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Ac4-5S-GlcNAc + [protein]-L-serine
UDP + ?
the donor substrate analogues Ac4-5S-GlcNAc and benzyl-2-acetamido-2-deoxy-alpha-D-galactopyranoside, might reduce the flux through the hexosamine pathway and reduce the amount of intracellular UDP-GlcNAc with potential side effects on glycan synthesis
-
-
?
adhesin PsrP + UDP-GlcNAc
? + UDP
benzyl-2-acetamido-2-deoxy-alpha-D-galactopyranoside + [protein]-L-serine
UDP + ?
the donor substrate analogues Ac4-5S-GlcNAc and benzyl-2-acetamido-2-deoxy-alpha-D-galactopyranoside, might reduce the flux through the hexosamine pathway and reduce the amount of intracellular UDP-GlcNAc with potential side effects on glycan synthesis
-
-
?
capsid protein of Plum pox virus + UDP-N-acetyl-D-glucosamine
UDP + N-acetyl-D-glucosaminyl-[capsid protein of Plum pox virus]
casein kinase II + UDP-GlcNAc
? + UDP
-
-
-
-
?
casein kinase II + UDP-N-azidoacetylglucosamine
? + UDP
-
-
-
-
?
casein kinase II peptide + UDP-GlcNAc
? + UDP
-
-
-
-
?
casein kinase II peptide + UDP-GlcNAc
UDP + ?
-
much poorer substrate than Nup 62
-
-
?
crystalline alpha + UDP-GlcNAc
? + UDP
-
i.e. small heat-shock protein crystalline alpha
-
-
?
GSK-3beta + UDP-GlcNAc
UDP + ?
-
rabbit skeletal muscle glycogen synthase kinase (GSK) -3beta
-
-
?
KENSPCVTPVSTA + UDP-GlcNAc
? + UDP
-
-
-
?
KKKYPGGSTPVSSANMM + UDP-4-deoxy-GalNAc
? + UDP
-
-
-
?
KKKYPGGSTPVSSANMM + UDP-4-deoxy-GlcNAc
? + UDP
22.2% yield
-
-
?
KKKYPGGSTPVSSANMM + UDP-6-deoxy-GalNAc
? + UDP
37.7% yield
-
-
?
KKKYPGGSTPVSSANMM + UDP-6-deoxy-GlcNAc
? + UDP
85% yield
-
-
?
KKKYPGGSTPVSSANMM + UDP-GlcNAc
? + UDP
peptide acceptor derived from casein kinase II
-
-
?
KKKYPGGSTPVSSANMM + UDP-GlcNAc
UDP + ?
-
Pep-CKII, known natural substrate for OGT
-
-
?
KKKYPGGSTPVSSANMM + UDP-GlcNAz
? + UDP
peptide acceptor derived from casein kinase II
-
-
?
KKKYPGGSTPVSSANMM + UDP-GlcNPr
? + UDP
the close vicinity between Met501 and the N-acyl group of GlcNPr, as well as the hydrophobic environment near Met501, are responsible for the selective binding of UDP-GlcNPr
-
-
?
mitochondrial motor-adaptor protein milton + UDP-GlcNAc
? + UDP
-
-
mitochondrial motor-adaptor protein Milton is a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues
-
?
nucleoporin p62 + UDP-GlcNAc
? + UDP
-
high affinity substrate
-
-
?
nucleoporin p62 + UDP-N-azidoacetylglucosamine
? + UDP
-
-
-
?
OIP106 protein + UDP-GlcNAc
O-GlcNAc-OIP106 protein + UDP
-
N-terminal deletions of OIP106 are generated as S-tagged constructs: DELTAnCC, DELTA491, DELTA639, DELTA859
-
-
?
RBL-2 + UDP-GlcNAc
? + UDP
acceptor RBL-2 is a key regulator of entry into cell division. Residue Ser420 is a possible O-GlcNAc site in RBL-2. Substitution of Ser 420 inhibits OGT activity
-
-
?
UDP-GlcNAc + Abi2 protein
UDP + N-acetly-D-glucosaminyl-[Abi2 protein]
-
-
-
?
UDP-GlcNAc + Abl2 protein
UDP + N-acetly-D-glucosaminyl-[Ab12 protein]
-
-
-
?
UDP-GlcNAc + Ablim2 protein
UDP + N-acetly-D-glucosaminyl-[Ablim2 protein]
-
-
-
?
UDP-GlcNAc + Add1 protein
UDP + N-acetly-D-glucosaminyl-[Add1 protein]
-
-
-
?
UDP-GlcNAc + AIPVSREEK
UDP + AIPV-(GlcNAc)SREEK
-
-
-
-
?
UDP-GlcNAc + Amot protein
UDP + N-acetly-D-glucosaminyl-[Amot protein]
-
-
-
?
UDP-GlcNAc + Arhgap32 protein
UDP + N-acetly-D-glucosaminyl-[Arhgap32 protein]
-
-
-
?
UDP-GlcNAc + Atf2 protein
UDP + N-acetly-D-glucosaminyl-[Atf2 protein]
-
-
-
?
UDP-GlcNAc + beta-amyloid associated protein
GlcNAc-beta-amyloid associated protein + UDP
-
-
-
-
?
UDP-GlcNAc + c-MYC intron binding protein 1
UDP + N-acetyl-D-gluosaminyl-[c-MYC intron binding protein 1]
-
-
-
?
UDP-GlcNAc + calcium/calmodulin-dependent kinase IV
UDP + N-acetyl-D-glucosaminyl-[calcium/calmodulin-dependent kinase IV]
-
-
-
?
UDP-GlcNAc + CARM1 protein
UDP + N-acetyl-D-glucosaminyl-[CARM1 protein]
-
-
-
?
UDP-GlcNAc + CKII peptide
UDP + N-acetyl-D-glucosaminyl-[CKII peptide]
UDP-GlcNAc + CKII peptide
UDP + N-acetylglucosaminyl-CKII alpha-peptide
PGGSTPVSSANMM
-
-
?
UDP-GlcNAc + Clasp2 protein
UDP + N-acetly-D-glucosaminyl-[Clasp2 protein]
-
-
-
?
UDP-GlcNAc + Clip1 protein
UDP + N-acetly-D-glucosaminyl-[Clip1 protein]
-
-
-
?
