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FUT8 (fucosyltransferase 8 (alpha (1,6) fucosyltransferase))

Written2010-08Hideyuki Ihara, Cong-xiao Gao, Yoshitaka Ikeda, Naoyuki Taniguchi
Division of Molecular Cell Biology, Department of Biomolecular Sciences, Saga University Faculty of Medicine, Saga, Japan (HI, YI); Department of Disease Glycomics, Institute of Scientific, Industrial Research, Osaka University, Osaka, Japan (CXG, NT); Disease Glycomics Team, Systems Glycobiology Research Group, Chemical Biology Department, Japan (NT)

(Note : for Links provided by Atlas : click)


Alias (NCBI)MGC26465
HGNC (Hugo) FUT8
HGNC Alias namealpha (1,6) fucosyltransferase
HGNC Previous namefucosyltransferase 8 (alpha (1,6) fucosyltransferase)
LocusID (NCBI) 2530
Atlas_Id 40649
Location 14q23.3  [Link to chromosome band 14q23]
Location_base_pair Starts at 65410592 and ends at 65744121 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping FUT8.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
ATG14 (14q22.3)::FUT8 (14q23.3)FUT8 (14q23.3)::AGBL4 (1p33)FUT8 (14q23.3)::CCDC85C (14q32.2)
FUT8 (14q23.3)::CTNNA1 (5q31.2)FUT8 (14q23.3)::FNTB (14q23.3)FUT8 (14q23.3)::IFT52 (20q13.12)
FUT8 (14q23.3)::NUMB (14q24.2)FUT8 (14q23.3)::SIPA1L1 (14q24.2)FUT8 (14q23.3)::TDRP (8p23.3)
IFRD1 (7q31.1)::FUT8 (14q23.3)


  Figure 1. Genomic organization of human FUT8 gene. Exons are represented by vertical bars. Exons denoted by ATG or TAA contain start and stop codons, respectively. These exons also have a part of the noncoding region.
Description Human FUT8 gene is located on chromosome 14q23.3 (Yamaguchi et al., 1999). This gene encompasses approximately 333 kb and contains nine exons with coding regions and three 5'-untranslated exons (Yamaguchi et al., 2000; Martinez-Duncker et al., 2004).
Transcription Some splicing variants of the 5'-untranslated region arise in a developmental stage-specific and tissue-specific manner (Martinez-Duncker et al., 2004). At least three different promoters appear to be functional in regulating the expression of the FUT8 gene. Three transcripts with different 5'-untranslated regions have been identified. With respect to coding region, four variants were reported to encode polypeptides containing 575, 446, 308 and 169 amino acid residues. The 575 residue protein is a fully active alpha1,6-fucosyltransferase, which was first of the variants to be identified. The other variants have not yet been examined for enzymatic activity and biological function. The 308 amino acid variant is known to be expressed in the retina (Yamaguchi et al., 2000).


  Figure 2. Protein structure of FUT8. CT and TM denote the cytoplasmic tail and the transmembrane domain, respectively. I, II and III represent the conserved motifs in alpha1,2-, alpha1,6- and protein O-fucosyltransferases.
Description FUT8 was purified and cloned as a cDNA from porcine brain and a human gastric cancer cell line (Uozumi et al., 1996, Yanagidani et al., 1997). Human FUT8 is comprised of 575 amino acids, with a calculated molecular weight of 66516. FUT8 contains no N-glycosylation sites. This enzyme belongs to the GT23 family of the CaZY classification. The structual analysis of a transmembrane domain-truncated form of FUT8 showed that the enzyme consists of a catalytic domain, an N-terminal coiled-coil domain and a C-terminal SH3 domain (Ihara et al., 2007). The catalytic domain was structurally classfied as a member of the GT-B group of glycosylatransferases.
