FUT5

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FUT5
Identifiers
AliasesFUT5, FUC-TV, fucosyltransferase 5
External IDsHomoloGene: 134030 GeneCards: FUT5
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for FUT5
Genomic location for FUT5
Band19p13.3Start5,865,826 bp[1]
End5,870,540 bp[1]
RNA expression pattern
PBB GE FUT3 211882 x at fs.png

PBB GE FUT5 211225 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002034

n/a

RefSeq (protein)

NP_002025

n/a

Location (UCSC)Chr 19: 5.87 – 5.87 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT5 gene.[3][4]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000130383 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". 
  3. ^ 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. 
  4. ^ "Entrez Gene: FUT5 fucosyltransferase 5 (alpha (1,3) fucosyltransferase)". 

Further reading[edit]

  • 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.