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EC Tree
IUBMB Comments The enzyme, found in animals and insects, is involved in the biosynthesis of the alpha-D-xylosyl-(1->3)-alpha-D-xylosyl-(1->3)-beta-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. Glycosylation takes place at the serine in the C-X-S-X-P-C motif. The enzyme is bifunctional also being active with UDP-alpha-xylose as donor (EC 2.4.2.63, EGF-domain serine xylosyltransferase). When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
[protein with EGF-like domain]-L-serine
=
+
[protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
Synonyms
protein o-glucosyltransferase, protein o-glucosyltransferase 1, poglut2, poglut3, poglut,
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POGLUT2
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formerly named KDELC1
POGLUT3
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formerly named KDELC2
protein O-glucosyltransferase
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protein O-glucosyltransferase 1
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protein O-glycosyltransferase
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protein-O-glucosyltransferase 1
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Poglut
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POGLUT1
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Rumi
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UDP-alpha-D-glucose + [protein with EGF-like domain]-L-serine = UDP + [protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-alpha-D-glucose:[protein with EGF-like domain]-L-serine O-beta-glucosyltransferase (configuration-inverting)
The enzyme, found in animals and insects, is involved in the biosynthesis of the alpha-D-xylosyl-(1->3)-alpha-D-xylosyl-(1->3)-beta-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. Glycosylation takes place at the serine in the C-X-S-X-P-C motif. The enzyme is bifunctional also being active with UDP-alpha-xylose as donor (EC 2.4.2.63, EGF-domain serine xylosyltransferase). When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein.
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UDP-alpha-D-glucose + [factor IX protein with EGF-like domain]-L-serine
UDP + [factor IX protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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UDP-alpha-D-glucose + [factor VII protein with EGF-like domain 1]-L-serine
UDP + [factor VII protein with EGF-like domain 1]-3-O-(beta-D-glucosyl)-L-serine
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?
UDP-alpha-D-glucose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
UDP-alpha-D-glucose + [Notch protein with EGF-like domain]-L-serine
UDP + [Notch protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain 11]-L-serine435
UDP + [Notch1 protein with EGF-like domain 11]-3-O-(beta-D-glucosyl)-L-serine435
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UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain 12]-L-serine
UDP + [Notch1 protein with EGF-like domain 12]-3-O-(beta-D-glucosyl)-L-serine
the enzyme can only glycosylate serine residues in the C1XSXPC2 motif
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UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain]-L-serine
UDP + [Notch1 protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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when glycosylating EGF repeats, the enzyme exhibits significant protein O-xylosyltransferase, preferring EGF repeats with a diserine motif in the consensus O-glucosylation motif (C1-X-S-S-(P/A)-C2)
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UDP-alpha-D-glucose + [Notch2 protein with EGF-like domain]-L-serine
UDP + [Notch2 protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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?
UDP-alpha-D-glucose + [Notch3 protein with EGF-like domain 10]-L-serine435
UDP + [Notch3 protein with EGF-like domain 10]-3-O-(beta-D-glucosyl)-L-serine435
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UDP-alpha-D-glucose + [protein with EGF-like domain]-L-serine
UDP + [protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
the enzyme can only glycosylate serine residues in the C1XSXPC2 motif
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?
additional information
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UDP-alpha-D-glucose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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highest activity
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?
UDP-alpha-D-glucose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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highest activity
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?
additional information
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the enzyme also functions as a protein O-xylosyltransferase
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additional information
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the enzyme functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
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additional information
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the enzyme functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-alpha-D-glucose + [factor IX protein with EGF-like domain]-L-serine
UDP + [factor IX protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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UDP-alpha-D-glucose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
UDP-alpha-D-glucose + [Notch protein with EGF-like domain]-L-serine
UDP + [Notch protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain 11]-L-serine435
UDP + [Notch1 protein with EGF-like domain 11]-3-O-(beta-D-glucosyl)-L-serine435
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UDP-alpha-D-glucose + [Notch1 protein with EGF-like domain]-L-serine
UDP + [Notch1 protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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when glycosylating EGF repeats, the enzyme exhibits significant protein O-xylosyltransferase, preferring EGF repeats with a diserine motif in the consensus O-glucosylation motif (C1-X-S-S-(P/A)-C2)
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?
UDP-alpha-D-glucose + [Notch2 protein with EGF-like domain]-L-serine
UDP + [Notch2 protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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UDP-alpha-D-glucose + [Notch3 protein with EGF-like domain 10]-L-serine435
UDP + [Notch3 protein with EGF-like domain 10]-3-O-(beta-D-glucosyl)-L-serine435
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UDP-alpha-D-glucose + [protein with EGF-like domain]-L-serine
UDP + [protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
the enzyme can only glycosylate serine residues in the C1XSXPC2 motif
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?
additional information
?
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UDP-alpha-D-glucose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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highest activity
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?
UDP-alpha-D-glucose + [factor VII protein with EGF-like domain]-L-serine
UDP + [factor VII protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
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highest activity
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additional information
?
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the enzyme also functions as a protein O-xylosyltransferase
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additional information
?
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the enzyme functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
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additional information
?
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the enzyme functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
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Mn2+
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10 mM used in assay conditions
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UDP-2-deoxy-2-fluoro-glucose
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Breast Neoplasms
Protein O-glucosyltransferase 1 overexpression downregulates p16 in BT474 human breast cancer cells.