Expression FUT8 gene is widely expressed in human tissues (Martinez-Duncker et al., 2004). The FUT8 gene is expressed at relatively high levels in the brain, placenta, lung, stomach, small intestine and jejunum, while pancreas, uterus, kidney and urinary bladder exhibit moderate expression. The FUT8 gene is weakly expressed in the heart, ileum, colon and spleen. On the other hand, the expression is not detectable in the normal liver (Miyoshi et al., 1997).
Localisation FUT8 is a typical type II membrane protein and is localized in the Golgi apparatus.
  Figure 3. The reaction catalysed by FUT8.
Function FUT8 catalyzes the transfer of a fucose residue from GDP-fucose to the reducing terminal GlcNAc of Asn-linked oligosaccharide (N-glycan) via an alpha1.6-linkage (Figure 3). The resulting fucosyl residue is often refered to as a core fucose. The reaction does not require any divalent cations or cofactors. The deletion of the FUT8 gene in mice leads to severe phenotypes that exhibit growth retardation, lung emphysema and death during postnatal development (Wang et al., 2005). As has been clearly shown in studies using knockout mice, the lack of core fucosylation resulted in the biological activities of various proteins to be perturbed (Taniguchi et al., 2006; Takahashi et al., 2009). Examples of this include the TGF-beta1 receptor (Wang et al., 2005), EGF receptor (Wang et al., 2006), VEGF receptor-2 (Wang et al., 2009), LRP-1 (Lee et al., 2006), E-cadherin (Osumi et al., 2009), alpha3beta1 integrin (Zhao et al., 2006), VCAM and alpha4beta1 integrin (Li et al., 2008). The binding affinity of the core fucose-deleted TGF-beta receptor to TGF-beta 1 is diminished in fut8-null mice, resulting in the downregulation of TGF-beta 1 signaling (Wang et al., 2005). The unusual overexpression of matrix metalloproteinases such as MMP-12 and MMP-13 is associated with the impaired receptor function, and has been proposed to cause the lung-destructive phenotypes. The EGF receptor in fut8 null mice is also affected in terms of its binding affinity to EGF and EGF-induced phoshorylation (Wang et al., 2006). These studies strongly suggest that FUT8 and core fucose structures regulate the receptor function.
In addition, core fucosylation was reported to be involved in antibodydependent cellular cytotoxicity (ADCC) (Shields et al., 2002; Shinkawa et al., 2003). The lack of core fucose of N-glycan in the Fc region of the IgG1 molecule enhances ADCC activity up to 50-100-fold. This discorvery promises to be useful in the development of antibody therapy in cancer treatment.
Homology The sequence identities between human FUT8 and other organisms are as follows :
Chimpangee (100%), Dog (97.7%), Cow (97.5%), Pig (95.6%), Rat (96.6%), Mouse (96.5%), Chicken (93.9%), Clawed frog (90.3%), Zebrafish (79.5%), Takifugu (80.2%), Tetraodon (79.8%), Sea squirt (23.2%), Fruit fly (43.7%), C. elegans (34.8%).
Eight cysteine residues in the catalytic domain are conserved among these species, except for ciona (Ihara et al., 2007).
FUT8 contains three short regions that are highly conserved in FUT8, alpha1,2-, bacterial alpha1,6-, and protein O-fucosyltransferases (Oriol et al., 1999; Takahashi et al., 2000a; Chazalet et al., 2001; Martinez-Duncker et al., 2003). The structual analysis has shown that these regions are located adjacent to one another in the Rossmann fold of FUT8 (Ihara et al., 2007). In addition, the C-terminal SH3 domain of FUT8 is structually similar to the typical SH3 domain that is found in many proteins.


Note One frame-shit mutation and 4 substitution mutants have been identified to date in various SNPs of the FUT8 gene. The frame shift mutant is due to the insertion of a T at position 2 of the codon for Val-85, resulting in 85-VLEEQLVK-92 being change to 85-VFRRAACter-92. The four substitution mutants are K101Q, L153V, E181G and T267K. These mutants are due to A being substituted by C at position 1 of codon 101, C to G at position 1 of codon 153, A to G at position 2 of codon 181, and C to A at posision 2 of codon 267, respectively. Effects of these substitutions on enzymatic activity are not currently known.

