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The protein encoded by FUT9 belongs to the glycosyltransferase family.
Showing 3 out of 6 products:
N-linked glycan mass spectrometry profile of wild-type mouse kidney glycoproteins revealed the presence of abundant terminal fucoses, which were lost following knockout of the Fut9 gene
Mice lacking alpha1,3-fucosyltransferase 9 exhibit modulation of in vivo immune responses against pathogens.
We found that Fut1 (show FUT1 Proteins) mRNA and Fut4 (show FUT4 Proteins) mRNA were upregulated, while Fut2 (show FUT2 Proteins) mRNA and Fut9 mRNA were downregulated by androgen in the caput epididymis.
FUT9 plays a significant role during human, but not mouse, E-selectin (show SELE Proteins)-mediated cell adhesion.
Alpha1,3-fucosyltransferase IX (Fut9)regulates expression of the Lewis X (Lex (show FUT4 Proteins)) carbohydrate structure in brain development
Mice lacking fut9 demonstrate disappearance of Lewis x (show FUT4 Proteins) structure in brain and increased anxiety-like behaviors.
N-glycosylation of human alpha1,3-fucosyltransferase IX is required for enzyme stability and activity.
Downregulation of fucosyltransferase 9 leads to decreased Lewis(x (show FUT4 Proteins)) levels and impaired neurite outgrowth.
Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor- and site-specificity profile
FUTIX plays a key role in the synthesis of Lex (show FUT4 Proteins) groups of CEACAM1 (show CEACAM1 Proteins)
FUT9 was found to be a trans-Golgi and trans-Golgi network (TGN (show TG Proteins)) glycosyltransferase (show GTDC2 Proteins) from confocal immunofluorescence co-localization with the markers of the secretory pathway beta4-galactosyltransferase (show GGTA1 Proteins) (trans-Golgi and TGN (show TG Proteins)) and TGN-46 (show TGOLN2 Proteins) (TGN (show TG Proteins))
A single nucleotide polymorphism in FUT9, rs3811070, was significantly associated with placental malaria infection.
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.
, alpha-1,3-fucosyltransferase 9B
, fucosyltransferase 9
, alpha3-fucosyltransferase 9
, fucosyltransferase IX
, galactoside 3-L-fucosyltransferase
, Fucosyltransferase IX
, Galactoside 3-L-fucosyltransferase
, alpha (1,3) fucosyltransferase type IX
, alpha-1,3-fucosyltransferase 9