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Information on EC 2.4.1.222 - O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
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EC Tree
2.4.1.222 O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferaseIUBMB Comments
The enzyme, found in animals and plants, is involved in the biosynthesis of the tetrasaccharides alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-alpha-L-Fuc and alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-alpha-L-Fuc, which are attached to L-Ser or L-Thr residues within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys in EGF-like domains in Notch and Factor-X proteins, respectively. The substrate is provided by EC 2.4.1.221, peptide-O-fucosyltransferase.
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Word Map
- 2.4.1.222
- notch
- glycosyltransferases
- somite
- mesoderm
- n-glycans
-
presomitic
- n-acetylglucosamine
-
somitogenesis
- udp-n-acetylglucosamine
-
galactosyltransferase
-
delta1
-
jagged1
-
paraxial
- dll1
-
delta-like
-
bisect
-
fucose-specific
-
unsegmented
-
o-fucosylation
- n-acetyllactosamine
-
o-mannose
-
glcnac-ts
-
delta-notch
-
n-acetylglucosaminylated
- pomgnt1s
- poly-n-acetyllactosamine
-
o-fucosyltransferase
-
tetraantennary
- gnt-ivs
-
o-mannosylated
- synthesis
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
n-acetylglucosaminyltransferase, lunatic fringe, radical fringe, manic fringe, beta1,3-n-acetylglucosaminyltransferase, beta-1,3-n-acetylglucosaminyltransferase, fringe protein, glycosyltransferase fringe, beta1,3-n-acetylglucosaminyltransferase-2, maniac fringe, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglucosaminylferase, uridine diphosphoacetylglucosamine:fucosyglycoprotein beta1-3-
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-
-
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beta-1,3-N-acetylglucosaminyltransferase
beta1,3-acetylglucosaminyltransferase
-
-
-
-
beta1,3-N-acetylglucosaminyltransferase
FNG
Fringe
fringe beta1,3 N-acetylglucosaminyltransferase
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-
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fringe glycosyltransferase
Fringe protein
LFNG
Lunatic Fringe
lunatic fringe glycosyltransferase
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Manic fringe
manic fringe glycosyltransferase
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MFng
O-fucose-beta1,3-N-acetylglucosaminyltransferase
O-fucosylpeptide beta-1,3-N-acetylglucosaminyltransferase
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Radical Fringe
radical fringe glycosyltransferase
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UDP-acetylglucosamine:fucosylglycoprotein
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UDP-D-GlcNAc:O-L-fucosylpeptide 3-beta-N-acetyl-D-glucosaminyltransferase
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UDP-GlcNAc:fucose beta1,3 N-acetylglucosaminyltransferase
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UDP-glucose:O-linked fucose beta1,3-glucosyltransferase
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Fringe
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-
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-
fringe glycosyltransferase
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O-fucose-beta1,3-N-acetylglucosaminyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-beta-D-GlcNAc + PCQNGGS(O-beta-L-fucosyl)-CKDQL = UDP + PCQNGGS(O-D-GlcNAcbeta(1-3)-L-Fucbeta)-CKDQL
UDP-beta-D-GlcNAc + PCQNGGS(O-beta-L-fucosyl)-CKDQL = UDP + PCQNGGS(O-D-GlcNAcbeta(1-3)-L-Fucbeta)-CKDQL
mechanism
-
UDP-beta-D-GlcNAc + PCQNGGS(O-beta-L-fucosyl)-CKDQL = UDP + PCQNGGS(O-D-GlcNAcbeta(1-3)-L-Fucbeta)-CKDQL
co-expressing of Notch and Fringe in Drosophila SL2 cells results in an increase of binding of ligand Delta to Notch
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UDP-beta-D-GlcNAc + PCQNGGS(O-beta-L-fucosyl)-CKDQL = UDP + PCQNGGS(O-D-GlcNAcbeta(1-3)-L-Fucbeta)-CKDQL
GlcNAc-transfer activity of Fringe is essential for it to modulate Notch signalling
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UDP-beta-D-GlcNAc + PCQNGGS(O-beta-L-fucosyl)-CKDQL = UDP + PCQNGGS(O-D-GlcNAcbeta(1-3)-L-Fucbeta)-CKDQL
EGF = epidermal growth factor, EGF-like domain = an evolutionary conserved domain containing 30 to 40 amino-acid residues first described from epidermal growth factor
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
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-
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:[protein with EGF-like domain]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine) 3-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
The enzyme, found in animals and plants, is involved in the biosynthesis of the tetrasaccharides alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-alpha-L-Fuc and alpha-Neu5Ac-(2->6)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-alpha-L-Fuc, which are attached to L-Ser or L-Thr residues within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys in EGF-like domains in Notch and Factor-X proteins, respectively. The substrate is provided by EC 2.4.1.221, peptide-O-fucosyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
299203-70-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
factor VII EGF repeat + UDP-D-GlcNAc
beta-D-glucosaminyl-factor VII EGF repeat + UDP
-
Manic fringe modifies O-fucose on mouse Notch1 at extracellular epidermal growth factor-like repeats within the ligand-binding site and the Abruptex region expressed in Lec1 cells
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?
Notch1 + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch1 + UDP
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Manic fringe modifies O-fucose on mouse Notch1 at extracellular epidermal growth factor-like repeats within the ligand-binding site and the Abruptex region expressed in Lec1 cells
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?
O-fucose residues on Jagged1 Notch ligand + UDP-GlcNAc
GlcNAc-beta1,3-fucitol-Jagged1 Notch
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human Jagged1 ligand, exogenous expressed in Chinese hamster ovary Lec1 cells, experiment in vivo
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?
O-fucose residues on Serrate Notch ligand + UDP-GlcNAc
?
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in vitro
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?
O-linked fucose on the epidermal growth factor-like sequence repeats of Notch + GlcNAc
GlcNAc-beta-1,3-fucitol-Notch
p-nitrophenyl-alpha-L-fucose + UDP-beta-D-GlcNAc
GlcNAc-beta-1,3-fucitol + p-nitrophenol + UDP
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?
UDP-GlcNAc + Notch epidermal growth factor-like sequence repeat-O-fucose
UDP + ?
Drosophila sp. (in: flies)
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the enzyme (Fringe) regulates fly Notch signaling by adding GlcNAc to O-fucose on Notch epidermal growth factor-like sequence repeats EGF8, -9, and -12
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?
[factor VII]-fucose + UDP-alpha-D-N-acetylglucosamine
[factor VII]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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residues on EGF repeat from factor VII
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?
[factor VII]-fucose + UDP-alpha-N-acetyl-2-amino-2-deoxy-D-glucose
[factor VII]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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residues on EGF repeat from factor VII
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?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
epidermal growth factor-like sequence repeats-O-fucose + UDP-GlcNAc
?
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Drosophila Fringe, Lunic Fringe, Manic Fringe
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?
epidermal growth factor-like sequence repeats-O-fucose + UDP-GlcNAc
?
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Drosophila Fringe, Lunic Fringe, Manic Fringe
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
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enzyme completely inhibits binding of Notch protein to its serrate ligands by capping of O-fucose sites, regulation of enzyme activity via expression level in correspondance to the expression level of protein O-fucosyltransferase
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
enzyme modulates signaling through Notch receptors by modifying O-linked fucose on epidermal growth factor-like domains
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
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enzyme plays a key role in the specification of boundaries during development by modulating the ability of Notch ligands to activate Notch receptors
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
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Fringe and protein O-fucosyltransferase regulate Notch signaling via binding to cell surface Notch receptors, overview
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
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Notch protein is O-fucosylated at a serine or threonine residue in epidermal growth factor-like repeats, identification of glycosylation sites
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
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Notch protein is O-fucosylated at a serine or threonine residue in the epidermal growth factor-like domain
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
Notch protein is O-fucosylated at a serine or threonine residue in the epidermal growth factor-like domain
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-
?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
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glycosylation of Notch enables it to activate signaling through binding to Delta ligand required for the specification of secondary mesenchym cells, loss of enzyme delays ectoderm patterning
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
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Notch protein is O-fucosylated at serine or threonine residues in the extracellular epidermal growth factor-like repeats, enzyme is O-fucose-specific
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?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
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different enzyme forms, glycosylation of Notch modulates its binding to different receptors, e.g. binding to Serrate is decreased, while binding to Delta is enhanced, the enzyme thereby inhibits or activates signaling, Fringe proteins differentially modulate ligand-induced proteolysis of Notch1
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?