UDP-GlcNAc + Cnot4 protein
UDP + N-acetly-D-glucosaminyl-[Cnot4 protein]
-
-
-
?
UDP-GlcNAc + Cnskr2 protein
UDP + N-acetly-D-glucosaminyl-[Cnskr2 protein]
-
-
-
?
UDP-GlcNAc + Corp1b protein
UDP + N-acetly-D-glucosaminyl-[Corp1b protein]
-
-
-
?
UDP-GlcNAc + Crtc1 protein
UDP + N-acetly-D-glucosaminyl-[Crtc1 protein]
-
-
-
?
UDP-GlcNAc + CSNK1D
CSNK1D-GlcNAc + UDP
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
-
-
?
UDP-GlcNAc + DCTN1
DCTN1-GlcNAc + UDP
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
-
-
?
UDP-GlcNAc + DELTA639 protein
UDP + N-acetyl-D-glucosaminyl-[DELTA639 protein]
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
UDP-GlcNAc + DELTAnCC protein
UDP + N-acetyl-D-glucosaminyl-[DELTAnCC protein]
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
UDP-GlcNAc + Dlgap2 protein
UDP + N-acetly-D-glucosaminyl-[Dlgap2 protein]
-
-
-
?
UDP-GlcNAc + Dvl1 protein
UDP + N-acetly-D-glucosaminyl-[Dv11 protein]
-
-
-
?
UDP-GlcNAc + dynamin-related protein 1
UDP + dynamin-related protein 1-GlcNAc
dynamin-related protein 1 is O-linked-N-acetyl-glucosamine-glycosylated at threonine 585 and 586
-
-
?
UDP-GlcNAc + Enah protein
UDP + N-acetly-D-glucosaminyl-[Enah protein]
-
-
-
?
UDP-GlcNAc + Foxk2 protein
UDP + N-acetly-D-glucosaminyl-[Foxk2 protein]
-
-
-
?
UDP-GlcNAc + Foxp1 protein
UDP + N-acetly-D-glucosaminyl-[Foxp1 protein]
-
-
-
?
UDP-GlcNAc + Frs3 protein
UDP + N-acetly-D-glucosaminyl-[Frs3 protein]
-
-
-
?
UDP-GlcNAc + glutathione S-transferase
glutathione S-transferase-GlcNAc + UDP
UDP-GlcNAc + glutathione S-transferase-CARM1
glutathione S-transferase-CARM1-GlcNAc + UDP
UDP-GlcNAc + glutathione S-transferase-MYPT1
glutathione S-transferase-MYPT1-GlcNAc + UDP
UDP-GlcNAc + H2O
UDP + GlcNAc
UDP-GlcNAc + host cell factor C1
UDP + N-acetyl-D-gluosaminyl-[host cell factor C1]
the enzyme both O-GlcNAcylates the HCF-1N subunit and directly cleaves the host cell factor-1PRO repeat
-
-
?
UDP-GlcNAc + ITISETPSSTTTTQITK
UDP + ITI-(GlcNAc)SETPSSTTTTQITK
-
-
-
-
?
UDP-GlcNAc + KKFELLPTPPLSPSRR
UDP + KKFELLP-(GlcNAc)TPPLSPSRR
-
-
-
-
?
UDP-GlcNAc + Mamld1 protein
UDP + N-acetly-D-glucosaminyl-[Mamld1 protein]
-
-
-
?
UDP-GlcNAc + MYPT1
MYPT1-GlcNAc + UDP
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
-
-
?
UDP-GlcNAc + Nav1 protein
UDP + N-acetly-D-glucosaminyl-[Nav1 protein]
-
-
-
?
UDP-GlcNAc + Ncoa1 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa1 protein]
-
-
-
?
UDP-GlcNAc + Ncoa2 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa2 protein]
-
-
-
?
UDP-GlcNAc + Ncoa5 protein
UDP + N-acetly-D-glucosaminyl-[Ncoa5 protein]
-
-
-
?
UDP-GlcNAc + NFATc1
O-GlcNAc-NFATc1 + UDP
-
-
-
-
?
UDP-GlcNAc + Nfia protein
UDP + N-acetly-D-glucosaminyl-[Nfia protein]
-
-
-
?
UDP-GlcNAc + Notch epidermal growth factor 20 repeat
UDP + N-acetyl-D-gluosaminyl-[Notch epidermal growth factor 20 repeat]
-
-
-
?
UDP-GlcNAc + Nr3c1 protein
UDP + N-acetly-D-glucosaminyl-[Nr3c1 protein]
-
-
-
?
UDP-GlcNAc + Nup 62 protein
UDP + ?
-
-
-
-
?
UDP-GlcNAc + Nup62 protein
UDP + N-acetyl-D-glucosaminyl-[Nup62 protein]
-
-
-
?
UDP-GlcNAc + Nup62 protein
UDP + N-acetyl-D-glucosmainyl-[Nup62 protein]
UDP-GlcNAc + O-GlcNAcase
O-GlcNAcase-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + p62 protein
UDP + N-acetyl-D-glucosaminyl-[p62 protein]
-
-
-
?
UDP-GlcNAc + PGC-1alpha
UDP + N-acetyl-D-gluosaminyl-[PGC-1alpha]
-
-
-
?
UDP-GlcNAc + PGGSTPVS(PO3)-SANMM
? + UDP
-
-
-
-
?
UDP-GlcNAc + PGGSTPVSSANMM
UDP + PGGSTPV-(GlcNAc)SSANMM
-
PGGSTPVSSANMM is the best acceptor
-
-
?
UDP-GlcNAc + Plec protein
UDP + N-acetly-D-glucosaminyl-[Plec protein]
-
-
-
?
UDP-GlcNAc + Psd3 protein
UDP + N-acetly-D-glucosaminyl-[Psd3 protein]
-
-
-
?
UDP-GlcNAc + Rapgef2 protein
UDP + N-acetly-D-glucosaminyl-[Rapgef2 protein]
-
-
-
?
UDP-GlcNAc + Rasgrf2 protein
UDP + N-acetly-D-glucosaminyl-[Rasgrf2 protein]
-
-
-
?
UDP-GlcNAc + SAP130
SAP130-GlcNAc + UDP
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
-
-
?
UDP-GlcNAc + Sirt2 protein
UDP + N-acetly-D-glucosaminyl-[Sirt2 protein]
-
-
-
?
