FUT5: Difference between revisions

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'''Alpha-(1,3)-fucosyltransferase''' is an [[enzyme]] that in humans is encoded by the ''FUT5'' [[gene]].<ref name="pmid1740457">{{cite journal |vauthors=Weston BW, Nair RP, Larsen RD, Lowe JB | title = Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities | journal = J Biol Chem | volume = 267 | issue = 6 | pages = 4152–60 |date=Mar 1992 | pmid = 1740457 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FUT5 fucosyltransferase 5 (alpha (1,3) fucosyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2527| accessdate = }}</ref>
'''Alpha-(1,3)-fucosyltransferase''' is an [[enzyme]] that in humans is encoded by the ''FUT5'' [[gene]].<ref name="pmid1740457">{{cite journal | vauthors = Weston BW, Nair RP, Larsen RD, Lowe JB | title = Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities | journal = The Journal of Biological Chemistry | volume = 267 | issue = 6 | pages = 4152–60 | date = February 1992 | pmid = 1740457 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FUT5 fucosyltransferase 5 (alpha (1,3) fucosyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2527| accessdate = }}</ref>


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== References ==
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==References==
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==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Chiu PC, Chung MK, Koistinen R, Koistinen H, Seppala M, Ho PC, Ng EH, Lee KF, Yeung WS | title = Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding | journal = Journal of Cell Science | volume = 120 | issue = Pt 1 | pages = 33–44 | date = January 2007 | pmid = 17148576 | doi = 10.1242/jcs.03258 }}
| citations =
* {{cite journal | vauthors = Inaba Y, Ohyama C, Kato T, Satoh M, Saito H, Hagisawa S, Takahashi T, Endoh M, Fukuda MN, Arai Y, Fukuda M | title = Gene transfer of alpha1,3-fucosyltransferase increases tumor growth of the PC-3 human prostate cancer cell line through enhanced adhesion to prostatic stromal cells | journal = International Journal of Cancer | volume = 107 | issue = 6 | pages = 949–57 | date = December 2003 | pmid = 14601054 | doi = 10.1002/ijc.11513 }}
*{{cite journal |vauthors=Chiu PC, Chung MK, Koistinen R |title=Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding. |journal=J. Cell Sci. |volume=120 |issue= Pt 1 |pages= 33–44 |year= 2007 |pmid= 17148576 |doi= 10.1242/jcs.03258 |display-authors=etal}}
* {{cite journal | vauthors = Roos C, Kolmer M, Mattila P, Renkonen R | title = Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism | journal = The Journal of Biological Chemistry | volume = 277 | issue = 5 | pages = 3168–75 | date = February 2002 | pmid = 11698403 | doi = 10.1074/jbc.M107927200 }}
*{{cite journal |vauthors=Inaba Y, Ohyama C, Kato T |title=Gene transfer of alpha1,3-fucosyltransferase increases tumor growth of the PC-3 human prostate cancer cell line through enhanced adhesion to prostatic stromal cells. |journal=Int. J. Cancer |volume=107 |issue= 6 |pages= 949–57 |year= 2004 |pmid= 14601054 |doi= 10.1002/ijc.11513 |display-authors=etal}}
* {{cite journal | vauthors = Nishihara S, Iwasaki H, Kaneko M, Tawada A, Ito M, Narimatsu H | 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 Letters | volume = 462 | issue = 3 | pages = 289–94 | date = December 1999 | pmid = 10622713 | doi = 10.1016/S0014-5793(99)01549-5 }}
*{{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 | vauthors = McCurley RS, Recinos A, Olsen AS, Gingrich JC, Szczepaniak D, Cameron HS, Krauss R, Weston BW | title = Physical maps of human alpha (1,3)fucosyltransferase genes FUT3-FUT6 on chromosomes 19p13.3 and 11q21 | journal = Genomics | volume = 26 | issue = 1 | pages = 142–6 | date = March 1995 | pmid = 7782074 | doi = 10.1016/0888-7543(95)80094-3 }}
*{{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 | vauthors = Cameron HS, Szczepaniak D, Weston BW | title = Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms | journal = The Journal of Biological Chemistry | volume = 270 | issue = 34 | pages = 20112–22 | date = August 1995 | pmid = 7650030 | doi = 10.1074/jbc.270.34.20112 }}
*{{cite journal |vauthors=McCurley RS, Recinos A, Olsen AS |title=Physical maps of human alpha (1,3)fucosyltransferase genes FUT3-FUT6 on chromosomes 19p13.3 and 11q21. |journal=Genomics |volume=26 |issue= 1 |pages= 142–6 |year= 1995 |pmid= 7782074 |doi=10.1016/0888-7543(95)80094-3 |display-authors=etal}}
* {{cite journal | vauthors = Weston BW, Smith PL, Kelly RJ, Lowe JB | title = Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes | journal = The Journal of Biological Chemistry | volume = 267 | issue = 34 | pages = 24575–84 | date = December 1992 | pmid = 1339443 | doi =  }}
*{{cite journal |vauthors=Cameron HS, Szczepaniak D, Weston BW |title=Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20112–22 |year= 1995 |pmid= 7650030 |doi=10.1074/jbc.270.34.20112 }}
*{{cite journal |vauthors=Weston BW, Smith PL, Kelly RJ, Lowe JB |title=Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24575–84 |year= 1992 |pmid= 1339443 |doi=  }}
}}
{{refend}}
{{refend}}