O-fucose residues on Delta Notch ligand + UDP-GlcNAc
GlcNAc-beta-1,3-fucitol-Delta Notch
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in vitro
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?
O-fucose residues on Delta Notch ligand + UDP-GlcNAc
GlcNAc-beta-1,3-fucitol-Delta Notch
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rat Delta1 ligand, exogenous expressed in Chinese hamster ovary Lec1 cells, experiment in vivo
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?
O-linked fucose on the epidermal growth factor-like sequence repeats of Notch + GlcNAc
GlcNAc-beta-1,3-fucitol-Notch
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?
O-linked fucose on the epidermal growth factor-like sequence repeats of Notch + GlcNAc
GlcNAc-beta-1,3-fucitol-Notch
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endogenous Notch1, Manic Fringe
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?
p-nitrophenyl-alpha-L-fucose + UDP-GlcNAc
GlcNAc-beta-1,3-fucitol + p-nitrophenol + UDP
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p-nitrophenyl-alpha-L-fucose structurally mimics O-linked fucose, Lunic Fringe, Manic Fringe, Drosophila Fringe
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?
p-nitrophenyl-alpha-L-fucose + UDP-GlcNAc
GlcNAc-beta-1,3-fucitol + p-nitrophenol + UDP
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p-nitrophenyl-alpha-L-fucose structurally mimics O-linked fucose, Lunic Fringe, Manic Fringe, Drosophila Fringe
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?
UDP-beta-D-GlcNAc + fucosyl-protein
UDP + O-beta-D-GlcNAc-fucosyl-protein
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?
UDP-beta-D-GlcNAc + fucosyl-protein
UDP + O-beta-D-GlcNAc-fucosyl-protein
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?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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Fringe genes encode beta-1,3-N-acetyl-glucosaminyltransferases, which elongate O-fucose on the EGF repeat of Notch and its ligands
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?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
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?
additional information
?
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further substrate: recombinant epidermal growth factor repeat from the serum protein factor VII modified with O-linked fucose
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?
additional information
?
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no substrates: p-nitrophenyl-galactose, p-nitrophenyl-glucose
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?
additional information
?
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activity on different factor VII EGF repeat containing protein fragments, overview
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?
additional information
?
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
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O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255
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?
additional information
?
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Drosophila Fringe glycosyltransferase adds GlcNAc specifically to the O-fucose residues of Notch transmembrane proteins
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?
additional information
?
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Drosophila sp. (in: flies)
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Fringe is required for the differentiation of polar cell precursors. Fringe is necessary for generating positional information in localizing a high-affinity interaction between Notch and its ligand Delta, even if a second ligand is not essential
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?
additional information
?
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Drosophila sp. (in: flies)
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the glycosyltransferase Fringe promotes Delta-Notch signaling between neurons and glia, and is required for subtype-specific glial gene expression
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?
additional information
?
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
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MFng transfers GlcNAc in beta1-3-linkage to O-fucose residues present on the EGF repeats. Free MFng shows a specific activity with fucose and with 4 mM 4-nitrophenyl-2-fucose as acceptors. Transfer of C2-keto-glucose to fucose residues on EGF repeat from factor VII by the hum-MFng, substrate specificity, overview
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?
additional information
?
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the enzyme adds N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch
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?
additional information
?
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the enzyme adds N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch
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?
additional information
?
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the enzyme modifies EGF repeats in the Notch extracellular domain
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?
additional information
?
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the enzyme modifies EGF repeats in the Notch extracellular domain
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?
additional information
?
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the enzyme transfers beta-D-N-acetylglucosaminyl residues to EGF repeats of Notch proteins, Notch receptors and ligands are transmembrane proteins
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-
?
additional information
?
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the enzyme transfers beta-D-N-acetylglucosaminyl residues to EGF repeats of Notch proteins, Notch receptors and ligands are transmembrane proteins
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-
?
additional information
?
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the enzyme transfers beta-D-N-acetylglucosaminyl residues to EGF repeats of Notch proteins, Notch receptors and ligands are transmembrane proteins
-
-
?
additional information
?
-
-
further substrate: recombinant epidermal growth factor repeat from the serum protein factor VII modified with O-linked fucose
-
-
?
additional information
?
-
-
no substrates: p-nitrophenyl-galactose, p-nitrophenyl-glucose
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
Fringe elongates O-fucose residues on EGF-like repeat 4 and 5 of Notch3. Fringe plays a role in CADASIL pathophysiology
-
-
?
additional information
?
-
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transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
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LFNG, Lunatic Fringe, and MFNG, Manic Fringe, transfer N-acetylglucosamine (GlcNAc) to O-fucose attached to EGF-like repeats of NOTCH receptors
-
-
?
additional information
?
-
-
O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255
-
-
?
additional information
?
-
the enzyme adds N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch. Lfng inhibits activation of Notch1 and Notch4 in basal cells of the mouse prostate gland while enhancing Notch3 activation
-
-
?
additional information
?
-
the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221
-
-
?
additional information
?
-
-
the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221
-
-
?
additional information
?
-
Delta-like 3 is O-fucosylated at epidermal growth factor repeats two and five, and the fucosylated protein is a substrate for FNG proteins in cultured cells, the O-fucose-linked residues in EGF 2 and/or 5 are elongated by fringe protein, enzyme LFNG. Recognition of DLL3 by LFNG also does not depend on the presence of O-linked fucose
-
-
?
additional information
?
-
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Delta-like 3 is O-fucosylated at epidermal growth factor repeats two and five, and the fucosylated protein is a substrate for FNG proteins in cultured cells, the O-fucose-linked residues in EGF 2 and/or 5 are elongated by fringe protein, enzyme LFNG. Recognition of DLL3 by LFNG also does not depend on the presence of O-linked fucose
-
-
?
additional information
?
-
-
ligand-receptor interactions and role of fringe glycosylation, regulation of signaling, overview, Fringe proteins do not influence the surface expression of Notch1
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-GlcNAc + Notch epidermal growth factor-like sequence repeat-O-fucose
UDP + ?
Drosophila sp. (in: flies)
-
the enzyme (Fringe) regulates fly Notch signaling by adding GlcNAc to O-fucose on Notch epidermal growth factor-like sequence repeats EGF8, -9, and -12
-
-
?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
-
enzyme completely inhibits binding of Notch protein to its serrate ligands by capping of O-fucose sites, regulation of enzyme activity via expression level in correspondance to the expression level of protein O-fucosyltransferase
-
-
?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
enzyme modulates signaling through Notch receptors by modifying O-linked fucose on epidermal growth factor-like domains
-
-
?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
-
enzyme plays a key role in the specification of boundaries during development by modulating the ability of Notch ligands to activate Notch receptors
-
-
?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
-
Fringe and protein O-fucosyltransferase regulate Notch signaling via binding to cell surface Notch receptors, overview
-
-
?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
-
glycosylation of Notch enables it to activate signaling through binding to Delta ligand required for the specification of secondary mesenchym cells, loss of enzyme delays ectoderm patterning
-
-
?
Notch + UDP-D-GlcNAc
beta-D-glucosaminyl-Notch + UDP
-
different enzyme forms, glycosylation of Notch modulates its binding to different receptors, e.g. binding to Serrate is decreased, while binding to Delta is enhanced, the enzyme thereby inhibits or activates signaling, Fringe proteins differentially modulate ligand-induced proteolysis of Notch1
-
-
?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
-
-
-
-
?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
-
-
-
-
?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
-
Fringe genes encode beta-1,3-N-acetyl-glucosaminyltransferases, which elongate O-fucose on the EGF repeat of Notch and its ligands
-
-
?
[Notch]-fucose + UDP-alpha-D-N-acetylglucosamine
[Notch]-(3-O-beta-D-N-acetylglucosaminyl)fucose + UDP
-
-
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255
-
-
?
additional information
?