UDP-GlcNAc + Ss18l1 protein
UDP + N-acetly-D-glucosaminyl-[Ss1811 protein]
-
-
-
?
UDP-GlcNAc + Stat3 protein
UDP + N-acetly-D-glucosaminyl-[Stat3 protein]
-
-
-
?
UDP-GlcNAc + Tab1 protein
UDP + N-acetly-D-glucosaminyl-[Tab1 protein]
-
-
-
?
UDP-GlcNAc + TAB1 protein
UDP + N-acetyl-D-glucosaminyl-[TAB1 protein]
UDP-GlcNAc + tau protein
GlcNAc-tau protein + UDP
-
-
-
-
?
UDP-GlcNAc + Tbr1 protein
UDP + N-acetly-D-glucosaminyl-[Tbr1 protein]
-
-
-
?
UDP-GlcNAc + Tle4 protein
UDP + N-acetly-D-glucosaminyl-[Tle4 protein]
-
-
-
?
UDP-GlcNAc + Tnik protein
UDP + N-acetly-D-glucosaminyl-[Tnik protein]
-
-
-
?
UDP-GlcNAc + TRAK1 protein
UDP + N-acetyl-D-glucosaminyl-[TRAK1 protein]
UDP-GlcNAc + transcription factor FoxM1
O-GlcNAc-transcription factor FoxM1 + UDP
-
-
-
-
?
UDP-GlcNAc + transcription factor NFAT
UDP + N-acetyl-D-glucosaminyl-[transcription factor NFAT]
-
-
-
-
?
UDP-GlcNAc + transcription factor NFkappaB
UDP + N-acetyl-D-glucosaminyl-[transcription factor NFkappaB]
-
-
-
-
?
UDP-GlcNAc + YPGGSTPVSSANMM
UDP + YPGGSTPVS-3-O-(N-acetyl-D-glucosaminyl)-SANMM
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + ?
UDP-GlcNAc + YSDSPSTST
UDP + GlcNAc-YSDSPSTST
-
-
-
?
UDP-GlcNAc + YSDSPSTST
YSDSP-(GlcNAc)STST + UDP
-
coupled enzyme assay of C-654
-
-
?
UDP-GlcNAc + YSPTSPSYSPTSPS
UDP + Y-(GlcNAc)SPT-(GlcNAc)SPSYSPT-(GlcNAc)SPS
-
YSPTSPSYSPTSPS is a poor substrate
-
-
?
UDP-GlcNAc + Znf532 protein
UDP + N-acetly-D-glucosaminyl-[Znf532 protein]
-
-
-
?
UDP-GlcNAc + [YSPTSPSYSPTSPS]5
UDP + [Y-(GlcNAc)SP-(GlcNAc)TSPSYSP-(GlcNAc)TSPS]5
-
-
-
-
?
UDP-GlcNAc DELTA491 protein
UDP + N-acetyl-D-glucosaminyl-[DELTA491 protein]
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + FITC-YAVVPVSK peptide
UDP + ?
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [Nup62 protein]-L-serine
UDP + [Nup62 protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [octamer-binding protein 4]-L-serine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
UDP-N-acetyl-alpha-D-glucosamine + [octamer-binding protein 4]-L-threonine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine
UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine
UDP-N-acetyl-D-glucosamine + KKKYPGGSTPVSSANMM
UDP + ?
-
-
-
?
UDP-N-acetyl-D-glucosamine + YPGGSTPVSSANMM
UDP + YPGGSTPVS-3-O-(N-acetyl-D-glucosaminyl)-SANMM
-
-
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-serine
?
UDP-N-acetyl-5-deoxy-5-thio-alpha-D-glucosamine is a very poor (3200times slower) donor substrate compared to UDP-N-acetyl-D-glucosamine
-
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-serine
UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine
the enzyme transfers N-acetylglucosamine from the sugar donor UDP-GlcNAc onto specific serine or threonine residues of nucleocytoplasmic proteins with inversion of configuration at the anomeric center
-
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-serine
UDP + [protein]-O3-(N-acetyl-D-glucosaminyl)-L-serine
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-threonine
UDP + [protein]-O3-(N-acetyl-D-glucosaminyl)-L-threonine
-
-
-
-
?
YSDSPSTST + UDP-GlcNAc
UDP + ?
-
-
-
-
?
additional information
?
-
adhesin PsrP + UDP-GlcNAc
? + UDP
-
the core enzyme GtfA and co-activator GtfB form an OGT complex to glycosylate the first serine-rich repeat of adhesin PsrP (pneumococcal serine-rich repeat protein), which is involved in the infection and pathogenesis. Formation of the GtfA-GtfB complex is crucial for the O-GlcNAcylation activity
-
?
adhesin PsrP + UDP-GlcNAc
? + UDP
-
the core enzyme GtfA and co-activator GtfB form an OGT complex to glycosylate the first serine-rich repeat of adhesin PsrP (pneumococcal serine-rich repeat protein), which is involved in the infection and pathogenesis. Formation of the GtfA-GtfB complex is crucial for the O-GlcNAcylation activity
-
?
capsid protein of Plum pox virus + UDP-N-acetyl-D-glucosamine
UDP + N-acetyl-D-glucosaminyl-[capsid protein of Plum pox virus]
-
-
-
?
capsid protein of Plum pox virus + UDP-N-acetyl-D-glucosamine
UDP + N-acetyl-D-glucosaminyl-[capsid protein of Plum pox virus]
-
-
-
?
capsid protein of Plum pox virus + UDP-N-acetyl-D-glucosamine
UDP + N-acetyl-D-glucosaminyl-[capsid protein of Plum pox virus]
-
-
-
-
?
UDP-GlcNAc + CKII peptide
UDP + N-acetyl-D-glucosaminyl-[CKII peptide]
-
-
-
?
UDP-GlcNAc + CKII peptide
UDP + N-acetyl-D-glucosaminyl-[CKII peptide]
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase
glutathione S-transferase-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase
glutathione S-transferase-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-CARM1
glutathione S-transferase-CARM1-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-CARM1
glutathione S-transferase-CARM1-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-MYPT1
glutathione S-transferase-MYPT1-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-MYPT1
glutathione S-transferase-MYPT1-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + H2O
UDP + GlcNAc
-
-
-
?
