |title=The alpha1-6-fucosyltransferase gene and its biological significance. |journal=Biochim. Biophys. Acta |volume=1473 |issue= 1 |pages= 9-20 |year= 2000 |pmid= 10580126 |doi=  }}
*{{cite journal  |vauthors=Miyoshi E, Noda K, Yamaguchi Y |title=The alpha1-6-fucosyltransferase gene and its biological significance. |journal=Biochim. Biophys. Acta |volume=1473 |issue= 1 |pages= 9–20 |year= 2000 |pmid= 10580126 |doi=  10.1016/s0304-4165(99)00166-x|display-authors=etal}}
*{{cite journal  | author=Kalyanaraman VS, Rodriguez V, Veronese F, ''et al.'' |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371-80 |year= 1990 |pmid= 2187500 |doi= }}
*{{cite journal  |vauthors=Kalyanaraman VS, Rodriguez V, Veronese F |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371–80 |year= 1990 |pmid= 2187500 |doi=10.1089/aid.1990.6.371  |display-authors=etal}}
*{{cite journal  | author=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384-8 |year= 1989 |pmid= 2541446 |doi=  }}
*{{cite journal  |vauthors=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384–8 |year= 1989 |pmid= 2541446 |doi=10.1073/pnas.86.9.3384 | pmc=287137  }}
*{{cite journal  | author=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452-6 |year= 1989 |pmid= 2542563 |doi=  }}
*{{cite journal  |vauthors=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452–6 |year= 1989 |pmid= 2542563 |doi= | pmc=250699 }}
*{{cite journal  | author=Kozarsky K, Penman M, Basiripour L, ''et al.'' |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163-9 |year= 1989 |pmid= 2649653 |doi=  }}
*{{cite journal  |vauthors=Kozarsky K, Penman M, Basiripour L |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163–9 |year= 1989 |pmid= 2649653 |doi=  |display-authors=etal}}
*{{cite journal  | author=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265-82 |year= 1988 |pmid= 2829950 |doi=  }}
*{{cite journal  |vauthors=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265–82 |year= 1988 |pmid= 2829950 |doi=10.1089/aid.1987.3.265 }}
*{{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=Andersson B, Wentland MA, Ricafrente JY |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 |display-authors=etal}}
*{{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=Yu W, Andersson B, Worley KC |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  |display-authors=etal}}
*{{cite journal  | author=Yanagidani S, Uozumi N, Ihara Y, ''et al.'' |title=Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells. |journal=J. Biochem. |volume=121 |issue= 3 |pages= 626-32 |year= 1997 |pmid= 9133635 |doi=  }}
*{{cite journal  |vauthors=Yanagidani S, Uozumi N, Ihara Y |title=Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells. |journal=J. Biochem. |volume=121 |issue= 3 |pages= 626–32 |year= 1997 |pmid= 9133635 |doi=  10.1093/oxfordjournals.jbchem.a021631|display-authors=etal}}
*{{cite journal  | author=Costache M, Apoil PA, Cailleau A, ''et al.'' |title=Evolution of fucosyltransferase genes in vertebrates. |journal=J. Biol. Chem. |volume=272 |issue= 47 |pages= 29721-8 |year= 1997 |pmid= 9368041 |doi=  }}
*{{cite journal  |vauthors=Yamaguchi Y, Fujii J, Inoue S |title=Mapping of the alpha-1,6-fucosyltransferase gene, FUT8, to human chromosome 14q24.3. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1–2 |pages= 58–60 |year= 1999 |pmid= 10343104 |doi=10.1159/000015215 |display-authors=etal}}
*{{cite journal  | author=Yamaguchi Y, Fujii J, Inoue S, ''et al.'' |title=Mapping of the alpha-1,6-fucosyltransferase gene, FUT8, to human chromosome 14q24.3. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 58-60 |year= 1999 |pmid= 10343104 |doi= }}
*{{cite journal  |vauthors=Takahashi T, Ikeda Y, Tateishi A |title=A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues. |journal=Glycobiology |volume=10 |issue= 5 |pages= 503–10 |year= 2000 |pmid= 10764839 |doi=10.1093/glycob/10.5.503  |display-authors=etal}}
*{{cite journal  | author=Takahashi T, Ikeda Y, Tateishi A, ''et al.'' |title=A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues. |journal=Glycobiology |volume=10 |issue= 5 |pages= 503-10 |year= 2000 |pmid= 10764839 |doi=  }}
*{{cite journal  |vauthors=Yamaguchi Y, Ikeda Y, Takahashi T |title=Genomic structure and promoter analysis of the human alpha1, 6-fucosyltransferase gene (FUT8). |journal=Glycobiology |volume=10 |issue= 6 |pages= 637–43 |year= 2000 |pmid= 10814706 |doi=10.1093/glycob/10.6.637 |display-authors=etal}}