-
-
Drosophila Fringe glycosyltransferase adds GlcNAc specifically to the O-fucose residues of Notch transmembrane proteins
-
-
?
additional information
?
-
Drosophila sp. (in: flies)
-
Fringe is required for the differentiation of polar cell precursors. Fringe is necessary for generating positional information in localizing a high-affinity interaction between Notch and its ligand Delta, even if a second ligand is not essential
-
-
?
additional information
?
-
Drosophila sp. (in: flies)
-
the glycosyltransferase Fringe promotes Delta-Notch signaling between neurons and glia, and is required for subtype-specific glial gene expression
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
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?
additional information
?
-
the enzyme adds N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch
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?
additional information
?
-
-
the enzyme adds N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch
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-
?
additional information
?
-
the enzyme modifies EGF repeats in the Notch extracellular domain
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?
additional information
?
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-
the enzyme modifies EGF repeats in the Notch extracellular domain
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?
additional information
?
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the enzyme transfers beta-D-N-acetylglucosaminyl residues to EGF repeats of Notch proteins, Notch receptors and ligands are transmembrane proteins
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?
additional information
?
-
the enzyme transfers beta-D-N-acetylglucosaminyl residues to EGF repeats of Notch proteins, Notch receptors and ligands are transmembrane proteins
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?
additional information
?
-
the enzyme transfers beta-D-N-acetylglucosaminyl residues to EGF repeats of Notch proteins, Notch receptors and ligands are transmembrane proteins
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
Fringe elongates O-fucose residues on EGF-like repeat 4 and 5 of Notch3. Fringe plays a role in CADASIL pathophysiology
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor
-
-
?
additional information
?
-
-
LFNG, Lunatic Fringe, and MFNG, Manic Fringe, transfer N-acetylglucosamine (GlcNAc) to O-fucose attached to EGF-like repeats of NOTCH receptors
-
-
?
additional information
?
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-
O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255
-
-
?
additional information
?
-
the enzyme adds N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch. Lfng inhibits activation of Notch1 and Notch4 in basal cells of the mouse prostate gland while enhancing Notch3 activation
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-
?
additional information
?
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the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221
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?
additional information
?
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the enzyme interacts with Delta-like 3 (DLL3), a member of the DSL family of Notch ligands, epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for peptide-O-fucosyltransferase POFUT1, EC 2.4.1.221
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?
additional information
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ligand-receptor interactions and role of fringe glycosylation, regulation of signaling, overview, Fringe proteins do not influence the surface expression of Notch1
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Manganese
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-galactose
-
Gal is required for the enhancement of Notch signaling by LFNG, whereas Gal inhibits the enhancement of DLL1-induced NOTCH signaling by MFNG
additional information
-
enzyme expression is perturbed by injection of fringe morpholino antisense oligonucleotide resulting in a reduced number of secondary mesenchym cells and altered endoderm and mesoderm specification, as well as decreased and delayed archenteron invagination
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-galactose
-
Gal is required for the enhancement of Notch signaling by LFNG, whereas Gal inhibits the enhancement of DLL1-induced NOTCH signaling by MFNG
additional information
-
fringe requires a properly folded EGF repeat modified by O-fucose for its enzymatic activity
-
additional information
-
fringe requires a properly folded EGF repeat modified by O-fucose for its enzymatic activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Abortion, Spontaneous
Altered ?1,6-GlcNAc and bisecting GlcNAc-branched N-glycan on integrin ?1 are associated with early spontaneous miscarriage in humans.
Adenocarcinoma
Lunatic Fringe is a potent tumor suppressor in Kras-initiated pancreatic cancer.
alpha-1,6-mannosyl-glycoprotein 2-beta-n-acetylglucosaminyltransferase deficiency
Carbohydrate-deficient glycoprotein syndrome type II. An autosomal recessive N-acetylglucosaminyltransferase II deficiency different from typical hereditary erythroblastic multinuclearity, with a positive acidified-serum lysis test (HEMPAS).
Anemia
Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II.
Anemia, Dyserythropoietic, Congenital
Primary defect of congenital dyserythropoietic anemia type II. Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by lowered N-acetylglucosaminyltransferase II.
Breast Neoplasms
B3GNT3 overexpression promotes tumor progression and inhibits infiltration of CD8+ T cells in pancreatic cancer.
Breast Neoplasms
Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase.
Breast Neoplasms
Lunatic Fringe and p53 Cooperatively Suppress Mesenchymal Stem-Like Breast Cancer.
Breast Neoplasms
Lunatic fringe deficiency cooperates with the Met/Caveolin gene amplicon to induce basal-like breast cancer.
Breast Neoplasms
Manic fringe promotes a claudin-low breast cancer phenotype through notch-mediated PIK3CG induction.
Carcinogenesis
Effects of H-ras and v-sis overexpression on N-acetylglucosaminyltransferase V and metastasis-related phenotypes in human hepatocarcinoma cells.
Carcinoma
Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase.
Carcinoma
Notch signalling is linked to epidermal cell differentiation level in basal cell carcinoma, psoriasis and wound healing.
Carcinoma, Basal Cell
Notch signalling is linked to epidermal cell differentiation level in basal cell carcinoma, psoriasis and wound healing.
Carcinoma, Hepatocellular
Distribution of glycosyltransferases among Golgi apparatus subfractions from liver and hepatomas of the rat.
Carcinoma, Hepatocellular
Studies on UDP-N-acetylglucosamine : alpha-mannoside beta-N-acetylglucosaminyltransferase of rat liver and hepatomas.
Carcinoma, Non-Small-Cell Lung
Downregulation of N-Acetylglucosaminyltransferase GCNT3 by miR-302b-3p Decreases Non-Small Cell Lung Cancer (NSCLC) Cell Proliferation, Migration and Invasion.
Carcinoma, Renal Cell
Changes in N-acetylglucosaminyltransferase III, IV and V in renal cell carcinoma.
Carcinoma, Renal Cell
Nuclear and stromal expression of Manic fringe in renal cell carcinoma.
Choriocarcinoma
Abnormal biantennary sugar chains are expressed in human chorionic gonadotropin produced in the choriocarcinoma cell line, JEG-3.
Colonic Neoplasms
A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer.
Congenital Disorders of Glycosylation
Carbohydrate-deficient glycoprotein syndrome type II. An autosomal recessive N-acetylglucosaminyltransferase II deficiency different from typical hereditary erythroblastic multinuclearity, with a positive acidified-serum lysis test (HEMPAS).
Diphtheria
Biochemical studies of inositol N-acetylglucosaminyltransferase involved in mycothiol biosynthesis in Corynebacterium diphtheria.
Dysostoses
Disruption of the somitic molecular clock causes abnormal vertebral segmentation.
Dysostoses
Mutation of the LUNATIC FRINGE gene in humans causes spondylocostal dysostosis with a severe vertebral phenotype.
Glioma
Glioma cell fate decisions mediated by Dll1-Jag1-Fringe in Notch1 signaling pathway.
Infertility
A deficiency of lunatic fringe is associated with cystic dilation of the rete testis.
Lung Neoplasms
Downregulation of N-Acetylglucosaminyltransferase GCNT3 by miR-302b-3p Decreases Non-Small Cell Lung Cancer (NSCLC) Cell Proliferation, Migration and Invasion.
Lung Neoplasms
Manic fringe inhibits tumor growth by suppressing Notch3 degradation in lung cancer.
Lymphoma
A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: alpha-D-mannoside beta 1,6 N-acetylglucosaminyltransferase.
Malaria
N-acetylglucosaminyltransferase V-deficiency increases susceptibility to murine malaria.
Melanoma
Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis.
Melanoma
Comparative genomics reveals that loss of lunatic fringe (LFNG) promotes melanoma metastasis.
Melanoma
Melanoma-associated glycosyltransferase GCNT2 as an emerging biomarker and therapeutic target.
Melanoma
miR-146a Exerts Differential Effects on Melanoma Growth and Metastatization.
