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10 sources retrieved · Most recent: April 2026 · Index updated 14 days ago
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FUT8
fucosyltransferase 8
Chromosome 14 · 14q23.3
NCBI Gene: 2530Ensembl: ENSG00000033170.18HGNC: HGNC:4019UniProt: A8K8P8
127PubMed Papers
21Diseases
0Drugs
7Pathogenic Variants
CLINICAL
OMIM Disease Gene
DATA QUALITY
✓ Experimental GO Evidence✓ Swiss-Prot Reviewed
extracellular exosomeprotein N-linked glycosylationprotein bindingmembranecongenital disorder of glycosylation with defective fucosylationAbnormality of the skeletal systemgenetic disordergout
✦AI Summary

FUT8 (fucosyltransferase 8) is the sole enzyme responsible for catalyzing the addition of α1,6-fucose to the innermost GlcNAc residue of N-linked glycans, a modification known as core fucosylation 1. This glycosylation process is essential for protein stability and function across multiple physiological contexts. FUT8-mediated core fucosylation regulates critical cellular processes including immune responses, where it modulates checkpoint proteins like B7H3 and PD-L2, contributing to immune evasion in cancers 23. The enzyme also controls EGFR signaling through core fucosylation, affecting downstream pathways including JAK1-STAT3 activation 4. In reproductive biology, FUT8 is indispensable for follicular development by regulating FSH receptor function and granulosa cell-oocyte interactions 5. FUT8 is frequently upregulated in various cancers and plays roles in tumor progression, metastasis, and therapeutic resistance 1. Clinically, FUT8 deficiency causes congenital disorder of glycosylation with defective fucosylation, while its overexpression is associated with poor prognosis in multiple cancer types. Therapeutic targeting of FUT8 shows promise in combination therapies, particularly in enhancing anti-tumor immune responses and improving treatment efficacy.

Sources cited
1
FUT8 catalyzes addition of α1,6-fucose to innermost GlcNAc residue and is frequently upregulated in cancer
PMID: 33466384
2
FUT8 catalyzes B7H3 core fucosylation maintaining high expression and mediating immunosuppression in TNBC
PMID: 33976130
3
FUT8 is required for PD-L2 glycosylation and contributes to cetuximab therapy resistance
PMID: 34697216
4
FUT8 promotes EGFR core fucosylation and affects JAK1-STAT3-RIG-I signaling pathway
PMID: 38253527
5
FUT8 is essential for FSH receptor function and follicular development in female fertility
PMID: 38280716
Disease Associationsⓘ21
congenital disorder of glycosylation with defective fucosylationOpen Targets
0.79Strong
Abnormality of the skeletal systemOpen Targets
0.45Moderate
genetic disorderOpen Targets
0.41Moderate
goutOpen Targets
0.41Moderate
COVID-19Open Targets
0.38Weak
Intellectual disabilityOpen Targets
0.37Weak
SeizureOpen Targets
0.37Weak
myopathyOpen Targets
0.34Weak
bladder calculusOpen Targets
0.30Weak
Genu valgumOpen Targets
0.27Weak
Genu varumOpen Targets
0.26Weak
preeclampsiaOpen Targets
0.24Weak
placenta praeviaOpen Targets
0.18Weak
sprainOpen Targets
0.18Weak
cervical carcinomaOpen Targets
0.17Weak
glomerulonephritisOpen Targets
0.17Weak
adolescent idiopathic scoliosisOpen Targets
0.16Weak
autoimmune thyroid diseaseOpen Targets
0.16Weak
kidney diseaseOpen Targets
0.14Weak
breast cancerOpen Targets
0.10Weak
Congenital disorder of glycosylation with defective fucosylation 1UniProt
Pathogenic Variants7
NM_001371533.1(FUT8):c.715C>T (p.Arg239Ter)Pathogenic
Congenital disorder of glycosylation with defective fucosylation 1|not provided|Inborn genetic diseases|Malignant tumor of urinary bladder
★★☆☆2023→ Residue 239
NM_001371533.1(FUT8):c.786_789del (p.Ser263fs)Likely pathogenic
FUT8-related disorder
★☆☆☆2023→ Residue 263
NM_001371533.1(FUT8):c.952C>T (p.Arg318Ter)Likely pathogenic
Congenital disorder of glycosylation with defective fucosylation 1
★☆☆☆2022→ Residue 318
NM_001371533.1(FUT8):c.12G>A (p.Trp4Ter)Likely pathogenic
Congenital disorder of glycosylation with defective fucosylation 1
☆☆☆☆2020→ Residue 4
NM_001371533.1(FUT8):c.1009C>G (p.Arg337Gly)Pathogenic
Congenital disorder of glycosylation with defective fucosylation 1
☆☆☆☆2019→ Residue 337
NM_001371533.1(FUT8):c.1259+5G>TPathogenic
Congenital disorder of glycosylation with defective fucosylation 1
☆☆☆☆2019
NM_001371533.1(FUT8):c.943C>T (p.Arg315Ter)Pathogenic
Congenital disorder of glycosylation with defective fucosylation 1
☆☆☆☆2019→ Residue 315
View on ClinVar ↗
Related Genes
B4GALT1Protein interaction99%POFUT1Protein interaction99%MAN2A1Protein interaction98%MGAT3Protein interaction97%B4GALT2Protein interaction95%B4GALT3Protein interaction95%
Tissue Expression6 tissues
Brain
100%
Bone Marrow
40%
Ovary
37%
Heart
34%
Lung
27%
Liver
10%
Gene Interaction Network
Click a node to explore
FUT8B4GALT1POFUT1MAN2A1MGAT3B4GALT2B4GALT3
PROTEIN STRUCTURE
Preparing viewer…
PDB6X5H · 2.25 Å · X-ray
View on RCSB ↗
Constraintⓘ
LOEUFⓘ
0.67LoF Tolerant
pLIⓘ
0.00Tolerant
Observed/Expected LoF0.48 [0.35–0.67]
RankingsWhere FUT8 stands among ~20K protein-coding genes
  • #3,688of 20,598
    Most Researched127 · top quartile
  • #3,174of 5,498
    Most Pathogenic Variants7
  • #4,899of 17,882
    Most Constrained (LOEUF)0.67
Genes detectedFUT8
Sources retrieved10 papers
Response time—
📄 Sources
10▼
1
FUT8-mediated aberrant N-glycosylation of B7H3 suppresses the immune response in triple-negative breast cancer.
PMID: 33976130
Nat Commun · 2021
1.00
2
PD-L2 glycosylation promotes immune evasion and predicts anti-EGFR efficacy.
PMID: 34697216
J Immunother Cancer · 2021
0.90
3
FUT8-mediated aberrant N-glycosylation of SEMA7A promotes head and neck squamous cell carcinoma progression.
PMID: 38548747
Int J Oral Sci · 2024
0.80
4
FUT8 upregulates CD36 and its core fucosylation to accelerate pericyte-myofibroblast transition through the mitochondrial-dependent apoptosis pathway during AKI-CKD.
PMID: 39563263
Mol Med · 2024
0.70
5
FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer.
PMID: 33466384
Int J Mol Sci · 2021
0.60