*{{cite journal  | author=Yamaguchi Y, Ikeda Y, Takahashi T, ''et al.'' |title=Genomic structure and promoter analysis of the human alpha1, 6-fucosyltransferase gene (FUT8). |journal=Glycobiology |volume=10 |issue= 6 |pages= 637-43 |year= 2000 |pmid= 10814706 |doi= }}
*{{cite journal  |vauthors=Takahashi T, Ikeda Y, Miyoshi E |title=alpha1,6fucosyltransferase is highly and specifically expressed in human ovarian serous adenocarcinomas. |journal=Int. J. Cancer |volume=88 |issue= 6 |pages= 914–9 |year= 2000 |pmid= 11093814 |doi=10.1002/1097-0215(20001215)88:6<914::AID-IJC12>3.0.CO;2-1  |display-authors=etal}}
*{{cite journal  | author=Takahashi T, Ikeda Y, Miyoshi E, ''et al.'' |title=alpha1,6fucosyltransferase is highly and specifically expressed in human ovarian serous adenocarcinomas. |journal=Int. J. Cancer |volume=88 |issue= 6 |pages= 914-9 |year= 2000 |pmid= 11093814 |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=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=Coullin P, Crooijmans RP, Groenen MA |title=Assignment of FUT8 to chicken chromosome band 5q1.4 and to human chromosome 14q23.2→q24.1 by in situ hybridization. Conserved and compared synteny between human and chicken. |journal=Cytogenet. Genome Res. |volume=97 |issue= 3–4 |pages= 234–8 |year= 2003 |pmid= 12438718 |doi=10.1159/000066611  |display-authors=etal}}
*{{cite journal  | author=Coullin P, Crooijmans RP, Groenen MA, ''et al.'' |title=Assignment of FUT8 to chicken chromosome band 5q1.4 and to human chromosome 14q23.2-->q24.1 by in situ hybridization. Conserved and compared synteny between human and chicken. |journal=Cytogenet. Genome Res. |volume=97 |issue= 3-4 |pages= 234-8 |year= 2003 |pmid= 12438718 |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=Martinez-Duncker I, Michalski JC, Bauvy C |title=Activity and tissue distribution of splice variants of alpha6-fucosyltransferase in human embryogenesis. |journal=Glycobiology |volume=14 |issue= 1 |pages= 13–25 |year= 2004 |pmid= 14514715 |doi= 10.1093/glycob/cwh006 |display-authors=etal}}
*{{cite journal  | author=Martinez-Duncker I, Michalski JC, Bauvy C, ''et al.'' |title=Activity and tissue distribution of splice variants of alpha6-fucosyltransferase in human embryogenesis. |journal=Glycobiology |volume=14 |issue= 1 |pages= 13-25 |year= 2004 |pmid= 14514715 |doi= 10.1093/glycob/cwh006 }}
*{{cite journal  |vauthors=Ito Y, Miyauchi A, Yoshida H |title=Expression of alpha1,6-fucosyltransferase (FUT8) in papillary carcinoma of the thyroid: its linkage to biological aggressiveness and anaplastic transformation. |journal=Cancer Lett. |volume=200 |issue= 2 |pages= 167–72 |year= 2003 |pmid= 14568171 |doi=10.1016/S0304-3835(03)00383-5  |display-authors=etal}}
*{{cite journal  | author=Ito Y, Miyauchi A, Yoshida H, ''et al.'' |title=Expression of alpha1,6-fucosyltransferase (FUT8) in papillary carcinoma of the thyroid: its linkage to biological aggressiveness and anaplastic transformation. |journal=Cancer Lett. |volume=200 |issue= 2 |pages= 167-72 |year= 2003 |pmid= 14568171 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2530}}
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{{Glycosyltransferases}}


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{{gene-14-stub}}
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Revision as of 04:58, 31 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Alpha-(1,6)-fucosyltransferase is an enzyme that in humans is encoded by the FUT8 gene.[1][2]

This enzyme belongs to the family of fucosyltransferases. The product of this gene catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha1-3, and alpha1-4 fucose addition. The expression of this gene may contribute to the malignancy of cancer cells and to their invasive and metastatic capabilities. Alternatively spliced variants encoding different isoforms have been identified.[2]

References

  1. Costache M, Apoil PA, Cailleau A, Elmgren A, Larson G, Henry S, Blancher A, Iordachescu D, Oriol R, Mollicone R (Dec 1997). "Evolution of fucosyltransferase genes in vertebrates". J Biol Chem. 272 (47): 29721–8. doi:10.1074/jbc.272.47.29721. PMID 9368041.
  2. 2.0 2.1 "Entrez Gene: FUT8 fucosyltransferase 8 (alpha (1,6) fucosyltransferase)".

Further reading