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Human POFUT1 Protein expressed in Escherichia coli (E. coli) - ABIN1098747
Luo, Haltiwanger: O-fucosylation of notch occurs in the endoplasmic reticulum. in The Journal of biological chemistry 2005
Show all 2 references for ABIN1098747
POFUT1 gene expression in gastric cancer
POFUT1, POGLUT1 (show POGLUT1 Proteins) and ADAM10 (show ADAM10 Proteins) are processing enzymes that are involved in different steps of Notch (show NOTCH1 Proteins) receptor activation in the epidermis; the roles of these unique enzymes in a single pathway may explain both the overlapping and distinct clinical features of DDD (show KRT5 Proteins) and RAK (show FRK Proteins) patients
High expression of POFUT1 correlates with aggressive clinicopathological characteristics and poor prognosis of hepatocellular carcinoma patients.
The upregulation of poFUT1 by LIF (show LIF Proteins) facilitated trophoblast cell migration and invasion through activating the PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling pathway.
Silencing of Pofut1 expression exerted antiproliferative and antiadhesive effects on hepatocytes.
Only a novel 1-bp deletion (c.246+5delG) in POFUT1 was found in a Chinese family with Dowling-Degos disease (DDD (show KRT5 Proteins)). No other novel mutation or this deletion was detected in POFUT1 in a second DDD (show KRT5 Proteins) family and a sporadic DDD (show KRT5 Proteins) case by Sanger Sequencing.
Identification of six pathogenic POFUT1 mutations in Dowling-Degos disease patients of different ethnic origin.
POFUT1 expression can contribute to cancer progression and that POFUT1 may serve as a diagnostic marker and a therapeutic target for OSCCs.
The protein product of POFUT1 plays a significant and conserved role in melanin synthesis and transport.
fucosyltransferases, O-FucT-1 is a soluble protein that localizes to the endoplasmic reticulum and recognizes properly folded epidermal growth factor (show EGF Proteins)-like repeats.
results demonstrated that POFUT1-mediated O-fucosylation of NOTCH (show NOTCH1 Proteins) receptors regulates myogenic cell differentiation and affects postnatal muscle growth in mice
results establish the critical role of Pofut1 on Notch (show NOTCH1 Proteins) pathway activation during myogenic differentiation
mDLL1 O-fucosylation by POFUT1 is dispensable for ligand function
Loss of Pofut1 is associated with myeloid hyperplasia and impaired lymphopoiesis.
Pofut1 and O-fucose have roles in mammalian Notch (show NOTCH1 Proteins) signaling
Pofut1 is required for Notch (show NOTCH1 Proteins) signaling upstream of NICD1.
These data are consistent with a role for Pofut1 in AChR aggregation during synaptogenesis via the regulation of the synaptogenic activity of muscle agrin (show AGRN Proteins).
Reduced POFUT1 levels might affect Notch (show NOTCH1 Proteins) trafficking or overall O-fucosylation.
This gene encodes a member of the glycosyltransferase O-Fuc family. This enzyme adds O-fucose through an O-glycosidic linkage to conserved serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and secreted proteins. O-fucose glycans are involved in ligand-induced receptor signaling. Alternative splicing of this gene results in two transcript variants encoding different isoforms.
GDP-fucose protein O-fucosyltransferase 1
, putative protein-O-fucosyltransferase
, peptide-O-fucosyltransferase 1
, protein-O-fucosyltransferase 1
, protein O-fucosyltransferase 1
, o-fucosyltransferase protein