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    FUT9 fucosyltransferase 9 [ Homo sapiens (human) ]

    Gene ID: 10690, updated on 10-Dec-2024

    Summary

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    Official Symbol
    FUT9provided by HGNC
    Official Full Name
    fucosyltransferase 9provided by HGNC
    Primary source
    HGNC:HGNC:4020
    See related
    Ensembl:ENSG00000172461 MIM:606865; AllianceGenome:HGNC:4020
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    Fuc-TIX
    Summary
    The protein encoded by this gene belongs to the glycosyltransferase family. It is localized to the golgi, and catalyzes the last step in the biosynthesis of Lewis X (LeX) antigen, the addition of a fucose to precursor polysaccharides. This protein is one of the few fucosyltransferases that synthesizes the LeX oligosaccharide (CD15) expressed in the organ buds progressing in mesenchyma during embryogenesis. It is also responsible for the expression of CD15 in mature granulocytes. A common haplotype of this gene has also been associated with susceptibility to placental malaria infection. [provided by RefSeq, Nov 2011]
    Expression
    Biased expression in brain (RPKM 9.0), stomach (RPKM 7.9) and 2 other tissues See more
    Orthologs
    mouse all
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    Genomic context

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    See FUT9 in Genome Data Viewer
    Location:
    6q16.1
    Exon count:
    6
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 6 NC_000006.12 (96015974..96215612)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 6 NC_060930.1 (97186913..97387800)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 6 NC_000006.11 (96463850..96663488)

    Chromosome 6 - NC_000006.12Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC107986543 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 17407 Neighboring gene OCT4-NANOG hESC enhancer GRCh37_chr6:96250823-96251589 Neighboring gene uncharacterized LOC107986626 Neighboring gene P300/CBP strongly-dependent group 1 enhancer GRCh37_chr6:96425470-96426669 Neighboring gene uncharacterized LOC105377905 Neighboring gene keratin 18 pseudogene 50 Neighboring gene UFL1 antisense RNA 1 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 24840 Neighboring gene RNA, 7SL, cytoplasmic 797, pseudogene Neighboring gene ATAC-STARR-seq lymphoblastoid active region 24841 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr6:96967525-96968398 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr6:96968399-96969270 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr6:96969271-96970142 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr6:96970143-96971014 Neighboring gene UFM1 specific ligase 1

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: Tissue-specific circular RNA induction during human fetal development
    • Description: 35 human fetal samples from 6 tissues (3 - 7 replicates per tissue) collected between 10 and 20 weeks gestational time were sequenced using Illumina TruSeq Stranded Total RNA
    • BioProject: PRJNA270632
    • Publication: PMID 26076956
    • Analysis date: Mon Apr 2 22:54:59 2018

    Bibliography

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    Related articles in PubMed

    1. Structural basis for Lewis antigen synthesis by the α1,3-fucosyltransferase FUT9. Kadirvelraj R, et al. Nat Chem Biol, 2023 Aug. PMID 37202521, Free PMC Article
    2. Assignment of the human alpha 1,3-fucosyltransferase IX gene (FUT9) to chromosome band 6q16 by in situ hybridization. Kaneko M, et al. Cytogenet Cell Genet, 1999. PMID 10575236
    3. FUT4 and FUT9 genes are expressed early in human embryogenesis. Cailleau-Thomas A, et al. Glycobiology, 2000 Aug. PMID 10929005
    4. [Regulation by ovarian hormones of alpha 1,3-fucosyltransferase gene (FUT9) expression in human endometrium]. Li H, et al. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai), 2002 Nov. PMID 12417923
    5. A variant in the gene FUT9 is associated with susceptibility to placental malaria infection. Sikora M, et al. Hum Mol Genet, 2009 Aug 15. PMID 19460885

    See all (35) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. ELF4 contributes to esophageal squamous cell carcinoma growth and metastasis by augmenting cancer stemness via FUT9.
      Title: ELF4 contributes to esophageal squamous cell carcinoma growth and metastasis by augmenting cancer stemness via FUT9.
    2. FUT9 silencing decreases the expression of the colorectal cancer TIC marker CD44 and the level of the OCT4 transcription factor, which is known to support cancer stemness.
      Title: An integrated computational and experimental study uncovers FUT9 as a metabolic driver of colorectal cancer.
    3. N-glycosylation of human alpha1,3-fucosyltransferase IX is required for enzyme stability and activity.
      Title: N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity.
    4. FUT9 plays a significant role during human, but not mouse, E-selectin-mediated cell adhesion.
      Title: Silencing α1,3-fucosyltransferases in human leukocytes reveals a role for FUT9 enzyme during E-selectin-mediated cell adhesion.
    5. Downregulation of fucosyltransferase 9 leads to decreased Lewis(x) levels and impaired neurite outgrowth.
      Title: Expression of glycogenes in differentiating human NT2N neurons. Downregulation of fucosyltransferase 9 leads to decreased Lewis(x) levels and impaired neurite outgrowth.
    6. Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)
      Title: Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    7. A single nucleotide polymorphism in FUT9, rs3811070, was significantly associated with placental malaria infection.
      Title: A variant in the gene FUT9 is associated with susceptibility to placental malaria infection.
    8. FUT9 was found to be a trans-Golgi and trans-Golgi network (TGN) glycosyltransferase from confocal immunofluorescence co-localization with the markers of the secretory pathway beta4-galactosyltransferase (trans-Golgi and TGN) and TGN-46 (TGN)
      Title: Human fucosyltransferase IX: specificity towards N-linked glycoproteins and relevance of the cytoplasmic domain in intra-Golgi localization.
    9. FUTIX plays a key role in the synthesis of Lex groups of CEACAM1
      Title: CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues.
    10. Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor- and site-specificity profile
      Title: Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor- and site-specificity profile.
    Submit: New GeneRIF Correction