UDP-GlcNAc + H2O
UDP + GlcNAc
-
-
-
?
UDP-GlcNAc + Nup62 protein
UDP + N-acetyl-D-glucosmainyl-[Nup62 protein]
-
-
-
-
?
UDP-GlcNAc + Nup62 protein
UDP + N-acetyl-D-glucosmainyl-[Nup62 protein]
-
control substrate
-
-
?
UDP-GlcNAc + TAB1 protein
UDP + N-acetyl-D-glucosaminyl-[TAB1 protein]
-
-
-
?
UDP-GlcNAc + TAB1 protein
UDP + N-acetyl-D-glucosaminyl-[TAB1 protein]
-
-
-
-
?
UDP-GlcNAc + TAB1 protein
UDP + N-acetyl-D-glucosaminyl-[TAB1 protein]
-
-
-
-
?
UDP-GlcNAc + TRAK1 protein
UDP + N-acetyl-D-glucosaminyl-[TRAK1 protein]
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
-
-
?
UDP-GlcNAc + TRAK1 protein
UDP + N-acetyl-D-glucosaminyl-[TRAK1 protein]
-
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + ?
-
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + ?
-
highly specific synthetic peptide assay, affinity of the enzyme for UDP-GlcNAc is high and for the peptide substrate, YSDSPSTST, is only moderate
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [octamer-binding protein 4]-L-serine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [octamer-binding protein 4]-L-serine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
octamer-binding protein 4 (Oct4) is one of the key transcription factors required for pluripotency of embryonic stem cell and more recently, the generation of induced pluripotent stem cells. The action of Oct4 is modulated by the addition of several post-translational modifications, including O-GlcNAc. Human Oct4 activity is regulated by O-linked N-acetylglucosamine transferase by a mechanism that is distinct from mouse Oct4
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [octamer-binding protein 4]-L-threonine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [octamer-binding protein 4]-L-threonine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine
octamer-binding protein 4 (Oct4) is one of the key transcription factors required for pluripotency of embryonic stem cell and more recently, the generation of induced pluripotent stem cells. The action of Oct4 is modulated by the addition of several post-translational modifications, including O-GlcNAc. The action of Oct4 is modulated by the addition of several post-translational modifications, including O-GlcNAc. Human Oct4 activity is regulated by O-linked N-acetylglucosamine transferase by a mechanism that is distinct from mouse Oct4
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
essential enzyme that catalyzes the covalent bonding of N-acetylglucosamine to the hydroxyl group of a serine or threonine in the target protein. It plays an important role in many important cellular physiological catalytic reactions
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UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
Lys634, Asn838, Gln839, Lys842, His901, and Asp925 play an important role in stabilizing UDP at the active site of the enzyme via hydrogen bonds and pi-pi interactions. The binding free energy of the UDP-enzyme complex is mainly constituted by electrostatic interactions and side chain effects. The uridine diphosphate release mechanism is studied
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UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
the enzyme recognizes the majority of its substrates by binding them to the asparagine ladder within the lumen of superhelical tetratricopeptide repeat (TPR) domain of the enzyme
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UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine
essential enzyme that catalyzes the covalent bonding of N-acetylglucosamine to the hydroxyl group of a serine or threonine in the target protein. It plays an important role in many important cellular physiological catalytic reactions
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UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine
Lys634, Asn838, Gln839, Lys842, His901, and Asp925 play an important role in stabilizing UDP at the active site of the enzyme via hydrogen bonds and pi-pi interactions. The binding free energy of the UDP-enzyme complex is mainly constituted by electrostatic interactions and side chain effects. The uridine diphosphate release mechanism is studied
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UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine
UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine
the enzyme recognizes the majority of its substrates by binding them to the asparagine ladder within the lumen of superhelical tetratricopeptide repeat (TPR) domain of the enzyme
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additional information
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catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to Ser/Thr residues of proteins
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catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to Ser/Thr residues of proteins
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enzyme adds a single GlcNAc to hydroxyl groups of serine and threonine residues. In the plant Arabidopsis, OGT serves to attenuate the gibberillin pathway
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enzyme modifies the Plum pox virus capsid protein
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enzyme modifies the Plum pox virus capsid protein
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enzyme modifies the Plum pox virus capsid protein
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participates in plum pox virus infection, plants are inoculated with PPV-NK-GFP and observed at different times postinoculation under a fluorescence microscope
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participates in plum pox virus infection, plants are inoculated with PPV-NK-GFP and observed at different times postinoculation under a fluorescence microscope
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participates in plum pox virus infection, plants are inoculated with PPV-NK-GFP and observed at different times postinoculation under a fluorescence microscope
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additional information
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p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc are no substrates. The cloned enzyme cleaves GlcNAc, but not GalNAc, from glycopeptides
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additional information
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heat shock protein 90 (Hsp90) is involved in the regulation of O-linked beta-N-acetylglucosamine transferase. Inhibition of Hsp90 by radicicol or 17-N-allylamino-17-demethoxygeldanamycin destabilizes the enzyme and dramatically reduces its half-life in primary cultures of endothelial cells
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catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders
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catalyzes the transfer of O-linked GlcNAc to serine/threonine residues of a variety of target proteins, many of which have been implicated in such diseases as diabetes and neurodegeneration
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enzyme transfers N-acetylglucosamine from UDP-GlcNAc to selected serine and threonine residues
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regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
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regulation of O-GlcN acylation over a broad range of glucose concentrations, significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation
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transfer of O-linked GlcNAc to serine/threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders
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enzyme adds a single GlcNAc to hydroxyl groups of serine and threonine residues. Substrates are many proteins, e.g. transcription factors, kinases, cytoskeletal proteins, and nuclear pore proteins
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enzyme catalyzes O-GlcNAc addition
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enzyme catalyzes the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics. OGT protein amounts decrease during M phase
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enzyme is a key molecule for the timely progression of the cell cycle. Microinject recombinant proteins into oocytes to detail the relationship between cell cycle and O-GlcNAc
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enzyme modifies nuclear pore proteins and transcription factors