Melanoma
[Suppression of lung metastasis of B16 mouse melanoma cells by introduction of N-acetylglucosaminyltransferase III gene]
Multiple Sclerosis
Activity levels of a beta1,6 N-acetylglucosaminyltransferase in lymphomonocytes from multiple sclerosis patients.
Muscular Dystrophies
Biochemical and biophysical changes underlie the mechanisms of basement membrane disruptions in a mouse model of dystroglycanopathy.
Muscular Dystrophies
Retinal ectopias and mechanically weakened basement membrane in a mouse model of muscle-eye-brain (MEB) disease congenital muscular dystrophy.
Neoplasm Metastasis
Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis.
Neoplasm Metastasis
Comparative genomics reveals that loss of lunatic fringe (LFNG) promotes melanoma metastasis.
Neoplasm Metastasis
Effects of H-ras and v-sis overexpression on N-acetylglucosaminyltransferase V and metastasis-related phenotypes in human hepatocarcinoma cells.
Neoplasm Metastasis
Elevated expression of UDP-N-acetylglucosamine: alphamannoside beta1,6 N-acetylglucosaminyltransferase is an early event in hepatocarcinogenesis.
Neoplasm Metastasis
miR-146a Exerts Differential Effects on Melanoma Growth and Metastatization.
Neoplasm Metastasis
Recent progress in the molecular biology of the cloned N-acetylglucosaminyltransferases.
Neoplasm Metastasis
[Suppression of lung metastasis of B16 mouse melanoma cells by introduction of N-acetylglucosaminyltransferase III gene]
Neoplasms
A novel beta1,3-N-acetylglucosaminyltransferase involved in invasion of cancer cells as assayed in vitro.
Neoplasms
B3GNT3 overexpression promotes tumor progression and inhibits infiltration of CD8+ T cells in pancreatic cancer.
Neoplasms
Biosynthesis of blood group i-active polylactosaminoglycans. Partial purification and properties of an UDP-GlcNAc:N-acetyllactosaminide beta 1----3-N-acetylglucosaminyltransferase from Novikoff tumor cell ascites fluid.
Neoplasms
Correlated gene expression between beta-1,4-galactosyltransferase V and N-acetylglucosaminyltransferase V in human cancer cell lines.
Neoplasms
Elevated expression of UDP-N-acetylglucosamine: alphamannoside beta1,6 N-acetylglucosaminyltransferase is an early event in hepatocarcinogenesis.
Neoplasms
Inflammatory Stress Causes N-Glycan Processing Deficiency in Ocular Autoimmune Disease.
Neoplasms
Lunatic Fringe and p53 Cooperatively Suppress Mesenchymal Stem-Like Breast Cancer.
Neoplasms
Manic fringe inhibits tumor growth by suppressing Notch3 degradation in lung cancer.
Neoplasms
Novikoff ascites tumor cells contain N-acetyllactosaminide beta 1 leads to 3 and beta 1 leads to 6 N-acetylglucosaminyltransferase activity.
Neoplasms
Papillomavirus-mediated neoplastic progression is associated with reciprocal changes in JAGGED1 and manic fringe expression linked to notch activation.
Neoplasms
Recent progress in the molecular biology of the cloned N-acetylglucosaminyltransferases.
Neoplasms
The metastatic potential of rat prostate tumor variant R3327-MatLyLu is correlated with an increased activity of N-acetylglucosaminyl transferase III and V.
Neoplasms
Tumor-Suppressive Activity of Lunatic Fringe in Prostate through Differential Modulation of Notch Receptor Activation.
o-fucosylpeptide 3-beta-n-acetylglucosaminyltransferase deficiency
Lunatic fringe deficiency cooperates with the Met/Caveolin gene amplicon to induce basal-like breast cancer.
o-fucosylpeptide 3-beta-n-acetylglucosaminyltransferase deficiency
Manic Fringe deficiency imposes Jagged1 addiction to intestinal tumor cells.
Pancreatic Neoplasms
Lunatic Fringe is a potent tumor suppressor in Kras-initiated pancreatic cancer.
Pemphigoid, Bullous
Inflammatory Stress Causes N-Glycan Processing Deficiency in Ocular Autoimmune Disease.
Psoriasis
Notch signalling is linked to epidermal cell differentiation level in basal cell carcinoma, psoriasis and wound healing.
Tooth Abnormalities
Lunatic fringe, FGF, and BMP regulate the Notch pathway during epithelial morphogenesis of teeth.
Vesicular Stomatitis
Growth of enveloped RNA viruses in a line of chinese hamster ovary cells with deficient N-acetylglucosaminyltransferase activity.
Virus Diseases
[Mitochondrial N-acetylglucosaminyl transferase connected with viral infection]
Walker-Warburg Syndrome
Loss-of-function of an N-acetylglucosaminyltransferase, POMGnT1, in muscle-eye-brain disease.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Lunic Fringe has a higher specific activity than either Drosophila Fringe and Manic Fringe
additional information
-
free MFng shows a specific activity of 0.5 pmol/min/mg of protein with 100 mM fucose as an acceptor and 0.6 pmol/min/mg of protein with 4 mM 4-nitrophenyl-2-fucose as an acceptor
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
different enzyme forms, i.e. Radical Fringe, Lunatic Fringe, and Manic Fringe
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in the developing brain, Lfng is expressed in self-renewing progenitors
brenda
manic fringe is highly expressed in claudin-low breast cancer
brenda
-
expression is relatively constant during germ layer development and occurs in all cells, but becomes restricted during gastrulation
brenda
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isoform lunatic fringe Lfng is expressed by progenitors in neurogenic regions and downregulated in cells that have initiated neuronal differentiation
brenda
Lfng is expressed in the distal lung during saccular development
brenda
-
expression levels of three Fringe homologues in naive CD4+T cells in asthmatic rats, overview. Radical Fringe (Rfng) is highly expressed, whereas both Lunatic Fringe (Lfng) and Manic Fringe (Mfng) are expressed at low levels
brenda
additional information
-
distribution, Fringe is expressed in both the signaling and the receiving cells during the first Delta-Notch signal
brenda
-
Lfng is required cell autonomously in neural epithelial cells to limit the amount of neurogenesis and to maintain progenitors
brenda
expression of Lfng in the prostate is relatively low compared with manic fringe and radical fringe but more restricted to basal epithelium
brenda
expression of Lfng in the prostate is relatively low compared with manic fringe and radical fringe but more restricted to basal epithelium
brenda
-
Lfng continues to be highly expressed after thymus-seeding progenitors develop into T cell-committed DN2 (CD117+ CD25+) and then DN3a (CD117- CD25+) pro-T cells, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the family of glycosyltransferases. Binding to UDP and presence of DxD motif are two significant characteristics of glycosyltransferases
malfunction
metabolism
physiological function
additional information
malfunction
deletion of gene lfng impairs myofibroblast differentiation and alveogenesis, alveolar developmental defect in Lfng mutants with altered elastogenesis and collagen deposition in Lfng mutant lungs, phenotype, overview
malfunction
-
eliminating any of three highly conserved O-fucose sites at EGF 12, 26, or 27 within mouse Notch1 alters the activity in cell-based Notch signaling assays. EGF 12 is part of the ligand-binding region of Notch, a mouse line carrying a point mutation in the O-fucosylation site of EGF 12 in endogenous Notch1 shows loss of this site which results in a mild Notch phenotype with defects in T cell development
malfunction
-
impact of Lfng deficiency on beta-selection, decreasing Lfng expression during the DN3-DP transition minimizes the potent leukemogenic potential of Notch1 signaling
malfunction
-
Lfng depletion does not affect the balance between neuronally committed cells and selfrenewing progenitors, irrespective of the cell density of Lfng-depleted cells, and causes no obvious defects in brain development, but in vivo overexpression of Lfng shows that it strongly augments Notch signaling mediated by Delta-like 1 but not Jagged 1, phenotypes, overview
malfunction
-
Lfng modification of EGF12 in the Notch1 ligand-binding domain contributes to, but is not solely responsible for, the cell-nonautonomous inhibition of T cell development caused by transgenic Lfng expression in double-positive thymocytes. O-fucose site in the Notch1 ligand binding domain is partly responsible for the effects of Lfng overexpression