Implicated in

Entity Hepatocellular carcinoma (HCC)
Note It is well known that the core fucosylation of alpha-fetoprotein (AFP) is implicated in the development of HCC. AFP is a major fetal plasma protein, and its expression is elevated in hepatic diseases such as HCC, hepatitis and liver cirrhosis (Alpert et al., 1968; Ruoslahti et al., 1974). The AFP-L3 fraction was identified as the core-fucosylated isoform of AFP. The elevation in serum and liver tissue was found to be specific to HCC, but was not observed in other liver diseases (Taketa, 1990; Aoyagi, 1995; Miyoshi et al., 1999).
Thus, it appears that AFP-L3 could be used as a marker for HCC. The FUT8 gene is not expressed in the normal adult liver, but is highly expressed in HCC tissue. Surprisingly, however, such an elevation was also observed in liver cirrhosis in spite of the absence of a concomitant increase in AFP-L3 levels (Noda et al., 1998). This discrepancy can be attributed to the difference in the synthesis of GDP-fucose, a glycosyl donor substrate for fucosyltransferases, including FUT8, and by the altered intracellular sorting of fucosylated glycoproteins in hepatic cells. Because the intracellular concentration of GDP-fucose is higher in HCC, as compared to a normal liver, chronic hepatitis and liver cirrhosis, this increase would be expected to facilitate core fucosyltion of AFP (Noda et al., 2003). Core fucosylation appears to serve as a sorting signal for a glycoprotein to be directed to the bile, as revealed by the predominant distribution of fucosylated glycoproteins in bile rather than serum (Nakagawa et al., 2006). In fact, the levels of alpha-antitrypsin and alpha1-acid glycoprotein, both of which are fucosylated glycoproteins, are quite low in the bile of Fut8-null mice. The loss of polarity in cancer cells is likely to impair the regulated sorting, thus allowing abnormal secretion into the serum.
Prognosis AFP-L3-positive HCC patients were reported to show a poor prognosis (Yamashita et al., 1996).
Entity Ovarian cancer
Note FUT8 activity and mRNA levels are highly and specifically elavated in cases of ovarian serous adenocarcinoma, as compared to nomal ovary and other types of epithelial ovarian carcinoma (Takahashi et al., 2000b). In addition, core fucosylation levels in glycoproteins is also significantlly increased in cases of serous adenocarcinoma tissues.
Entity Thyroid cancer
Note The overexpression of FUT8 occurs in 33.3% of cases of papillary carcinoma of the thyroid (Ito et al., 2003), although FUT8 was not expressed in normal follicular cells. This overexpression was also shown to be correlated with tumor size and lymph node metastasis. These phenomena were not observed in cases of follicular carcinoma and anaplastic carcinoma.
Entity Pancreatic cancer
Note Haptoglobin was identified as a highly fucosylated glycoprotein in the serum of patients with pancreatic cancer (Okuyama et al., 2006). The increment of fucosylated haptoglobin was observed in pancreatic cancer rather than other diseases such as HCC, liver cirrhosis, gastric cancer and colon cancer, and also appeared to be correlated with the clinical stage. Structural analyses using lectin blotting and mass spectrometry showed that core fucosylation as well as alpha1,3/4-fucosylation is increased in haptoglobin from the serum of such patients. In addition, it was shown that interleukin 6 expressed in pancreatic cancer is a possible inducing factor for increasing the production of fucosylated haptoglobin in the liver (Narisada et al., 2008).
Entity Colorectal cancer
Note The enzymatic activity and protein expression of FUT8 were increased in tumor tissues of human colorectal carcinoma, but not in healthy tissues (Muinelo-Romay et al., 2008). This increment was well observed in cases of male, polypoid growth, no regional lymph node metastasis and early clinical stage. In addition, immunohistochemical examination has demonstrated that FUT8 is expressed at higher levels in tumor tissues of colorectal carcinoma than in healthy and transitional tissues.