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enzyme transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor
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enzyme does not modify peptide YSDSGSTST, cAMP-dependent protein kinase A, casein kinase I, mitogen activated protein kinase (extracellular signal-regulated kinase 2), or calmodulin-dependent protein kinase II
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additional information
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UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine is no substrate
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additional information
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heat shock protein 90 (Hsp90) is involved in the regulation of O-linked beta-N-acetylglucosamine transferase. Inhibition of Hsp90 by radicicol or 17-N-allylamino-17-demethoxygeldanamycin destabilizes the enzyme and dramatically reduces its half-life in primary cultures of endothelial cells
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additional information
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heat shock protein 90 (Hsp90) is involved in the regulation of O-linked beta-N-acetylglucosamine transferase. Inhibition of Hsp90 by radicicol or 17-N-allylamino-17-demethoxygeldanamycin destabilizes the enzyme and dramatically reduces its half-life in primary cultures of endothelial cells
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no activity with Tau protein
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no activity with Tau protein
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the enzyme is not able to transfer UDP-glucose or UDP-2-dehydro-alpha-D-glucose to peptide and protein substrates
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a combination of size and conformational restriction defines sequence specificity in the -3 to +2 subsites of O-GlcNAc modification. Although the N-terminal tetratricopeptide repeats of OGT may have roles in substrate recognition, the sequence restriction imposed by the peptide-binding site makes a substantial contribution to O-GlcNAc site specificity
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modification occurs predominantly in a random coil region, with signature sequence, PPVS/TSATT, around the modification site (underlined, position 0). A substrate (peptide or protein) with Pro, Ala at position -2, and/or Val, Ala, Thr, Ser at position -1, and/or Ala, Ser, Pro, Thr, Gly at position +2 would have more chances for O-GlcNAcylation
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the substitution of the N-acyl group, deoxy modification of C6/C4-OH or epimerization of C4-OH of the GlcNAc in UDP-GlcNAc decrease its affinity to isoform short OGT. The backbone carbonyl oxygen of Leu653 and the hydroxyl group of Thr560 in sOGT contribute to the recognition of the sugar moiety via hydrogen bonds
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the substitution of the N-acyl group, deoxy modification of C6/C4-OH or epimerization of C4-OH of the GlcNAc in UDP-GlcNAc decrease its affinity to isoform short OGT. The backbone carbonyl oxygen of Leu653 and the hydroxyl group of Thr560 in sOGT contribute to the recognition of the sugar moiety via hydrogen bonds
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aspartate residues far from the active site drive O-GlcNAc transferase substrate selection
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the enzyme is quite promiscuous for its donor sugar substrates. It can endogenously modify proteins with both N-acetyl-glucosamine and glucose
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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
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no activity with UDP-GalNAc, UDP-D-glucose, UDP-D-galactose, and UDP-D-xylose
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no activity with UDP-GalNAc, UDP-D-glucose, UDP-D-galactose, and UDP-D-xylose
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participates in plum pox virus infection, plants are inoculated with plum pox virus-NK-GFP and observed at different times postinoculation under a fluorescence microscope
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additional information
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catalyses the O-linked attachment of single GlcNAc moieties to serine and threonine residues on many cytosolic or nuclear proteins
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additional information
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catalyzes the attachment of GlcNAc monosaccharides to the hydroxyl group of serine or threonine residues of intracellular proteins and may play an important role in the hexosamine pathway
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enzyme catalyzes the abundant and dynamic posttranslational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc)
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O-GlcNAc transferase, the enzyme that adds O-GlcNAc to proteins, exists in stable and active complexes with the serine/threonine phosphatases PP1beta and PP1gamma, enzymes that remove phosphate from proteins
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p110 subunit of the enzyme forms both homo- and heterotrimers that appear to have different binding affinities for UDP-GlcNAc
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DELTA859 is not able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
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OGT-interacting proteins interact strongly with the tetratricopeptide repeat (TPR) domain of OGT, they are modified by O-GlcNAc and are excellent substrates of OGT
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additional information
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enzyme adds a single GlcNAc to hydroxyl groups of serine and threonine residues
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enzyme is able to hydrolyze UDP-GlcNAc
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enzyme is able to hydrolyze UDP-GlcNAc
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enzyme catalyzes O-GlcNAc addition
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additional information
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enzyme transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor
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additional information
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UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine is no substrate
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(2Z)-2-[(4-chlorophenyl)imino]-4-oxo-3-(2-tricyclo[3.3.1.1(3,7)]dec-1-ylethyl)-1,3-thiazinane-6-carboxylic acid
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donor analogue displacement probes
1-(4-acetamidophenyl)-4-(diphenylhydroxymethyl)-1H-1,2,3-triazole
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1-(4-acetamidophenyl)-4-(naphthalen-2-yl)-1H-1,2,3-triazole
i.e. APNT, cell-permeable inhibitor, able to inhibit OGlcNAcylation in cells without significant effects on cell viability
1-(4-acetamidophenyl)-4-([1,1'-biphenyl]-4-yl)-1H-1,2,3-triazole
i.e. APBT, cell-permeable inhibitor, able to inhibit OGlcNAcylation in cells without significant effects on cell viability
1-(4-chloroacetamidophenyl)-4-(diphenylhydroxymethyl)-1H-1,2,3-triazole
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1-(4-chloroacetamidophenyl)-4-(naphthalen-2-yl)-1H-1,2,3-triazole
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1-(4-chloroacetamidophenyl)-4-([1,1'-biphenyl]-4-yl)-1H-1,2,3-triazole
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2,4,5,6-tetraoxypyrimidine
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3-(2-adamantanylethyl)-2-[(4-chlorophenyl)azamethylene]-4-oxo-1,3-thiazaperhydroine-6-carboxylic acid
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3-(4-cyanobenzylthio)-1-(thiophen-2-yl)-5,6,7,8-tetrahydroisoquinoline-4-carboxylic acid
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donor analogue displacement probes
3-[2-adamantanylethyl]-2-[[4-chlorophenyl]azamethylene]-4-oxo-1,3-thiazaperhyd roine-6-carboxylic acid
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endothelin 1 effects are not observed when vessels are previously instilled with anti-O-GlcNAc transferase antibody or after incubation with an O-GlcNAc transferase inhibitor (100 microMol)
4-methoxyphenyl 5-acetyl-3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
