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Information on EC 2.4.1.255 - protein O-GlcNAc transferase and Organism(s) Mus musculus and UniProt Accession Q8CGY8

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.255 protein O-GlcNAc transferase
IUBMB Comments
Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
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This record set is specific for:
Mus musculus
UNIPROT: Q8CGY8
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
o-linked n-acetylglucosamine transferase, ogt protein, o-glcnac protein, n-acetylglucosamine transferase, o-glcnac-transferase, human ogt, secret agent, ncogt, o-linked glcnac transferase, o-linked n-acetylglucosaminyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EGF domain-specific O-GlcNAc transferase
-
O-GlcNAc transferase
-
O-linked GlcNAc transferase
-
O-linked N-acetylglucosamine transferase
-
EGF domain-specific O-GlcNAc transferase
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epidermal growth factor domain-specific O-GlcNAc transferase
-
ncOGT
-
-
O-GlcNAc transferase
-
-
O-GlcNAc-transferase
-
-
O-linked beta-N-acetylglucosamine transferase
-
-
O-linked beta-N-acetylglucosaminyltransferase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:protein-O-beta-N-acetyl-D-glucosaminyl transferase
Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-GlcNAc + Abi2 protein
UDP + N-acetly-D-glucosaminyl-[Abi2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Abl2 protein
UDP + N-acetly-D-glucosaminyl-[Ab12 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Ablim2 protein
UDP + N-acetly-D-glucosaminyl-[Ablim2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Add1 protein
UDP + N-acetly-D-glucosaminyl-[Add1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Amot protein
UDP + N-acetly-D-glucosaminyl-[Amot protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Arhgap32 protein
UDP + N-acetly-D-glucosaminyl-[Arhgap32 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Atf2 protein
UDP + N-acetly-D-glucosaminyl-[Atf2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Clasp2 protein
UDP + N-acetly-D-glucosaminyl-[Clasp2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Clip1 protein
UDP + N-acetly-D-glucosaminyl-[Clip1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Cnot4 protein
UDP + N-acetly-D-glucosaminyl-[Cnot4 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Cnskr2 protein
UDP + N-acetly-D-glucosaminyl-[Cnskr2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Corp1b protein
UDP + N-acetly-D-glucosaminyl-[Corp1b protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Crtc1 protein
UDP + N-acetly-D-glucosaminyl-[Crtc1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Dlgap2 protein
UDP + N-acetly-D-glucosaminyl-[Dlgap2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Dvl1 protein
UDP + N-acetly-D-glucosaminyl-[Dv11 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Enah protein
UDP + N-acetly-D-glucosaminyl-[Enah protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Foxk2 protein
UDP + N-acetly-D-glucosaminyl-[Foxk2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Foxp1 protein
UDP + N-acetly-D-glucosaminyl-[Foxp1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Frs3 protein
UDP + N-acetly-D-glucosaminyl-[Frs3 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Mamld1 protein
UDP + N-acetly-D-glucosaminyl-[Mamld1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Nav1 protein
UDP + N-acetly-D-glucosaminyl-[Nav1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Ncoa1 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Ncoa2 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Ncoa5 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa5 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Nfia protein
UDP + N-acetly-D-glucosaminyl-[Nfia protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Notch epidermal growth factor 20 repeat
UDP + N-acetyl-D-gluosaminyl-[Notch epidermal growth factor 20 repeat]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Nr3c1 protein
UDP + N-acetly-D-glucosaminyl-[Nr3c1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Plec protein
UDP + N-acetly-D-glucosaminyl-[Plec protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Psd3 protein
UDP + N-acetly-D-glucosaminyl-[Psd3 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Rapgef2 protein
UDP + N-acetly-D-glucosaminyl-[Rapgef2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Rasgrf2 protein
UDP + N-acetly-D-glucosaminyl-[Rasgrf2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Sirt2 protein
UDP + N-acetly-D-glucosaminyl-[Sirt2 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Ss18l1 protein
UDP + N-acetly-D-glucosaminyl-[Ss1811 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Stat3 protein
UDP + N-acetly-D-glucosaminyl-[Stat3 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Tab1 protein
UDP + N-acetly-D-glucosaminyl-[Tab1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Tbr1 protein
UDP + N-acetly-D-glucosaminyl-[Tbr1 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Tle4 protein
UDP + N-acetly-D-glucosaminyl-[Tle4 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Tnik protein
UDP + N-acetly-D-glucosaminyl-[Tnik protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + Znf532 protein
UDP + N-acetly-D-glucosaminyl-[Znf532 protein]
show the reaction diagram
-
-
-
?
UDP-GlcNAc + glutathione S-transferase
glutathione S-transferase-GlcNAc + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-CARM1
glutathione S-transferase-CARM1-GlcNAc + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-MYPT1
glutathione S-transferase-MYPT1-GlcNAc + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + O-GlcNAcase
O-GlcNAcase-GlcNAc + UDP
show the reaction diagram
-
-
-
-
?