    Phenotypes

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    Find tests for this gene in the NIH Genetic Testing Registry (GTR)

    Review eQTL and phenotype association data in this region using PheGenI

    EBI GWAS Catalog

    Description
    Biological insights from 108 schizophrenia-associated genetic loci.
    EBI GWAS Catalog

    Variation

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    See variants in ClinVar

    See studies and variants in dbVar

    See Variation Viewer (GRCh37.p13)

    See Variation Viewer (GRCh38)

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables alpha-(1->3)-fucosyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables alpha-(1->3)-fucosyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables alpha-(1->3)-fucosyltransferase activity TAS
    Traceable Author Statement
    more info
    		 PubMed 
    enables fucosyltransferase activity TAS
    Traceable Author Statement
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in L-fucose catabolic process NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in Lewis x epitope biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in N-glycan fucosylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in carbohydrate metabolic process TAS
    Traceable Author Statement
    more info
    		 PubMed 
    involved_in fucosylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in fucosylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in glycosphingolipid biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in neuron differentiation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in neuronal stem cell division IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in oligosaccharide biosynthetic process TAS
    Traceable Author Statement
    more info
    		  
    involved_in polysaccharide biosynthetic process ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in positive regulation of neuron projection development IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein N-linked glycosylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein O-linked glycosylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein glycosylation TAS
    Traceable Author Statement
    more info
    		 PubMed 
    involved_in regulation of leukocyte cell-cell adhesion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of leukocyte tethering or rolling IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in Golgi apparatus TAS
    Traceable Author Statement
    more info
    		 PubMed 
    located_in Golgi membrane TAS
    Traceable Author Statement
    more info
    		  
    located_in trans-Golgi network IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in trans-Golgi network membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
    Names
    alpha-(1,3)-fucosyltransferase 9
    fucT-IX
    fucosyltransferase 9 (alpha (1,3) fucosyltransferase)
    fucosyltransferase IX
    galactoside 3-L-fucosyltransferase
    NP_006572.2
    XP_011533687.1
    XP_016865677.1
    XP_016865679.1
    XP_047274044.1
    XP_047274045.1
    XP_054210029.1
    XP_054210030.1
    XP_054210031.1
    XP_054210032.1
    XP_054210033.1
    XP_054210034.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_006581.4 → NP_006572.2  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9

      See identical proteins and their annotated locations for NP_006572.2

      Status: REVIEWED

      Source sequence(s)
      AL512406, BC036101, CK299829, CK904220
      Consensus CDS
      CCDS5033.1
      UniProtKB/Swiss-Prot
      Q5T0W4, Q9Y231
      Related
      ENSP00000302599.4, ENST00000302103.6
      Conserved Domains (2) summary
      pfam00852
      Location:185 → 354
      Glyco_transf_10; Glycosyltransferase family 10 (fucosyltransferase) C-term
      pfam17039
      Location:62 → 169
      Glyco_tran_10_N; Fucosyltransferase, N-terminal

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000006.12 Reference GRCh38.p14 Primary Assembly

      Range
      96015974..96215612
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_047418089.1 → XP_047274045.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/Swiss-Prot
      Q5T0W4, Q9Y231

    2. XM_047418088.1 → XP_047274044.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/Swiss-Prot
      Q5T0W4, Q9Y231

    3. XM_017010190.2 → XP_016865679.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/Swiss-Prot
      Q5T0W4, Q9Y231
      Conserved Domains (2) summary
      pfam00852
      Location:185 → 354
      Glyco_transf_10; Glycosyltransferase family 10 (fucosyltransferase) C-term
      pfam17039
      Location:62 → 169
      Glyco_tran_10_N; Fucosyltransferase, N-terminal

    4. XM_011535385.3 → XP_011533687.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      See identical proteins and their annotated locations for XP_011533687.1

      UniProtKB/Swiss-Prot
      Q5T0W4, Q9Y231
      Conserved Domains (2) summary
      pfam00852
      Location:185 → 354
      Glyco_transf_10; Glycosyltransferase family 10 (fucosyltransferase) C-term
      pfam17039
      Location:62 → 169
      Glyco_tran_10_N; Fucosyltransferase, N-terminal

    5. XM_017010188.2 → XP_016865677.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/Swiss-Prot
      Q5T0W4, Q9Y231
      Conserved Domains (2) summary
      pfam00852
      Location:185 → 354
      Glyco_transf_10; Glycosyltransferase family 10 (fucosyltransferase) C-term
      pfam17039
      Location:62 → 169
      Glyco_tran_10_N; Fucosyltransferase, N-terminal

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060930.1 Alternate T2T-CHM13v2.0

      Range
      97186913..97387800
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_054354058.1 → XP_054210033.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/TrEMBL
      Q5Q0U2

    2. XM_054354056.1 → XP_054210031.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/TrEMBL
      Q5Q0U2

    3. XM_054354059.1 → XP_054210034.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/TrEMBL
      Q5Q0U2

    4. XM_054354057.1 → XP_054210032.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/TrEMBL
      Q5Q0U2

    5. XM_054354054.1 → XP_054210029.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/TrEMBL
      Q5Q0U2

    6. XM_054354055.1 → XP_054210030.1  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 isoform X1

      UniProtKB/TrEMBL
      Q5Q0U2
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q9Y231.2 GenPept UniProtKB/Swiss-Prot:Q9Y231

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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