FUT5

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

FUT5
Identifiers
Aliases	FUT5, FUC-TV, fucosyltransferase 5
External IDs	OMIM: 136835; HomoloGene: 134030; GeneCards: FUT5; OMA:FUT5 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.3 Start 5,865,826 bp End 5,870,540 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow right lobe of liver anterior pituitary skin of leg testicle islet of Langerhans left testis right testis head skin of abdomen n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity alpha-(1->3)-fucosyltransferase activity 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity glycosyltransferase activity fucosyltransferase activity Cellular component integral component of membrane Golgi cisterna membrane Golgi apparatus membrane Golgi membrane Biological process protein glycosylation L-fucose catabolic process fucosylation ceramide metabolic process carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2527 n/a Ensembl ENSG00000130383 n/a UniProt Q11128 n/a RefSeq (mRNA) NM_002034 n/a RefSeq (protein) NP_002025 n/a Location (UCSC) Chr 19: 5.87 – 5.87 Mb n/a PubMed search n/a
Wikidata
View/Edit Human

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. hdl:10722/45488. 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. S2CID 7078688.
• 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. S2CID 37842289.
• 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. doi:10.1016/S0021-9258(18)35803-4. PMID 1339443.