Entity Cystic fibrosis
Note Fucosylation is known to be increased in cystic fibrosis. The alpha1,6-fucosylation of a membrane glycoprotein is elevated in cystic fibrosis fibroblast (Wang et al., 1990).


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PMID 4171303
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PMID 7496131
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Ihara H, Ikeda Y, Toma S, Wang X, Suzuki T, Gu J, Miyoshi E, Tsukihara T, Honke K, Matsumoto A, Nakagawa A, Taniguchi N.
Glycobiology. 2007 May;17(5):455-66. Epub 2006 Dec 15.
PMID 17172260
Expression of alpha1,6-fucosyltransferase (FUT8) in papillary carcinoma of the thyroid: its linkage to biological aggressiveness and anaplastic transformation.
Ito Y, Miyauchi A, Yoshida H, Uruno T, Nakano K, Takamura Y, Miya A, Kobayashi K, Yokozawa T, Matsuzuka F, Taniguchi N, Matsuura N, Kuma K, Miyoshi E.
Cancer Lett. 2003 Oct 28;200(2):167-72.
PMID 14568171
Loss of core fucosylation of low-density lipoprotein receptor-related protein-1 impairs its function, leading to the upregulation of serum levels of insulin-like growth factor-binding protein 3 in Fut8-/- mice.
Lee SH, Takahashi M, Honke K, Miyoshi E, Osumi D, Sakiyama H, Ekuni A, Wang X, Inoue S, Gu J, Kadomatsu K, Taniguchi N.
J Biochem. 2006 Mar;139(3):391-8.
PMID 16567404
Reduced alpha4beta1 integrin/VCAM-1 interactions lead to impaired pre-B cell repopulation in alpha 1,6-fucosyltransferase deficient mice.
Li W, Ishihara K, Yokota T, Nakagawa T, Koyama N, Jin J, Mizuno-Horikawa Y, Wang X, Miyoshi E, Taniguchi N, Kondo A.
Glycobiology. 2008 Jan;18(1):114-24. Epub 2007 Oct 2.
PMID 17913729
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PMID 14514715
The alpha1-6-fucosyltransferase gene and its biological significance.
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PMID 10580126
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PMID 9378548
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PMID 18491404
Fucosylation of N-glycans regulates the secretion of hepatic glycoproteins into bile ducts.
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J Biol Chem. 2006 Oct 6;281(40):29797-806. Epub 2006 Aug 9.
PMID 16899455
Identification of an inducible factor secreted by pancreatic cancer cell lines that stimulates the production of fucosylated haptoglobin in hepatoma cells.
Narisada M, Kawamoto S, Kuwamoto K, Moriwaki K, Nakagawa T, Matsumoto H, Asahi M, Koyama N, Miyoshi E.
Biochem Biophys Res Commun. 2008 Dec 19;377(3):792-6. Epub 2008 Oct 23.
PMID 18951869
Relationship between elevated FX expression and increased production of GDP-L-fucose, a common donor substrate for fucosylation in human hepatocellular carcinoma and hepatoma cell lines.
Noda K, Miyoshi E, Gu J, Gao CX, Nakahara S, Kitada T, Honke K, Suzuki K, Yoshihara H, Yoshikawa K, Kawano K, Tonetti M, Kasahara A, Hori M, Hayashi N, Taniguchi N.
Cancer Res. 2003 Oct 1;63(19):6282-9.
PMID 14559815
Fucosylated haptoglobin is a novel marker for pancreatic cancer: a detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation.
Okuyama N, Ide Y, Nakano M, Nakagawa T, Yamanaka K, Moriwaki K, Murata K, Ohigashi H, Yokoyama S, Eguchi H, Ishikawa O, Ito T, Kato M, Kasahara A, Kawano S, Gu J, Taniguchi N, Miyoshi E.
Int J Cancer. 2006 Jun 1;118(11):2803-8.
PMID 16385567
Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria.
Oriol R, Mollicone R, Cailleau A, Balanzino L, Breton C.