Endometrial Neoplasms
MicroRNA-134 suppresses endometrial cancer stem cells by targeting POGLUT1 and Notch pathway proteins.
Leukemia, Myeloid
Protein O-glucosyltransferase 1 overexpression downregulates p16 in BT474 human breast cancer cells.
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brenda
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brenda
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brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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malfunction
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enzyme mutations can cause Dowling-Degos disease
malfunction
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enzyme mutations cause a temperature-dependent loss of Notch signalling
metabolism
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the enzyme is essential for Notch signaling
metabolism
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the enzyme is necessary for efficient trafficking of endogenous Notch1 from the endoplasmic reticulum to the cell surface in HEK-293T cells
metabolism
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the enzyme regulates Notch protein folding and/or trafficking and allows signalling at the cell membrane by O-glycosylation of Notch in the endoplasmic reticulum
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PGLT1_BOVIN
392
0
46009
Swiss-Prot
Secretory Pathway (Reliability: 1 )
PGLT1_HUMAN
392
0
46189
Swiss-Prot
Secretory Pathway (Reliability: 1 )
PGLT1_MOUSE
392
0
46379
Swiss-Prot
Secretory Pathway (Reliability: 5 )
PGLT1_RAT
392
0
46510
Swiss-Prot
Secretory Pathway (Reliability: 4 )
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enzyme in binary or ternary complexes with factor IX EGF repeat residues 46-84 and UDP/UDP-alpha-D-glucose, hanging drop vapor diffusion method
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enzyme in complexes with three different EGF-like domains and either UDP, UDP-2-deoxy-2-fluoro-glucose or UDP-methyl-glucose, hanging drop vapor diffusion method, using 10-20% (w/v) PEG 5000 MME, 50 mM MES pH 6.5, 2-10 mM CaCl2, 0-250 mM NaCl, 5-10% (v/v) glycerol or 2-methyl-2,4-pentanediol
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A124F
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the mutation reduces the in vitro enzyme activity
A192F
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the mutation markedly reduces the in vitro enzyme activity
F122A
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the mutant retains only a trace amount of activity compared to the wild type enzyme
G199V
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the mutant retains only a trace amount of activity compared to the wild type enzyme
P197A
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the mutation markedly reduces the in vitro enzyme activity
R245L
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the mutation markedly reduces the enzyme activity
R298W
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the mutation completely abolishes the enzyme activity in vitro
S231A
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the mutation markedly reduces the in vitro enzyme activity
T267I
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the mutation markedly reduces the enzyme activity
D233E
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the mutation causes a class of adult-onset limb-girdle muscular dystrophy with reduced Notch signaling in muscular stem cells, called satellite cells, and hypoglycosylation on alpha-dystroglycan in muscles
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IgG Sepharose affinity chromatography, HiTrap Sepharose column chromatography, and Superdex 200 gel filtration
Ni-NTA agarose column chromatography
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Ni-NTA agarose column chromatography and Superdex 200 gel filtration
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Ni-NTA column chromatography
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expressed in Drosophila melanogaster mutant clones
expressed in HEK-293T cell
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expressed in HEK-293T cells
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expressed in Drosophila melanogaster mutant clones
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expressed in Drosophila melanogaster mutant clones
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Yu, H.; Takeuchi, H.
Protein O-glucosylation another essential role of glucose in biology
Curr. Opin. Struct. Biol.
56
64-71
2019
Homo sapiens
brenda
Takeuchi, H.; Haltiwanger, R.S.
Enzymatic analysis of the protein O-glycosyltransferase, Rumi, acting toward epidermal growth factor-like (EGF) repeats
Methods Mol. Biol.
1022
119-128
2013
Drosophila melanogaster
brenda
Yu, H.; Takeuchi, H.; Takeuchi, M.; Liu, Q.; Kantharia, J.; Haltiwanger, R.; Li, H.
Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations
Nat. Chem. Biol.
12
735-740
2016
Drosophila melanogaster
brenda
Li, Z.; Fischer, M.; Satkunarajah, M.; Zhou, D.; Withers, S.; Rini, J.
Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1)
Nat. Commun.
8
185
2017
Homo sapiens (Q8NBL1), Homo sapiens
brenda
Takeuchi, H.; Fernandez-Valdivia, R.; Caswell, D.; Nita-Lazar, A.; Rana, N.; Garner, T.; Weldeghiorghis, T.; Macnaughtan, M.; Jafar-Nejad, H.; Haltiwanger, R.
Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase
Proc. Natl. Acad. Sci. USA
108
16600-16605
2011
Homo sapiens, Mus musculus
brenda
Takeuchi, H.; Schneider, M.; Williamson, D.; Ito, A.; Takeuchi, M.; Handford, P.; Haltiwanger, R.
Two novel protein O-glucosyltransferases that modify sites distinct from POGLUT1 and affect Notch trafficking and signaling
Proc. Natl. Acad. Sci. USA
115
E8395-E8402
2018
Homo sapiens
brenda
Takeuchi, H.; Haltiwanger, R.
The role of O-glucosylation in Notch signaling
Trends Glycosci. Glycotechnol.
20
159-170
2008
Drosophila melanogaster
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brenda
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2.4.1.376 EGF-domain serine glucosyltransferase
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