UDP-GlcNAc + TRAK1 protein
UDP + N-acetyl-D-glucosaminyl-[TRAK1 protein]
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme catalyzes the addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) onto serine and threonine residues in response to stimuli or stress analogous to phosphorylation by Ser/Thr-kinases
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activates
Mg2+
activates
Mn2+
activates, highest activity in the presence of 1 mM Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Insulin
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tyrosine phosphorylation of OGT increases significantly after a 10 min insulin treatment
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UDP-N-acetyl-D-glucosamine
-
-
vanadate
-
tyrosine phosphatase inhibitor sodium vanadate, treatment increases OGT activity. When insulin is added to cells preincubated with sodium vanadate, there is a further increase in OGT activity versus inhibitor alone
additional information
-
insulin signaling stimulates tyrosine phosphorylation of OGT, increases its catalytic activity, affects OGT localization, and results in the O-GlcNAc modification of STAT3, a key kinase and transcription factor in 3T3-L1 adipocytes
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest expression
Manually annotated by BRENDA team
lowest expression
Manually annotated by BRENDA team
contains very little of the ogt transcripts
Manually annotated by BRENDA team
-
neuro-2a murine neuroblastoma cell, ATCC
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
enzyme activation of by UDP-GlcNAc blocks compound C-induced increases in 26S proteasome assembly and activation
physiological function
-
the enzyme plays a major role in AMPK regulation of the proteasome
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OGT1_MOUSE
1046
0
116952
Swiss-Prot
other Location (Reliability: 3)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
N-glycosylation sites Asn-263 and Asn-354, but not Asn-493, are modified with N-glycans. Both residues are modified with oligomannose N-glycans. Loss of an individual N-glycan does not affect endoplasmic reticulum localization of the enzyme (EOGT), enzyme activity, and ability to O-GlcNAcylate Notch1 in HEK-293T cells. Simultaneous substitution of both N-glycosylation sites affects both enzyme maturation and expression levels without an apparent change in enzymatic activity, suggesting that N-glycosylation at a single site is sufficient for enzyme maturation and expression
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N263Q/N354Q
a decrease in O-GlcNAc stoichiometry is observed in Notch1 co-expressed with an N263Q/N354Q variant compared with wild-type enzyme. The N263Q/N354Q variant exhibits altered subcellular distribution within the endoplasmic reticulum in HEK293T cells, indicating that N-glycosylation of EOGT is required for its localization in the endoplasmic reticulum at the cell periphery
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells
modified with both O-GlcNAc and tyrosine phosphorylation when overexpressed in insect cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Whelan, S.A.; Lane, M.D.; Hart, G.W.
Regulation of the O-linked beta-N-acetylglucosamine transferase by insulin signaling
J. Biol. Chem.
283
21411-21417
2008
Mus musculus
Manually annotated by BRENDA team
Hanover, J.A.; Yu, S.; Lubas, W.B.; Shin, S.H.; Ragano-Caracciola, M.; Kochran, J.; Love, D.C.
Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
Arch. Biochem. Biophys.
409
287-297
2003
Homo sapiens, Rattus norvegicus, Mus musculus (Q8CGY8), Mus musculus
Manually annotated by BRENDA team
Cheung, W.D.; Sakabe, K.; Housley, M.P.; Dias, W.B.; Hart, G.W.
O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins
J. Biol. Chem.
283
33935-33941
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Sakaidani, Y.; Ichiyanagi, N.; Saito, C.; Nomura, T.; Ito, M.; Nishio, Y.; Nadano, D.; Matsuda, T.; Furukawa, K.; Okajima, T.
O-linked-N-acetylglucosamine modification of mammalian Notch receptors by an atypical O-GlcNAc transferase Eogt1
Biochem. Biophys. Res. Commun.
419
14-19
2012
Mus musculus (Q8CGY8), Mus musculus
Manually annotated by BRENDA team
Xu, J.; Wang, S.; Viollet, B.; Zou, M.H.
Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT)
PLoS ONE
7
e36717
2012
Mus musculus
Manually annotated by BRENDA team
Alfaro, J.F.; Gong, C.X.; Monroe, M.E.; Aldrich, J.T.; Clauss, T.R.; Purvine, S.O.; Wang, Z.; Camp, D.G.; Shabanowitz, J.; Stanley, P.; Hart, G.W.; Hunt, D.F.; Yang, F.; Smith, R.D.
Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets
Proc. Natl. Acad. Sci. USA
109
7280-7285
2012
Mus musculus (Q8CGY8), Mus musculus
Manually annotated by BRENDA team
Alam, S.M.D.; Tsukamoto, Y.; Ogawa, M.; Senoo, Y.; Ikeda, K.; Tashima, Y.; Takeuchi, H.; Okajima, T.
N-Glycans on EGF domain-specific O-GlcNAc transferase (EOGT) facilitate EOGT maturation and peripheral endoplasmic reticulum localization
J. Biol. Chem.
295
8560-8574
2020
Mus musculus (Q8BYW9), Mus musculus
Manually annotated by BRENDA team