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Latest revision as of 05:38, 15 February 2018

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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
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Wikidata
View/Edit Human

Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT5 gene.[1][2]

References

  1. ↑ Weston BW, Nair RP, Larsen RD, Lowe JB (February 1992). "Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities". The Journal of Biological Chemistry. 267 (6): 4152–60. PMID 1740457.
  2. ↑ "Entrez Gene: FUT5 fucosyltransferase 5 (alpha (1,3) fucosyltransferase)".

Further reading

  • Chiu PC, Chung MK, Koistinen R, Koistinen H, Seppala M, Ho PC, Ng EH, Lee KF, Yeung WS (January 2007). "Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding". Journal of Cell Science. 120 (Pt 1): 33–44. doi:10.1242/jcs.03258. PMID 17148576.
  • Inaba Y, Ohyama C, Kato T, Satoh M, Saito H, Hagisawa S, Takahashi T, Endoh M, Fukuda MN, Arai Y, Fukuda M (December 2003). "Gene transfer of alpha1,3-fucosyltransferase increases tumor growth of the PC-3 human prostate cancer cell line through enhanced adhesion to prostatic stromal cells". International Journal of Cancer. 107 (6): 949–57. doi:10.1002/ijc.11513. PMID 14601054.
  • Roos C, Kolmer M, Mattila P, Renkonen R (February 2002). "Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism". The Journal of Biological Chemistry. 277 (5): 3168–75. doi:10.1074/jbc.M107927200. PMID 11698403.
  • Nishihara S, Iwasaki H, Kaneko M, Tawada A, Ito M, Narimatsu H (December 1999). "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 Letters. 462 (3): 289–94. doi:10.1016/S0014-5793(99)01549-5. PMID 10622713.
  • McCurley RS, Recinos A, Olsen AS, Gingrich JC, Szczepaniak D, Cameron HS, Krauss R, Weston BW (March 1995). "Physical maps of human alpha (1,3)fucosyltransferase genes FUT3-FUT6 on chromosomes 19p13.3 and 11q21". Genomics. 26 (1): 142–6. doi:10.1016/0888-7543(95)80094-3. PMID 7782074.
  • Cameron HS, Szczepaniak D, Weston BW (August 1995). "Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms". The Journal of Biological Chemistry. 270 (34): 20112–22. doi:10.1074/jbc.270.34.20112. PMID 7650030.
  • Weston BW, Smith PL, Kelly RJ, Lowe JB (December 1992). "Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes". The Journal of Biological Chemistry. 267 (34): 24575–84. PMID 1339443.
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