malfunction
-
Lfng overexpression results in significantly decreased Th2 cytokine production in asthma, which is the same effect as the gamma-secretase inhibitor GSI treatment alone, but has an increased effect on Th1 cytokines than GSI treatment
malfunction
-
the NOTCH signaling effect through MFNG is abolished by a DDD to DDA mutation in MFNG that inactivates its GlcNAc transferase activity
malfunction
deletion of Lfng in mice causes altered Notch activation in the prostate, associated with elevated accumulation of Notch1, Notch2, and Notch4 intracellular domains, decreased levels of the putative Notch3 intracellular fragment, as well as increased expression of Hes1, Hes5, and Hey2. Loss of Lfng results in expansion of the basal layer, increased proliferation of both luminal and basal cells, and ultimately, prostatic intraepithelial neoplasia. The Lfng-null prostate shows down-regulation of prostatic tumor suppressor gene NKX3.1 and increased androgen receptor expression. Deletion of Lfng caused dysregulation of Notch signaling in the prostate. Increased epithelial proliferation and prostatic intraepithelial neoplasia in the Lfng-null mutant gland
malfunction
-
Fringe-dependent Notch signaling is disrupted in a nac and Efr double mutant, reduction of Notch signaling may account for the developmental defects associated with CDG IIc
malfunction
knockdown of LFNG in DU-145 prostate cancer cells leads to expansion of CD44+CD24- and CD49f+CD24- stem/progenitor-like cell population associated with enhanced prostatosphere-forming capacity. The Lfng-null prostate shows down-regulation of prostatic tumor suppressor gene NKX3.1 and increased androgen receptor expression
malfunction
loss of the DSL protein DLL3 in the mouse results in severe somite patterning defects, which are virtually indistinguishable from the defects in mice that lack the enzyme lunatic fringe. Embryos double homozygous for null mutations in Dll3 and Lfng are phenotypically indistinguishable from the single mutants supporting a potential common function. Mutation of the O-fucosylation sites in DLL3 does not disrupt the interaction of DLL3 with LFNG or full length Notch1or DLL1, and O-fucosylation-deficient DLL3 can still inhibit Notch in cis in vitro. In contrast to wild type DLL3, O-fucosylation-deficient DLL3 cannot compensate for the loss of endogenous DLL3 during somitogenesis in the embryo
malfunction
Mfng silencing in claudin-low breast cancer CLBC cell lines reduces cell migration, tumorsphere formation, and in vivo tumorigenicity associated with a decrease in the stem-like cell population. Lfng deficiency induces basal-like breast cancer
malfunction
a Japanese Spondylocostal dysostosis case with multiple severe vertebral anomalies from cervical to sacral spine is a compound heterozygote for c.372delG (p.K124Nfs*) and c.601G>A (p.D201N) variants of the enzyme (LFNG), which encodes a glycosyltransferase (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase). The missense variant is in the DxD motif, an active-site motif of the glycosyltransferase, and its loss of the enzyme function is confirmed by an in vitro enzyme assay
metabolism
-
O-GlcNAc is added to Notch by an enzymatic activity distinct from the well-known nuclear/cytoplasmic O-GlcNAc transferase, OGT, EC 2.4.1.255. The structure GlcNAcbeta1-3Fucalpha1-OSer/Thr can be further elongated in mammals to the tetrasaccharide by sequential action of a beta1-4galactosyltransferase and an alpha2-3 or alpha2-6sialyltransferase
physiological function
-
isoform manic fringe expression is not required for embryonic development. Despite significant overlap in expression patterns, there are no obvious synergistic defects in mice in the absence of two, or all three, fringe genes during development of the axial skeleton, limbs, hindbrain, and cranial nerves
physiological function
-
isoforms lunatic fringe and manic fringe cooperatively enhance the Delta-like-1-Notch2 interaction to promote splenic marginal zone B cell development
physiological function
-
Lfng is required cell autonomously in neural epithelial cells to limit the amount of neurogenesis and to maintain progenitors. Lfng is not required for the role of Notch in interneuronal fate choice, which is mediated by Notch1a. The expression of Lfng does not require Notch activity, but rather is regulated downstream of proneural genes that are widely expressed by neural progenitors
physiological function
-
Fringe modulates Notch receptor expression and promotes the Notch signaling pathway through receptor-ligand binding, essential role of Fringe, overview. Notch signaling is more activated in asthmatic naive CD4+T cells than in control cells, and Lfng, but not Mfng or Rfng, partly inhibit Notch signaling in asthmatic naive CD4+T lymphocytes
physiological function
-
Fringe proteins are glycosyltransferases that add N-acetylglucosamine to O-fucose moieties to the extracellular domains of Notch receptors. In the immune system, Lunatic Fringe, Lfng, plays a key role in the early stages of T-lymphocyte development, critically enhancing DL4/Notch1-dependent suppression of alternative B-lineage potential and promoting T-lineage specification. Furthermore, Lfng and Manic Fringe cooperatively enhance DL1-induced Notch2 activation to promote marginal zone B-cell development. Lfng enhances Notch1 activation by Delta-like 4 to promote Notch1-dependent T-lineage commitment of thymus-seeding progenitors. Lfng temporally sustains Delta-like-induced Notch1 signaling to prolong proliferative self-renewal of pre-DP thymocytes. Pre-TCR signaling greatly augments Notch trophic functions to promote robust proliferation of pre-double positive progenitors. In the absence of DL/Notch signaling, pre-TCR expressing progenitors rapidly atrophy and differentiate into double positive thymocytes
physiological function
-
LFNG and MFNG are both required for the optimal generation of MZB cells in spleen consistent with a synergistic action on Notch. Differential modification of EGF repeats on Notch by LFNG versus MFNG: MFNG promotes DLL1-induced NOTCH signaling better in the absence of Gal than in its presence, the effect is reversed in Lec8 cells corrected by expression of a UDP-Gal transporter cDNA. MFNG activity is required to enhance DLL1-induced Notch signaling in Lec8 cells. In co-culture Notch signaling assays, LFNG generally enhances DLL1-induced Notch signaling, but not in either Lec8 or Lec20 CHO mutants lacking Gal on O-fucose glycans. LFNG generally inhibits JAG1-induced Notch signaling, but in mutant CHO cells that do not add galactose to the GlcNAc transferred by Fringe, JAG1-induced Notch signaling is not inhibited by LFNG or MFNG, roles for Gal in LFNG and MFNG modulation of DLL1-induced Notch signaling in CHO cells, overview
physiological function
Lunatic Fringe, Lfng, is a beta1-3 N-acetylglucosamine transferase that modifies Notch receptors to facilitate their activation by Delta-like (Dll1/4) ligands, Lfng functions to enhance Notch-dependent induction of myofibroblast differentiation during embryonic lung development in the mouse
physiological function
-
Notch signaling is essential for the self-renewal of mammalian neural progenitor cells. A variety of mechanisms modulate Notch signaling to balance the self-renewal and differentiation of progenitor cells. Fringe is a major Notch regulator and promotes or suppresses Notch signaling, depending on the Notch ligands. Lfng potentiates Notch signaling cell autonomously in neural progenitor cells of developinmg brain. Lfng and Notch intracellular domain affect embryonic self-renewing progenitor cell identity and cell proliferation in a similar way
physiological function
-
