FUT5

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Fucosyltransferase 5 (alpha (1,3) fucosyltransferase)
Identifiers
Symbols FUT5 ; FUC-TV
External IDs OMIM136835 HomoloGene34780 ChEMBL: 3146 GeneCards: FUT5 Gene
EC number 2.4.1.65
RNA expression pattern
PBB GE FUT5 211225 at tn.png
PBB GE FUT3 211882 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2527 n/a
Ensembl ENSG00000130383 n/a
UniProt Q11128 n/a
RefSeq (mRNA) NM_002034.2 n/a
RefSeq (protein) NP_002025.2 n/a
Location (UCSC) Chr 19:
5.87 – 5.9 Mb
n/a
PubMed search [1] n/a

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


References[edit]

  1. ^ Weston BW, Nair RP, Larsen RD, Lowe JB (Mar 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. 
  2. ^ "Entrez Gene: FUT5 fucosyltransferase 5 (alpha (1,3) fucosyltransferase)". 

Further reading[edit]

  • 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. doi:10.1016/S0014-5793(99)01549-5. 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. doi:10.1016/0888-7543(95)80094-3. 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. doi:10.1074/jbc.270.34.20112. PMID 7650030. 
  • 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.