Glycobiology. 1999 Apr;9(4):323-34. (REVIEW)
PMID 10089206
Core fucosylation of E-cadherin enhances cell-cell adhesion in human colon carcinoma WiDr cells.
Osumi D, Takahashi M, Miyoshi E, Yokoe S, Lee SH, Noda K, Nakamori S, Gu J, Ikeda Y, Kuroki Y, Sengoku K, Ishikawa M, Taniguchi N.
Cancer Sci. 2009 May;100(5):888-95. Epub 2009 Mar 11.
PMID 19302290
Serum alpha-fetoprotein: diagnostic significance in liver disease.
Ruoslahti E, Salaspuro M, Pihko H, Andersson L, Seppala M.
Br Med J. 1974 Jun 8;2(5918):527-9.
PMID 4407283
Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity.
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J Biol Chem. 2002 Jul 26;277(30):26733-40. Epub 2002 May 1.
PMID 11986321
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PMID 12427744
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PMID 19508951
A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues.
Takahashi T, Ikeda Y, Tateishi A, Yamaguchi Y, Ishikawa M, Taniguchi N.
Glycobiology. 2000a May;10(5):503-10.
PMID 10764839
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Taketa K.
Hepatology. 1990 Dec;12(6):1420-32. (REVIEW)
PMID 1701754
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PMID 16971114
Purification and cDNA cloning of porcine brain GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1-->6fucosyltransferase.
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PMID 8910378
Requirement of Fut8 for the expression of vascular endothelial growth factor receptor-2: a new mechanism for the emphysema-like changes observed in Fut8-deficient mice.
Wang X, Fukuda T, Li W, Gao CX, Kondo A, Matsumoto A, Miyoshi E, Taniguchi N, Gu J.
J Biochem. 2009 May;145(5):643-51. Epub 2009 Jan 29.
PMID 19179362
Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling.
Wang X, Gu J, Ihara H, Miyoshi E, Honke K, Taniguchi N.
J Biol Chem. 2006 Feb 3;281(5):2572-7. Epub 2005 Nov 29.
PMID 16316986
Dysregulation of TGF-beta1 receptor activation leads to abnormal lung development and emphysema-like phenotype in core fucose-deficient mice.
Wang X, Inoue S, Gu J, Miyoshi E, Noda K, Li W, Mizuno-Horikawa Y, Nakano M, Asahi M, Takahashi M, Uozumi N, Ihara S, Lee SH, Ikeda Y, Yamaguchi Y, Aze Y, Tomiyama Y, Fujii J, Suzuki K, Kondo A, Shapiro SD, Lopez-Otin C, Kuwaki T, Okabe M, Honke K, Taniguchi N.
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PMID 16236725
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Clin Chim Acta. 1990 May;188(3):193-210.
PMID 2387072
Genomic structure and promoter analysis of the human alpha1, 6-fucosyltransferase gene (FUT8).
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PMID 8831594
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PMID 9133635
Deletion of core fucosylation on alpha3beta1 integrin down-regulates its functions.
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J Biol Chem. 2006 Dec 15;281(50):38343-50. Epub 2006 Oct 16.
