POFUT1 report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of POFUT1 at tissue level.

III. Associated gene sets

GO_0016266Biological processO-glycan processing
GO_0001525Biological processangiogenesis
GO_0008593Biological processregulation of Notch signaling pathway
GO_0001756Biological processsomitogenesis
GO_0007219Biological processNotch signaling pathway
GO_0006004Biological processfucose metabolic process
GO_0006493Biological processprotein O-linked glycosylation
GO_0007399Biological processnervous system development
GO_0006355Biological processregulation of DNA-templated transcription
GO_0007507Biological processheart development
GO_0036066Biological processprotein O-linked fucosylation
GO_0005783Cellular componentendoplasmic reticulum
GO_0016020Cellular componentmembrane
GO_0046922Molecular functionpeptide-O-fucosyltransferase activity
GO_0008417Molecular functionfucosyltransferase activity

IV. Literature review

[source]
Gene namePOFUT1
Protein nameGDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 1) (O-FucT-1)
Protein O-fucosyltransferase 1
GDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 1)
SynonymsKIAA0180
FUT12
DescriptionFUNCTION: 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). .

AccessionsA0A9L9PY15
Q9H488
ENST00000706472.1
ENST00000375749.8 [Q9H488-1]
ENST00000375730.3 [Q9H488-2]
ENST00000706471.1
A0A9L9PX68