the compound fully inactivates the enzyme within 5 min at a 1:1 ratio of inhibitor:enzyme
4-methoxyphenyl 6-acetyl-2-oxobenzo[d]oxazole-3(2H)-carboxylate
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4-methoxyphenyl 6-chloro-3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
about 30% inhibition with a 3fold excess of inhibitor
5'-O-(hydroxy[3-[(2R,3R)-3-hydroxypyrrolidin-2-yl]propyl]phosphoryl)uridine
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5'-O-(hydroxy[3-[(2R,3R,4S,5R)-3,4,5-trihydroxypyrrolidin-2-yl]propyl]phosphoryl)uridine
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5'-O-(hydroxy[3-[(2R,3R,4S,5R)-3,4,5-tris(benzyloxy)pyrrolidin-2-yl]propyl]phosphoryl)uridine
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5'-O-[hydroxy(phosphonomethyl)phosphoryl]uridine
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non-hydrolysable alpha,beta-methylene bisphosphonate analogue with the diphosphate oxygen replaced by a methylene group
5'-O-[[(2-(N-acetyl-akoga-D-glucosaminopyranosyl)-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
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5'-O-[[(2-(N-acetyl-beta-D-glucosaminopyranosyl)-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
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5'-O-[[(2-alpha-D-glucopyranosyl-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
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5'-O-[[(2-beta-D-glucopyranosyl-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
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5'-O-[[3-(alpha-D-glucopyranosyl)propyl](hydroxy)phosphoryl]uridine
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5'-O-[[3-(N-acetyl-alpha-D-glucosaminopyranosyl)propyl](hydroxy)phosphoryl]uridine
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5'-O-[[3-[(2R,3R)-3-(benzyloxy)pyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
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5'-O-[[3-[(2R,3S,4S)-3,4-bis(benzyloxy)pyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
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5'-O-[[3-[(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
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5'-O-[[3-[(2S,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
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ATP
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has a much lower affinity for OGT
benzyl-2-acetamido-2-deoxy-alpha-D-galactopyranoside
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ethyl (R)-4-(2-(2-((2-ethoxy-2-oxoethyl)(thiophen-2-ylmethyl)amino)-2-oxo-1-((2-oxo-1,2-dihydroquinoline)-6-sulfonamido)ethyl)phenoxy)butanoate
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ethyl (R)-N-(2-((7-chloro-2-oxo-1,2-dihydroquinoline)-6-sulfonamido)-2-(2-methoxyphenyl)acetyl)-N-(thiophen-2-ylmethyl)glycinate
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GlcNAc
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inhibited by GlcNAc, but not by GalNAc
goblin1
bisubstrate-linked inhibitor in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring. Goblin1 co-crystallizes with OGT, revealing an ordered C3 linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates
methyl (R)-N-(2-(2-methoxyphenyl)-2-((2-oxo-1,2-dihydroquinoline)-6-sulfonamido)acetyl)-N-(thiophen-2-ylmethyl)glycinate
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O-(2-acetamido-2-deoxy-D-glucopyranosylidene) amino N-phenylcarbamate
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phenyl 3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
about 70% inhibition with a 3fold excess of inhibitor
phenyl 3-hydroxy-5-methoxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
about 10% inhibition with a 3fold excess of inhibitor
phenyl 3-hydroxy-5-nitro-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
about 60% inhibition with a 3fold excess of inhibitor
phenyl 6-chloro-2-oxobenzo[d]oxazole-3(2H)-carboxylate
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donor analogue displacement probes
phenyl 6-chloro-3-hydroxy-2-oxo-2,3-dihydro-1H-indole-1-carboxylate
the compound causes an irreversible loss of enzyme activity, about 48% inhibition with a 3fold excess of inhibitor
thiouridine diphosphate
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SUDP
UDP-1-deoxy-1-methylene-N-acetyl-alpha-D-glucosamine
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine
UDP-5-thio-N-acetyl-alpha-D-glucosamine
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UDP-galactose
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much lower affinity for OGT compared with UDP-GlcNAc
UDP-GalNAc
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UMP and UDP-GalNAc are 100fold less potent than UDP, UTP, and UDP-GlcNAc
UDP-glucose
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much lower affinity for OGT compared with UDP-GlcNAc
UDP-N-acetyl-5-deoxy-5-thio-alpha-D-glucosamine
effective inhibitor
UMP
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UMP and UDP-GalNAc are 100fold less potent than UDP, UTP, and UDP-GlcNAc
uridine 5'-[[(2-acetylamino-5-hydroxymethyl-benzyl)-phosphono]phosphate]
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designed to mimic the transition state of the natural donor involved in the enzymatic reaction. The analogue shows low activity as an inhibitor
alloxan
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alloxan
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low micromolar inhibitor
KCl
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50 mM causes 66% inhibition
KCl
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lowers OGT activity by reducing enzyme affinity for UDP-GlcNAc
NaCl
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50 mM causes 66% inhibition
UDP
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completely inhibiting
UDP
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UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
UDP-1-deoxy-1-methylene-N-acetyl-alpha-D-glucosamine
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weak hOGT inhibitor
UDP-1-deoxy-1-methylene-N-acetyl-alpha-D-glucosamine
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binds weakly
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine
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a sub-millimolar inhibitor of hOGT and substrate binding probe
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine
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binds weakly
UDP-GlcNAc
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UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
UDP-S-GlcNAc
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UTP
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UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
UTP
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has a high affinity for OGT
additional information
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testing UDP-GlcNAc/UDP analogues and evaluate their inhibitory properties and structural binding modes in vitro. These analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation
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additional information
not inhibited by EDTA
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additional information
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not inhibited by EDTA
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additional information
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the isolated tetratricopeptide repeat domain of OGT competitively inhibits glycosylation of the OID protein, but does not inhibit glycosylation of small peptides, providing kinetic evidence for the role of the tetratricopeptide repeat domain as a protein substrate docking site
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additional information
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testing UDP-GlcNAc/UDP analogues and evaluate their inhibitory properties and structural binding modes in vitro. These analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation
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Adenocarcinoma of Lung
High O-linked N-acetylglucosamine transferase expression predicts poor survival in patients with early stage lung adenocarcinoma.
Alzheimer Disease
Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain.
Alzheimer Disease
Early and Persistent O-GlcNAc Protein Modification in the Streptozotocin Model of Alzheimer's Disease.