PMID 17043354


This paper should be referenced as such :
Ihara, H ; Gao, CX ; Ikeda, Y ; Taniguchi, N
FUT8 (fucosyltransferase 8 (alpha (1,6) fucosyltransferase))
Atlas Genet Cytogenet Oncol Haematol. 2011;15(5):410-414.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)FUT8   4019
Atlas Explorer : (Salamanque)FUT8
Entrez_Gene (NCBI)FUT8    fucosyltransferase 8
AliasesCDGF; CDGF1
GeneCards (Weizmann)FUT8
Ensembl hg19 (Hinxton)ENSG00000033170 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000033170 [Gene_View]  ENSG00000033170 [Sequence]  chr14:65410592-65744121 [Contig_View]  FUT8 [Vega]
ICGC DataPortalENSG00000033170
TCGA cBioPortalFUT8
AceView (NCBI)FUT8
Genatlas (Paris)FUT8
SOURCE (Princeton)FUT8
Genetics Home Reference (NIH)FUT8
Genomic and cartography
GoldenPath hg38 (UCSC)FUT8  -     chr14:65410592-65744121 +  14q23.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FUT8  -     14q23.3   [Description]    (hg19-Feb_2009)
GoldenPathFUT8 - 14q23.3 [CytoView hg19]  FUT8 - 14q23.3 [CytoView hg38]
Genome Data Viewer NCBIFUT8 [Mapview hg19]  
OMIM602589   618005   
Gene and transcription
Genbank (Entrez)AB049740 AF052088 AJ514324 AJ514325 AJ536053
RefSeq transcript (Entrez)NM_001371533 NM_001371534 NM_001371536 NM_004480 NM_178154 NM_178155 NM_178156 NM_178157
Consensus coding sequences : CCDS (NCBI)FUT8
Gene ExpressionFUT8 [ NCBI-GEO ]   FUT8 [ EBI - ARRAY_EXPRESS ]   FUT8 [ SEEK ]   FUT8 [ MEM ]
Gene Expression Viewer (FireBrowse)FUT8 [ Firebrowse - Broad ]
GenevisibleExpression of FUT8 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2530
GTEX Portal (Tissue expression)FUT8
Human Protein AtlasENSG00000033170-FUT8 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9BYC5   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9BYC5  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9BYC5
Catalytic activity : Enzyme2.4.1.68 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)GT23 (PS51659)    SH3 (PS50002)   
Domains : Interpro (EBI)Fut8    Fut8_SH3    GT23_dom    SH3-like_dom_sf    SH3_domain   
Domain families : Pfam (Sanger)SH3_9 (PF14604)   
Domain families : Pfam (NCBI)pfam14604   
Domain families : Smart (EMBL)SH3 (SM00326)  
Conserved Domain (NCBI)FUT8
PDB (RSDB)2DE0    6VLD    6VLE    6X5H    6X5R    6X5S    6X5T    6X5U   
PDB Europe2DE0    6VLD    6VLE    6X5H    6X5R    6X5S    6X5T    6X5U   
PDB (PDBSum)2DE0    6VLD    6VLE    6X5H    6X5R    6X5S    6X5T    6X5U   
PDB (IMB)2DE0    6VLD    6VLE    6X5H    6X5R    6X5S    6X5T    6X5U   
Structural Biology KnowledgeBase2DE0    6VLD    6VLE    6X5H    6X5R    6X5S    6X5T    6X5U   
SCOP (Structural Classification of Proteins)2DE0    6VLD    6VLE    6X5H    6X5R    6X5S    6X5T    6X5U   
CATH (Classification of proteins structures)2DE0    6VLD    6VLE    6X5H    6X5R    6X5S    6X5T    6X5U   
AlphaFold pdb e-kbQ9BYC5   
Human Protein Atlas [tissue]ENSG00000033170-FUT8 [tissue]
Protein Interaction databases
IntAct (EBI)Q9BYC5
Ontologies - Pathways
Ontology : AmiGOGolgi membrane  in utero embryonic development  protein binding  Golgi apparatus  protein N-linked glycosylation  N-glycan processing  transforming growth factor beta receptor signaling pathway  integrin-mediated signaling pathway  respiratory gaseous exchange by respiratory system  glycoprotein 6-alpha-L-fucosyltransferase activity  glycoprotein 6-alpha-L-fucosyltransferase activity  oligosaccharide biosynthetic process  regulation of gene expression  membrane  integral component of membrane  cell migration  SH3 domain binding  protein N-linked glycosylation via asparagine  viral protein processing  Golgi cisterna membrane  protein glycosylation in Golgi  N-glycan fucosylation  L-fucose catabolic process  receptor metabolic process  GDP-L-fucose metabolic process  alpha-(1->6)-fucosyltransferase activity  extracellular exosome  regulation of cellular response to oxidative stress  