Notch1 activation by Delta-like Notch ligands is essential to induce T cell commitment and to suppress B cell development from thymus-seeding progenitors. Thymus-seeding progenitor competition for Delta-like ligand DL4 is critically regulated by Lunatic Fringe, which glycosylates epidermal growth factor repeats in the Notch1 extracellular domain to enhance binding avidity for Delta-like ligands. Notch1 activation is also essential for the process of beta-selection, which drives TCRbeta+ CD4/CD8 double-negative 3 precursors to proliferate and generate a large pool of CD4/CD8 double-positive thymocytes. Lunatic Fringe enhances competition for delta-like Notch ligands but does not overcome defective pre-TCR signaling during thymocyte beta-selection in vivo, importance of Lfng-Notch1 interactions in regulating competition of preselection and postselection DN3 thymocytes for DL ligands in vivo, overview. Transgenic Lfng confers a competitive advantage to wild-type but not Rag2-/- DN3 thymocytes. Lfng improves the competitive fitness of Lck-deficient and Ptcra-deficient DN3beta thymocytes
physiological function
-
the O-fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellulr domain. O-GlcNAc modification, a third form of O-glycosylation, occurs on EGF repeats, on hydroxy amino acids between the fifth and sixth conserved Cys of an EGF repeat. Similar to O-fucosylation, the major effect of Fringe-mediated O-fucose elongation appears to be modulation of Notch-ligand binding, whereby Delta activation of Notch is potentiated, while signaling via Serrate is inhibited. GlcNAc is the terminal sugar added to O-fucose residues on Drosophila Notch, and the disaccharide is sufficient for observing a Fringe effect, In vitro extension to trisaccharide causes no change in in vitro ligand binding as assessed in vitro
physiological function
-
the O-fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellulr domain. O-GlcNAc modification, a third form of O-glycosylation, occurs on EGF repeats, on hydroxy amino acids between the fifth and sixth conserved Cys of an EGF repeat. Similar to O-fucosylation, the major effect of Fringe-mediated O-fucose elongation appears to be modulation of Notch-ligand binding, whereby Delta activation of Notch is potentiated, while signaling via Serrate is inhibited. Mammalian Fringe modification also alters ligand binding. Elongation beyond GlcNAc to the trisaccharide (Galbeta1-4GlcNAcbeta1-3-Fucosealpha1-O-Ser/Thr) is necessary to see a Fringe effect in a mammalian cell system
physiological function
-
Drosophila Fringe is a glycosyltransferase, which adds GlcNAc specifically to the O-fucose residues on EGF-like repeats of Notch protein. The O-fucose is important as an acceptor for GlcNAc. The GlcNAc modification modulates the binding between Notch and two different ligands for Notch. This modulation of Notch-ligand interaction is required for region-specific activation of Notch signaling, which is essential for morphogenesis of various organs
physiological function
enzyme lunatic fringe is a glycosyltransferase involved in modifying Notch signaling. modification of DLL3 by O-linked fucose via the action of enzyme lunatic fringe is essential for its function during somitogenesis
physiological function
fringe genes code for O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferases that can add N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch. This modification modulates specificity and sensitivity of Notch receptors for different ligands. Therefore, fringes are powerful regulators of ligand-mediated Notch signaling. Tumor-suppressive activity of lunatic fringe in prostate through differential modulation of Notch receptor activation. The enzyme plays a critical role in regulation of prostate epithelial differentiation and proliferation, as well as in prostate tumor suppression
physiological function
fringe genes code for O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferases that can add N-acetylglucosamine to O-linked fucose residues on epidermal growth factor repeats of Notch. This modification modulates specificity and sensitivity of Notch receptors for different ligands. Therefore, fringes are powerful regulators of ligand-mediated Notch signaling. Tumor-suppressive activity of lunatic fringe in prostate through differential modulation of Notch receptor activation. The enzyme plays a critical role in regulation of prostate epithelial differentiation and proliferation, as well as in prostate tumor suppression
physiological function
manic fringe promotes a claudin-low breast cancer phenotype through notch-mediated phosphoinositide kinase PIK3CG induction. The enzyme functions as an oncogen in claudin-low breast cancer. Phosphoinossitide kinase Pik3cg is a direct target of enzyme Mfng-enhanced Notch signaling in claudin-low breast cancer
physiological function
the enzyme adds N-acetylglucoseamine to O-linked fucose on epidermal growth factor repeats of Notch. Fringe is a Golgi resident glycosyltransferase that requires a specific DxD active site motif to function. It specifically binds to uridinediphosphate (UDP)
physiological function
Drosophila sp. (in: flies)
-
the enzyme (Fringe) regulates fly Notch signaling by adding GlcNAc to O-fucose on Notch EGF8, -9, and -12. Fringe-modified EGF8, -9, and -12 promote Delta-Notch signaling in wing vein formation. Fringe-modified EGF8 and -12 prevent cis-inhibition of Serrate by Notch in vivo
additional information
-
Fringe elongation to the GlcNAc-beta1,3-fucose causes a significant conformational shift of several residues within the O-fucose consensus region. This may provide a mechanism for how Fringe modification indirectly exerts its effects on Notch activity at EGF 12
additional information
-
Lfng overexpression enhances proliferative expansion of DN3 and DN4 thymocytes in response to Delta-like ligands in vitro. Lfng overexpression augments binding of Delta-like 1 and Delta-like 4 by double negative and double positive thymocytes
additional information
enzyme structure modelling using Mus musculus manic fringe crystal structure, PDB ID 2J0A, as template, comparison with the other human fringe enzymes, overview. Homology modeling and molecular dynamics simulation, overview
additional information
enzyme structure modelling using Mus musculus manic fringe crystal structure, PDB ID 2J0A, as template, comparison with the other human fringe enzymes, overview. Homology modeling and molecular dynamics simulation, overview
additional information
enzyme structure modelling using Mus musculus manic fringe crystal structure, PDB ID 2J0A, as template, comparison with the other human fringe enzymes, overview. Homology modeling and molecular dynamics simulation, overview
additional information
expression of LFNG and NKX3.1 are positively correlated in publically available human prostate cancer data sets
additional information
-
expression of LFNG and NKX3.1 are positively correlated in publically available human prostate cancer data sets
Show AA Sequence and Transmembrane Helices (1545 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
-
x * 53000, recombinant galectin-1-hum-MFng fusion protein, SDS-PAGE, x * 33000, recombinant detagged MFng, SDS-PAGE
53000
-
x * 53000, recombinant galectin-1-hum-MFng fusion protein, SDS-PAGE, x * 33000, recombinant detagged MFng, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 53000, recombinant galectin-1-hum-MFng fusion protein, SDS-PAGE, x * 33000, recombinant detagged MFng, SDS-PAGE
additional information
additional information
enzyme structure homology modelling using Mus musculus manic fringe crystal structure, PDB ID 2J0A, as template, comparison with the other human fringe enzymes, overview
additional information
enzyme structure homology modelling using Mus musculus manic fringe crystal structure, PDB ID 2J0A, as template, comparison with the other human fringe enzymes, overview
additional information
enzyme structure homology modelling using Mus musculus manic fringe crystal structure, PDB ID 2J0A, as template, comparison with the other human fringe enzymes, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour diffusion method. Abolishing the glycosylation sites by site-directed mutagenesis was necessary in order to obtain orthorhombic crystals that diffracted to 1.8 A resolution. Crystals belonged to space group P2(1)2(1)2. The unit-cell parameters (a = 162.6, b = 41.4, c = 38.8 A) are consistent with the presence of one molecule in the asymmetric unit
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D327N
EMS mutagenesis, transheterozygote, mutation on allele 14, lethal phenotype
E220K
EMS mutagenesis, transheterozygote, mutation on allele 3, lethal phenotype
G295D
EMS mutagenesis, transheterozygote, mutation on allele L81, lethal phenotype
