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FUT5 - Wikipedia, the free encyclopedia

FUT5

From Wikipedia, the free encyclopedia


Fucosyltransferase 5 (alpha (1,3) fucosyltransferase)
Identifiers
Symbol(s) FUT5; FUC-TV
External IDs OMIM: 136835 HomoloGene74416
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 2527 n/a
Ensembl ENSG00000130383 n/a
Uniprot Q11128 n/a
Refseq NM_002034 (mRNA)
NP_002025 (protein)
n/a (mRNA)
n/a (protein)
Location Chr 19: 5.82 - 5.82 Mb n/a
Pubmed search [1] n/a

Fucosyltransferase 5 (alpha (1,3) fucosyltransferase), also known as FUT5, is a human gene.[1]


[edit] References

[edit] Further reading

  • Chiu PC, Chung MK, Koistinen R, et al. (2007). "Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding.". J. Cell. Sci. 120 (Pt 1): 33–44. doi:10.1242/jcs.03258. PMID 17148576. 
  • Inaba Y, Ohyama C, Kato T, et al. (2004). "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.". Int. J. Cancer 107 (6): 949–57. doi:10.1002/ijc.11513. PMID 14601054. 
  • 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. 
  • 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. PMID 10622713. 
  • McCurley RS, Recinos A, Olsen AS, et al. (1995). "Physical maps of human alpha (1,3)fucosyltransferase genes FUT3-FUT6 on chromosomes 19p13.3 and 11q21.". Genomics 26 (1): 142–6. PMID 7782074. 
  • Cameron HS, Szczepaniak D, Weston BW (1995). "Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms.". J. Biol. Chem. 270 (34): 20112–22. PMID 7650030. 
  • Weston BW, Nair RP, Larsen RD, Lowe JB (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.". J. Biol. Chem. 267 (6): 4152–60. PMID 1740457. 
  • Weston BW, Smith PL, Kelly RJ, Lowe JB (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.". J. Biol. Chem. 267 (34): 24575–84. PMID 1339443. 


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