Alzheimer Disease
Loss of O-GlcNAc glycosylation in forebrain excitatory neurons induces neurodegeneration.
Alzheimer Disease
The mitochondrial O-linked N-acetylglucosamine transferase (mOGT) in the diabetic patient could be the initial trigger to develop Alzheimer disease.
Alzheimer Disease
UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme.
Breast Neoplasms
O-GlcNAc Transferase Inhibition Differentially Affects Breast Cancer Subtypes.
Carcinogenesis
Formal modeling and analysis of the hexosamine biosynthetic pathway: role of O-linked N-acetylglucosamine transferase in oncogenesis and cancer progression.
Carcinogenesis
O-linked N-acetylglucosamine transferase enhances secretory clusterin expression via liver X receptors and sterol response element binding protein regulation in cervical cancer.
Carcinogenesis
O-linked N-acetylglucosamine transferase promotes cervical cancer tumorigenesis through human papillomaviruses E6 and E7 oncogenes.
Carcinoma
A common sugar-nucleotide-mediated mechanism of inhibition of (glycosamino)glycan biosynthesis, as evidenced by 6F-GalNAc (Ac3).
Carcinoma
Critical role of O-GlcNAc transferase in prostate cancer invasion, angiogenesis and metastasis.
Carcinoma
MicroRNAs MiR-15a and MiR-26a cooperatively regulate O-GlcNAc-transferase to control proliferation in clear cell renal cell carcinoma.
Carcinoma
O-GlcNAcylation is associated with the development and progression of gastric carcinoma.
Carcinoma
O-linked N-acetylglucosamine transferase (OGT) is overexpressed and promotes O-linked protein glycosylation in esophageal squamous cell carcinoma.
Carcinoma, Hepatocellular
O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E.
Carcinoma, Renal Cell
MicroRNAs MiR-15a and MiR-26a cooperatively regulate O-GlcNAc-transferase to control proliferation in clear cell renal cell carcinoma.
Cardiovascular Diseases
Shaken, not stirred: bioanalytical study of the antioxidant activities of martinis.
Cataract
Shaken, not stirred: bioanalytical study of the antioxidant activities of martinis.
Cholangiocarcinoma
Overexpression of O-GlcNAc-Transferase Associates with Aggressiveness of Mass-Forming Cholangiocarcinoma.
Colorectal Neoplasms
Identification of an HLA-A0201-restricted CTL epitope generated by a tumor-specific frameshift mutation in a coding microsatellite of the OGT gene.
Diabetes Complications
Increased OGA Expression and Activity in Leukocytes from Patients with Diabetes: Correlation with Inflammation Markers.
Diabetes Complications
Insights into the role of maladaptive hexosamine biosynthesis and O-GlcNAcylation in development of diabetic cardiac complications.
Diabetes Mellitus
O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats.
Diabetic Nephropathies
O-linked N-acetylglucosaminyltransferase OGT inhibits diabetic nephropathy by stabilizing histone methyltransferases EZH2 via the HES1/PTEN axis.
Esophageal Neoplasms
Downregulation of O-linked N-acetylglucosamine transferase by RNA interference decreases MMP9 expression in human esophageal cancer cells.
Esophageal Neoplasms
MiRNA-485-5p, inhibits esophageal cancer cells proliferation and invasion by down-regulating O-linked N-acetylglucosamine transferase.
Esophageal Squamous Cell Carcinoma
O-linked N-acetylglucosamine transferase (OGT) is overexpressed and promotes O-linked protein glycosylation in esophageal squamous cell carcinoma.
Hepatitis C
Functional microRNA screen uncovers O-linked N-acetylglucosamine transferase as a host factor modulating hepatitis C virus morphogenesis and infectivity.
Herpes Simplex
Inhibition of O-Linked N-Acetylglucosamine Transferase Reduces Replication of Herpes Simplex Virus and Human Cytomegalovirus.
Infections
Human metapneumovirus infection of airway epithelial cells is associated with changes in core metabolic pathways.
Infections
SECRET AGENT, an Arabidopsis thaliana O-GlcNAc transferase, modifies the Plum pox virus capsid protein.
Insulin Resistance
Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia.
Insulin Resistance
Enhanced O-GlcNAc protein modification is associated with insulin resistance in GLUT1-overexpressing muscles.
Insulin Resistance
Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity.
Insulin Resistance
Insights into the role of maladaptive hexosamine biosynthesis and O-GlcNAcylation in development of diabetic cardiac complications.
Insulin Resistance
O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes.
Insulin Resistance
Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 adipocytes.
Intellectual Disability
Disease related single point mutations alter the global dynamics of a tetratricopeptide (TPR) ?-solenoid domain.
Kidney Diseases
Endothelial Dysfunction: The Secret Agent Driving Kidney Disease.
Liver Cirrhosis
O-GlcNAcylation inhibits hepatic stellate cell activation.
Liver Neoplasms
Regulation of miR-483-3p by the O-linked N-acetylglucosamine transferase links chemosensitivity to glucose metabolism in liver cancer cells.
Lymphatic Metastasis
Cyclin Y regulates the proliferation, migration, and invasion of ovarian cancer cells via Wnt signaling pathway.
Malaria
Studies on O-glycans of Plasmodium-falciparum-infected human erythrocytes. Evidence for O-GlcNAc and O-GlcNAc-transferase in malaria parasites.
Neoplasm Metastasis
Cyclin Y regulates the proliferation, migration, and invasion of ovarian cancer cells via Wnt signaling pathway.
Neoplasm Metastasis
OGT regulated O-GlcNAcylation promotes papillary thyroid cancer malignancy via activating YAP.
Neoplasms
Cyclin Y regulates the proliferation, migration, and invasion of ovarian cancer cells via Wnt signaling pathway.
Neoplasms
Formal modeling and analysis of the hexosamine biosynthetic pathway: role of O-linked N-acetylglucosamine transferase in oncogenesis and cancer progression.
Neoplasms
HINCUTs in cancer: hypoxia-induced noncoding ultraconserved transcripts.
Neoplasms
Normalizing glucose levels reconfigures the mammary tumor immune and metabolic microenvironment and decreases metastatic seeding.
Neoplasms
O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation.
Neoplasms
O-GlcNAc Transferase Inhibition Differentially Affects Breast Cancer Subtypes.
Neoplasms
O-GlcNAcylation is associated with the development and progression of gastric carcinoma.