K196E
EMS mutagenesis, transheterozygote, mutation on allele 11, lethal phenotype
K196N
EMS mutagenesis, transheterozygote, mutation on allele 11, lethal phenotype
L213F
EMS mutagenesis, transheterozygote, mutation on allele L83, lethal phenotype
L398Q
EMS mutagenesis, transheterozygote, mutation on allele 2, phenotype overview
S350T
EMS mutagenesis, transheterozygote, mutation on allele 1, lethal phenotype
D288A
active site mutant to short loop side of residue D289, activity too low to measure
G334H
donor specificity mutant, 94.6% of wild-type UDP-beta-D-GlcNAc utilization, 78.0% of wild-type UDP-Glc utilization
H313A
donor specificity mutant, 6.2% of wild-type UDP-beta-D-GlcNAc utilization, 75.9% of wild-type UDP-Glc utilization
H313A/G334H
donor specificity mutant, 3.1% of wild-type UDP-beta-D-GlcNAc utilization, 34.7% of wild-type UDP-Glc utilization
L314R
donor specificity mutant, 21.7% of wild-type UDP-beta-D-GlcNAc utilization, 119.5% of wild-type UDP-Glc utilization
S312T
donor specificity mutant, 1.9% of wild-type UDP-beta-D-GlcNAc utilization, 18.1% of wild-type UDP-Glc utilization
additional information
additional information
construction and genetic analysis of mutated alleles, several mutants with introduced stop codons, mutant phenotypes analysis, mutants show altered wing vein numbers and structure, overview
additional information
enzyme knockout by LFNG-small hairpin RNA (shRNA) construct in retroviral red fluorescent protein (RFP) vector targeting 5'-AGCAGGTGACGCTGAGCTACGGTATGTTT- 3' sequences of the human LFNG gene
additional information
-
enzyme knockout by LFNG-small hairpin RNA (shRNA) construct in retroviral red fluorescent protein (RFP) vector targeting 5'-AGCAGGTGACGCTGAGCTACGGTATGTTT- 3' sequences of the human LFNG gene
additional information
-
enzyme expression is perturbed by injection of fringe morpholino antisense oligonucleotide resulting in a reduced number of secondary mesenchym cells and altered endoderm and mesoderm specification, as well as decreased and delayed archenteron invagination
additional information
-
a DDD to DDA mutation inactivates MFNG GlcNAc transferase activity
additional information
-
expression of Radical Fringe, Lunatic Fringe, and Manic Fringe in 293T cells and NIH 3T3 cells leads to increased receptor Delta1 binding and activation of Notch1 signaling, and to suppression of Jagged1-induced signaling by Lunatic and Manic Fringe, overview
additional information
-
gene silencing by Rfng-specific siRNA and overexpression of Lfng or Mfng in asthmatic CD4+ T lymphocytes. Downregulation of Rfng and overexpression of Lfng or Mfng enhance Th1 cytokines but suppress Th2 cytokine production, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant fusion protein galectin-1-hum-MFng from Escherichia coli strain Rosetta (DE3) pLysS, the fusion protein is cleaved with Tev protease to release the MFng protein, further purification by UDP-agarose chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain of murine Manic Fringe is expressed in the baculovirus/insect-cell system as a secreted protein
coexpression of Flag-tagged DLL3 and HA-tagged LFNG in CHO cells, the two proteins coprecipitate
DNA acid sequence determination and analysis, expression as insoluble His-tagged protein in Escherichia coli strain XL1-Blue
-
expression of MFeng as soluble protein in fusion with galectin-1 from pLgals1-hum-MFng in Escherichia coli Rosetta (DE3) pLysS
-
expression of Radical Fringe, Lunatic Fringe, and Manic Fringe in HEK 293T cells and NIH 3T3 cells
-
full-length, His-tagged FNG is expressed in S2 cells from a pMTHy vector construct
-
gene fng, DNA and amino acid sequence determination and analysis
gene Lfng, Lfng is located at 7p22 arm of human chromosome
gene LFNG, quantitative RT-PCR enzyme expression analysis
gene Rfng, Rfng is localized at 17q25 arm of human chromosome
genes lfng and mfng, expression in wild-type CHO cells, in Lec1.3C, Lec2.6A, Lec8.3D, and Lec20.15C CHO glycosylation mutant lines, and in Lec8 and Lec20 CHO mutant lines
-
mouse FRINGE coding sequences are ligated into pcDNA3 for transfection of NIH3T3 cells
-
Notch alone or Fringe alone expressed in Drosophila SL2 cells or Notch and Fringe co-expressed in Drosophila SL2 cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of Lfng does not require Notch activity, but rather is regulated downstream of proneural genes that are widely expressed by neural progenitors
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
the Notch signaling pathway is involved in numerous developmental cascades in mammals, mutations in the pathway have been implicated in a variety of Human diseases, like CADASIL, spondylocostal dysostosis, alagille syndrome, cancer and multiple sclerosis
synthesis
-
use of manic fringe in engineering of a mammalian O-glycosylation pathway in the yeast Saccharomyces cerevisiae for production of O-fucosylated epidermal growth factor domains. In the system, manic fringe facilitates the addition of N-acetylglucosamine to the EGF domain from factor IX but not from factor VII
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moloney, D.J.; Panin, V.M.; Johnston, S.H.; Chen, J.; Shao, U.; Wilson, R.; Wang, Y.; Stanley, P.; Irvine, K.D.; Haltwanger, R.S.; Vogt, T.F.
Fringe is a glycosyltransferase that modifies Notch
Nature
406
369-375
2000
Drosophila melanogaster, Mammalia
brenda
Bruckner, K.; Perez, L.; Clausen, H.; Cohen, S.
Glycosyltransferase activity of Fringe modulates Notch-Delta interactions
Nature
406
411-415
2000
Drosophila melanogaster
brenda
Panin, V.M.; Shao, L.; Lei, L.; Moloney, D.J.; Irvine, K.D.; Haltiwanger, R.S.
Notch ligands are substrates for protein O-fucosyltransferase-1 and Fringe
J. Biol. Chem.
277
29945-29952
2002
Drosophila melanogaster, Mammalia
brenda
Peterson, R.E.; McClay, D.R.
A Fringe-modified Notch signal affects specification of mesoderm and endoderm in the sea urchin embryo
Dev. Biol.
282
126-137
2005
Lytechinus variegatus
brenda
Okajima, T.; Xu, A.; Irvine, K.D.
Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe
J. Biol. Chem.
278
42340-42345
2003
Drosophila melanogaster
brenda
Shao, L.; Moloney, D.J.; Haltiwanger, R.
Fringe modifies O-fucose on mouse Notch1 at epidermal growth factor-like repeats within the ligand-binding site and the Abruptex region
J. Biol. Chem.
278
7775-7782
2003
Drosophila melanogaster
brenda
Xu, A.; Lei, L.; Irvine, K.D.
Regions of Drosophila Notch that contribute to ligand binding and the modulatory influence of Fringe
J. Biol. Chem.
280
30158-30165
2005
Drosophila melanogaster
brenda
Yang, L.T.; Nichols, J.T.; Yao, C.; Manilay, J.O.; Robey, E.A.; Weinmaster, G.
Fringe glycosyltransferases differentially modulate Notch1 proteolysis induced by Delta1 and Jagged1
Mol. Biol. Cell
16
927-942
2005
Rattus norvegicus
brenda
Correia, T.; Papayannopoulos, V.; Panin, V.; Woronoff, P.; Jiang, J.; Vogt, T.F.; Irvine, K.D.
Molecular genetic analysis of the glycosyltransferase Fringe in Drosophila
Proc. Natl. Acad. Sci. USA
100
6404-6409
2003
Drosophila melanogaster (Q24324)
brenda
Jinek, M.; Conti, E.
Eukaryotic expression, purification, crystallization and preliminary X-ray analysis of murine Manic Fringe
Acta Crystallogr. Sect. F
62
774-777
2006
Mus musculus (O09008), Mus musculus
brenda
Althauser, C.; Jordan, K.C.; Deng, W.M.; Ruohola-Baker, H.
Fringe-dependent notch activation and tramtrack function are required for specification of the polar cells in Drosophila oogenesis
Dev. Dyn.
232
1013-1020
2005
Drosophila sp. (in: flies)
brenda
Thomas, G.B.; van Meyel, D.J.
The glycosyltransferase Fringe promotes Delta-Notch signaling between neurons and glia, and is required for subtype-specific glial gene expression
Development
134
591-600
2007
Drosophila sp. (in: flies)
brenda
Arboleda-Velasquez, J.F.; Rampal, R.; Fung, E.; Darland, D.C.; Liu, M.; Martinez, M.C.; Donahue, C.P.; Navarro-Gonzalez, M.F.; Libby, P.; DAmore, P.A.; Aikawa, M.; Haltiwanger, R.S.; Kosik, K.S.
CADASIL mutations impair Notch3 glycosylation by Fringe
Hum. Mol. Genet.
14
1631-1639
2005
Mus musculus
brenda
Jinek, M.; Chen, Y.W.; Clausen, H.; Cohen, S.M.; Conti, E.
Structural insights into the Notch-modifying glycosyltransferase Fringe
Nat. Struct. Mol. Biol.
13
945-946
2006
Mus musculus (O09008), Mus musculus
brenda
Shifley, E.T.; Cole, S.E.
Lunatic fringe protein processing by proprotein convertases may contribute to the short protein half-life in the segmentation clock
Biochim. Biophys. Acta
1783
2384-2390
2008
Mus musculus
brenda
Okajima, T.; Reddy, B.; Matsuda, T.; Irvine, K.D.
Contributions of chaperone and glycosyltransferase activities of O-fucosyltransferase 1 to Notch signaling
BMC Biol.
6
1-10
2008
Drosophila melanogaster
brenda
Rampal, R.; Luther, K.B.; Haltiwanger, R.S.
Notch signaling in normal and disease States: possible therapies related to glycosylation
Curr. Mol. Med.
7
427-445
2007
Drosophila melanogaster, Homo sapiens, Mammalia
brenda
Sato, A.; Tomlinson, A.
Dorsal-ventral midline signaling in the developing Drosophila eye
Development
134
659-667
2007
Drosophila melanogaster
brenda
Shifley, E.T.; Vanhorn, K.M.; Perez-Balaguer, A.; Franklin, J.D.; Weinstein, M.; Cole, S.E.
Oscillatory lunatic fringe activity is crucial for segmentation of the anterior but not posterior skeleton
Development
135
899-908
2008
Mus musculus
brenda
Chigira, Y.; Oka, T.; Okajima, T.; Jigami, Y.
Engineering of a mammalian O-glycosylation pathway in the yeast Saccharomyces cerevisiae: production of O-fucosylated epidermal growth factor domains
Glycobiology
18
303-314
2008
Homo sapiens
brenda
Xu, A.; Haines, N.; Dlugosz, M.; Rana, N.A.; Takeuchi, H.; Haltiwanger, R.S.; Irvine, K.D.
In vitro reconstitution of the modulation of Drosophila Notch-ligand binding by Fringe
J. Biol. Chem.
282
35153-35162
2007
Drosophila melanogaster
brenda
Moran, J.L.; Shifley, E.T.; Levorse, J.M.; Mani, S.; Ostmann, K.; Perez-Balaguer, A.; Walker, D.M.; Vogt, T.F.; Cole, S.E.
Manic fringe is not required for embryonic development, and fringe family members do not exhibit redundant functions in the axial skeleton, limb, or hindbrain
Dev. Dyn.
238
1803-1812
2009
Mus musculus
brenda
Nikolaou, N.; Watanabe-Asaka, T.; Gerety, S.; Distel, M.; Koester, R.W.; Wilkinson, D.G.
Lunatic fringe promotes the lateral inhibition of neurogenesis
Development
136
2523-2533
2009
Danio rerio
brenda
Tan, J.B.; Xu, K.; Cretegny, K.; Visan, I.; Yuan, J.S.; Egan, S.E.; Guidos, C.J.
Lunatic and manic fringe cooperatively enhance marginal zone B cell precursor competition for delta-like 1 in splenic endothelial niches
Immunity
30
254-263
2009
Mus musculus
brenda
Luther, K.B.; Schindelin, H.; Haltiwanger, R.S.
Structural and mechanistic insights into lunatic fringe from a kinetic analysis of enzyme mutants
J. Biol. Chem.
284
3294-3305
2009
Mus musculus (O09008)
brenda
Xu, K.; Nieuwenhuis, E.; Cohen, B.; Wang, W.; Canty, A.; Danska, J.; Coultas, L.; Rossant, J.; Wu, M.; Piscione, T.; Nagy, A.; Gossler, A.; Hicks, G.; Hui, C.; Henkelman, R.; Yu, L.; Sled, J.; Gridley, T.; Egan, S.
Lunatic Fringe-mediated Notch signaling is required for lung alveogenesis
Am. J. Physiol. Lung Cell Mol. Physiol.
298
L45-L56
2010
Mus musculus (O09010)
brenda
Yuan, J.S.; Tan, J.B.; Visan, I.; Matei, I.R.; Urbanellis, P.; Xu, K.; Danska, J.S.; Egan, S.E.; Guidos, C.J.
Lunatic Fringe prolongs Delta/Notch-induced self-renewal of committed alphabeta T-cell progenitors
Blood
117
1184-1195
2011
Mus musculus
brenda
Rana, N.A.; Haltiwanger, R.S.
Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors
Curr. Opin. Struct. Biol.
21
583-589
2011
Drosophila melanogaster, Mus musculus
brenda
Pasek, M.; Ramakrishnan, B.; Boeggeman, E.; Mercer, N.; Dulcey, A.E.; Griffiths, G.L.; Qasba, P.K.
The N-acetyl-binding pocket of N-acetylglucosaminyltransferases also accommodates a sugar analog with a chemical handle at C2
Glycobiology
22
379-388
2012
Homo sapiens
brenda
Hou, X.; Tashima, Y.; Stanley, P.
Galactose differentially modulates Lunatic and Manic Fringe effects on Delta1-induced NOTCH signaling
J. Biol. Chem.
287
474-483
2012
Mus musculus
brenda
Visan, I.; Yuan, J.S.; Liu, Y.; Stanley, P.; Guidos, C.J.
Lunatic Fringe enhances competition for delta-like Notch ligands but does not overcome defective pre-TCR signaling during thymocyte beta-selection in vivo
J. Immunol.
185
4609-4617
2010
Mus musculus
brenda
Kato, T.M.; Kawaguchi, A.; Kosodo, Y.; Niwa, H.; Matsuzaki, F.
Lunatic fringe potentiates Notch signaling in the developing brain
Mol. Cell. Neurosci.
45
12-25
2010
Mus musculus
brenda
Gu, W.; Xu, W.; Ding, T.; Guo, X.
Fringe controls naive CD4(+)T cells differentiation through modulating notch signaling in asthmatic rat models
PLoS ONE
7
e47288
2012
Rattus norvegicus
brenda
Zhang, S.; Chung, W.C.; Wu, G.; Egan, S.E.; Miele, L.; Xu, K.
Manic fringe promotes a claudin-low breast cancer phenotype through notch-mediated PIK3CG induction
Cancer Res.
75
1936-1943
2015
Homo sapiens (O00587), Homo sapiens
brenda
Matsumoto, K.; Ishio, A.; Matsuno, K.
O-Fucose glycan in Drosophila Notch signaling
Glycosci. Biol. Med.
2015
841-847
2015
Drosophila melanogaster
-
brenda
Azam, S.; Akhunzada, M.
Structure and dynamic studies of lunatic, manic and radical fringe
J. Mol. Liq.
188
186-195
2013
Homo sapiens (O00587), Homo sapiens (Q8NES3), Homo sapiens (Q9Y644)
-
brenda
Zhang, S.; Chung, W.C.; Wu, G.; Egan, S.E.; Xu, K.
Tumor-suppressive activity of lunatic fringe in prostate through differential modulation of Notch receptor activation
Neoplasia
16
158-167
2014
Mus musculus (O09008), Homo sapiens (Q8NES3), Homo sapiens
brenda
Serth, K.; Schuster-Gossler, K.; Kremmer, E.; Hansen, B.; Marohn-Khn, B.; Gossler, A.
O-Fucosylation of DLL3 is required for its function during somitogenesis
PLoS ONE
10
e0123776
2015
Mus musculus (O09010), Mus musculus
brenda
Pandey, A.; Harvey, B.M.; Lopez, M.F.; Ito, A.; Haltiwanger, R.S.; Jafar-Nejad, H.
Glycosylation of specific Notch EGF repeats by O-Fut1 and Fringe regulates Notch signaling in Drosophila
Cell Rep.
29
2054-2066
2019
Drosophila sp. (in: flies)
brenda
Otomo, N.; Mizumoto, S.; Lu, H.F.; Takeda, K.; Campos-Xavier, B.; Mittaz-Crettol, L.; Guo, L.; Takikawa, K.; Nakamura, M.; Yamada, S.; Matsumoto, M.; Watanabe, K.; Ikegawa, S.
Identification of novel LFNG mutations in spondylocostal dysostosis
J. Hum. Genet.
64
261-264
2019
Homo sapiens (Q8NES3)
brenda
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