Ontology : EGO-EBIGolgi membrane  in utero embryonic development  protein binding  Golgi apparatus  protein N-linked glycosylation  N-glycan processing  transforming growth factor beta receptor signaling pathway  integrin-mediated signaling pathway  respiratory gaseous exchange by respiratory system  glycoprotein 6-alpha-L-fucosyltransferase activity  glycoprotein 6-alpha-L-fucosyltransferase activity  oligosaccharide biosynthetic process  regulation of gene expression  membrane  integral component of membrane  cell migration  SH3 domain binding  protein N-linked glycosylation via asparagine  viral protein processing  Golgi cisterna membrane  protein glycosylation in Golgi  N-glycan fucosylation  L-fucose catabolic process  receptor metabolic process  GDP-L-fucose metabolic process  alpha-(1->6)-fucosyltransferase activity  extracellular exosome  regulation of cellular response to oxidative stress  
REACTOMEQ9BYC5 [protein]
REACTOME PathwaysR-HSA-975578 [pathway]   
NDEx NetworkFUT8
Atlas of Cancer Signalling NetworkFUT8
Wikipedia pathwaysFUT8
Orthology - Evolution
GeneTree (enSembl)ENSG00000033170
Phylogenetic Trees/Animal Genes : TreeFamFUT8
Homologs : HomoloGeneFUT8
Homology/Alignments : Family Browser (UCSC)FUT8
Gene fusions - Rearrangements
Fusion : MitelmanATG14::FUT8 [14q22.3/14q23.3]  
Fusion : MitelmanFUT8::AGBL4 [14q23.3/1p33]  
Fusion : MitelmanFUT8::CCDC85C [14q23.3/14q32.2]  
Fusion : MitelmanFUT8::FNTB [14q23.3/14q23.3]  
Fusion : MitelmanFUT8::SIPA1L1 [14q23.3/14q24.2]  
Fusion : FusionHubABCA5--FUT8    ARIH2--FUT8    ATG14--FUT8    CERS6--FUT8    CGRRF1--FUT8    CNTNAP4--FUT8    DDX26B--FUT8    FAM13C--FUT8    FUT8--AGBL4    FUT8--AL139022.1   
FUT8--CCDC85C    FUT8--CDK12    FUT8--CEP290    FUT8--CHURC1-FNTB    FUT8--CTNNA1    FUT8--DMXL1    FUT8--DSTN    FUT8--ERO1L    FUT8--FBXO33    FUT8--FNTB   
FUT8--IFT52    FUT8--IKZF1    FUT8--KCNH5    FUT8--LRRFIP2    FUT8--NUMB    FUT8--RAD51B    FUT8--RP11-762H8.4    FUT8--SIPA1L1    FUT8--SLC11A2    FUT8--SRPK2   
FUT8--STK3    FUT8--UTY    FUT8--YLPM1    FUT8--ZNF224    IFRD1--FUT8    MLK4--FUT8    MOK--FUT8    PAPOLA--FUT8    PPP1R13B--FUT8    PRKCH--FUT8   
TG--FUT8    ZBTB38--FUT8   
Fusion : QuiverFUT8
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFUT8 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)FUT8
Exome Variant ServerFUT8
GNOMAD BrowserENSG00000033170
Varsome BrowserFUT8
ACMGFUT8 variants
Genomic Variants (DGV)FUT8 [DGVbeta]
DECIPHERFUT8 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisFUT8 
ICGC Data PortalFUT8 
TCGA Data PortalFUT8 
Broad Tumor PortalFUT8
OASIS PortalFUT8 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICFUT8  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DFUT8
Mutations and Diseases : HGMDFUT8
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)FUT8
DoCM (Curated mutations)FUT8
CIViC (Clinical Interpretations of Variants in Cancer)FUT8
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM602589    618005   
Genetic Testing Registry FUT8
NextProtQ9BYC5 [Medical]
Target ValidationFUT8
Huge Navigator FUT8 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDFUT8
Pharm GKB GenePA28435
Clinical trialFUT8
DataMed IndexFUT8
PubMed104 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Thu Jan 20 14:07:52 CET 2022

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