AlphaFold predicted structure
POFUT1 · Q9H488
Mean pLDDT
93.1/ 100
Very high
388 residues
Confidence breakdown
- Very high(≥ 90)87%
- Confident(70–90)4%
- Low(50–70)5%
- Very low(< 50)4%
Open interactive 3D viewer
AlphaFold (Jumper et al., 2021) · CC BY 4.0
POFUT1
Chr 20q11.21protein O-fucosyltransferase 1
- Aliases:
- O-FUT, O-Fuc-T, KIAA0180, FUT12
- MANE:
- ENST00000375749.8
Annotations refreshed 9 hours ago.
Predicted protein structure
Clinical relevance (Genomics England PanelApp)
Diagnostic Grade (Green)
Pigmentary skin disorders
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Disease associations (Open Targets)
Dowling-Degos disease
0.72neurodegenerative disease
0.52skin neoplasm
0.24actinic keratosis
0.24placental retention
0.24hereditary disease
0.19hypertensive disorder
0.12colorectal carcinoma
0.11neoplasm
0.10hepatocellular carcinoma
0.10
Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.
Protein function (UniProt)
GDP-fucose protein O-fucosyltransferase 1
Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs)