FUT8
Alpha-(1,6)-fucosyltransferase
Also known as: FUT8_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9BYC5
- Gene
- FUT8
- Ensembl
- ENSG00000033170
- Chromosome
- 14
- Canonical length
- 575 aa
- Protein class
- Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins
- Subcellular location
- Nucleoplasm,Golgi apparatus,Cytosol
OverviewNCBI Gene
This gene encodes an enzyme belonging to the family of fucosyltransferases. The product of this gene catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha1-3, and alpha1-4 fucose addition. The expression of this gene may contribute to the malignancy of cancer cells and to their invasive and metastatic capabilities. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2011]
Canonical amino-acid sequenceUniProt
575 residues, UniProt reviewed canonical sequence.
>Q9BYC5|FUT8
1 MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL
61 RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY KKQTRNGLGK DHEILRRRIE
121 NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR
181 EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT
241 LILESQNWRY ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR
301 PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI
361 GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PSLLKEAKTK
421 YPNYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ
481 TLHPDASANF HSLDDIYYFG GQNAHNQIAI YAHQPRTADE IPMEPGDIIG VAGNHWDGYS
541 KGVNRKLGRT GLYPSYKVRE KIETVKYPTY PEAEKLocalizationUniProt · AlphaFold · HPA
Whether an antibody against FUT8 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Other membrane
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.3
- Highest tissue expression
- 40 nTPM
Expression across tissuesHPA
Tissue
- salivary gland: 40 nTPM
- spinal cord: 37 nTPM
- stomach: 30 nTPM
- cerebral cortex: 19 nTPM
- hippocampal formation: 18 nTPM
- tonsil: 17 nTPM
Single-cell type
- oligodendrocytes: 1,155 nCPM
- salivary acinar cells: 916 nCPM
- mucous neck cells: 705 nCPM
- plasma cells: 632 nCPM
- foveolar cells: 545 nCPM
- pituitary stem cells: 472 nCPM
Immune cell
- memory B-cell: 16 nTPM
- NK-cell: 15 nTPM
- T-reg: 10 nTPM
- naive B-cell: 8.3 nTPM
- naive CD4 T-cell: 6.6 nTPM
- naive CD8 T-cell: 6.6 nTPM
Brain region
- white matter: 158 nTPM
- cerebellum: 122 nTPM
- basal ganglia: 108 nTPM
- medulla oblongata: 100 nTPM
- cerebral cortex: 96 nTPM
- midbrain: 92 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about FUT8.
Disease | AllUniProt
Conditions FUT8 is implicated in, by any mechanism.
- Congenital disorder of glycosylation with defective fucosylation 1 (CDGF1) MIM:618005
Disease | GeneticClinVar
8 pathogenic / likely-pathogenic of 181 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Congenital disorder of glycosylation with defective fucosylation 1
- Inborn genetic diseases
- Malignant tumor of urinary bladder
- FUT8-related disorder
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.51
- gnomAD pLI
- 0.01
- gnomAD missense Z
- 2.2
- DepMap mean gene effect
- 0.04
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- fibroblast migration
- in utero embryonic development
- integrin-mediated signaling pathway
- L-fucose catabolic process
- N-glycan processing
- oligosaccharide biosynthetic process
- protein N-linked glycosylation
- protein N-linked glycosylation via asparagine
- regulation of cellular response to oxidative stress
- regulation of gene expression
- respiratory gaseous exchange by respiratory system
- transforming growth factor beta receptor signaling pathway
- viral protein processing
- GDP-L-fucose metabolic process
- receptor metabolic process
Molecular functions
- SH3 domain binding
- alpha-(1->6)-fucosyltransferase activity
- glycoprotein 6-alpha-L-fucosyltransferase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- SH3 domain
- SH3-like domain superfamily
- Variant SH3 domain
- Alpha-(1,6)-fucosyltransferase
- Glycosyltransferase family 23 (GT23) domain
- Alpha-(1,6)-fucosyltransferase, SH3 domain
- Alpha-(1,6)-fucosyltransferase, N- and catalytic domain
- Alpha-(1,6)-fucosyltransferase N- and catalytic domains
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of FUT8 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads FUT8 as an antibody target. Whether an autoantibody or antibody against FUT8 could matter depends on whether native FUT8 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
FUT8 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label FUT8 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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