Neoplasms
O-Linked N-Acetylglucosamine (O-GlcNAc) Expression Levels Epigenetically Regulate Colon Cancer Tumorigenesis by Affecting the Cancer Stem Cell Compartment via Modulating Expression of Transcriptional Factor MYBL1.
Neoplasms
O-linked N-acetylglucosamine transferase enhances secretory clusterin expression via liver X receptors and sterol response element binding protein regulation in cervical cancer.
Neoplasms
OGT regulated O-GlcNAcylation promotes papillary thyroid cancer malignancy via activating YAP.
Neuroblastoma
A?-affected pathogenic induction of S-nitrosylation of OGT and identification of Cys-NO linkage triplet.
Neurodegenerative Diseases
Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain.
Neurodegenerative Diseases
Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc).
Neurodegenerative Diseases
Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
Osteosarcoma
Relationship Between O-GlcNAcase Expression and Prognosis of Patients With Osteosarcoma.
phosphomannomutase deficiency
Carbohydrate-deficient glycoprotein syndrome.
Prostatic Neoplasms
Critical role of O-GlcNAc transferase in prostate cancer invasion, angiogenesis and metastasis.
Renal Insufficiency
Silencing of O-linked N-acetylglucosamine transferase ameliorates hypercalcemia-induced neurotoxicity in renal failure by regulating EZH2/KLF2/CXCL1 axis.
Starvation
ULK1 O-GlcNAcylation Is Crucial for Activating VPS34 via ATG14L during Autophagy Initiation.
Stomach Neoplasms
Silencing ?-linked N-acetylglucosamine transferase induces apoptosis in human gastric cancer cells through PUMA and caspase-3 pathways.
Stroke
Shaken, not stirred: bioanalytical study of the antioxidant activities of martinis.
Thyroid Cancer, Papillary
OGT regulated O-GlcNAcylation promotes papillary thyroid cancer malignancy via activating YAP.
Uterine Cervical Neoplasms
O-linked N-acetylglucosamine transferase enhances secretory clusterin expression via liver X receptors and sterol response element binding protein regulation in cervical cancer.
Uterine Cervical Neoplasms
O-linked N-acetylglucosamine transferase promotes cervical cancer tumorigenesis through human papillomaviruses E6 and E7 oncogenes.
Virus Diseases
Identification of secret agent as the O-GlcNAc transferase that participates in Plum pox virus infection.
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sec spy double mutant
double-mutant embryos aborted at various stages of development and no double-mutant seedlings are obtained. These results indicate that OGT activity is required during gametogenesis and embryogenesis with lethality occurring when parentally derived SEC, SPY, and/or O-GlcNAcylated proteins become limiting
sec-1
has a tDNA insertion within the exon encoding the ninth tetratricopeptide repeat, no obvious phenotype. Two SEC tDNA insertional mutants are identified and analyzed. sec mutant plants do not exhibit obvious phenotypes, sec and spy mutations have a synthetic lethal interaction
sec-2
contains an insertion within an intron adjacent to exons encoding the putative catalytic portion of the protein, no obvious phenotype. Two SEC tDNA insertional mutants are identified and analyzed. sec mutant plants do not exhibit obvious phenotypes, sec and spy mutations have a synthetic lethal interaction
spy-3
Columbia (Col-0) background, has a Gly-to-Ser substitution in the C-terminal region of the protein. The spy plants have defects in a number of processes, including gibberellin and cytokinin responses, flowering, circadian regulation, and light inhibition of hypocotyls elongation
H537A
5.6% of wild-type activity
H596F
3.0% of wild-type activity
K872M
mutation of a key catalytic lysine, crystallized in complex with the inhibitor/substrate analogue UDP-5S-GlcNAc. Inactive
C835A
the mutation has no effect compared with wild type enzyme
C836S
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
C839S
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
D368A
activity is identical to wild-type enzyme
D386A/D420A
activity is 190% compared to wild-type enzyme
D386A/D420A/D454A
activity is 170% compared to wild-type enzyme
D407A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D4209A/D454A
activity is 80% compared to wild-type enzyme
D420A
activity is 130% compared to wild-type enzyme
D422A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I, produces a 50-100% increase in activity
D431A
single-point mutation, peptide-binding mutant
D438A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D454A
activity is 130% compared to wild-type enzyme
D488A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D505A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D549A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D554A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
D925N
single-point mutation, UDP-GlcNAc-binding mutant
DELTAN-DELTAKEN-FoxM1
-
O-GlcNAcation required the N terminus
E482A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
E556A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
E568A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F439A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F460A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
F721A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
F752A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 110% activity compared to wild type
F776A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, 10% activity compared to wild type
G402S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G453S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G472A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
G538S
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
H498A
single-point mutation, peptide-binding mutant
H558A
-
active site mutant
H558D
-
active site mutant
H558E
-
active site mutant
H901Y
-
active site mutant
H920A
-
active site mutant, deleterious
K842M
single-point mutation, UDP-GlcNAc-binding mutant
L796A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
N458A
single-point mutation, peptide-binding mutant
ncOGT
-
long OGT isoform, nucleocytoplasmic OGT, microinjected into immature oocytes prior to progesterone incubation
Q839A
single-point mutation, UDP-GlcNAc-binding mutant
Q839E
-
active site mutant
Q839N
-
active site mutant, low specific activity
R637A
single-point mutation, peptide-binding mutant
S18A/H127A
OGlcNAcylation on the mutant enzyme sharply declines
S52A
O-GlcNAcylation on the mutant enzyme increases
S56A
O-GlcNAcylation on the mutant enzyme increases
sOGT
-
N-terminally truncated isoform, short OGT, microinjected into immature oocytes prior to progesterone incubation
T12A
O-GlcNAcylation on the mutant enzyme declines
T12A/H127A
OGlcNAcylation on the mutant enzyme sharply declines
T12G
sharply reduced O-GlcNAcylation of short-form O-GlcNAc transferase
T12L
sharply reduced O-GlcNAcylation of short-form O-GlcNAc transferase
T12Y
sharply reduced O-GlcNAcylation of short-form O-GlcNAc transferase
T560A
single-point mutation, UDP-GlcNAc-binding mutant
W536A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
W735A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W748A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W812A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
W878A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD II, less than 1% activity compared to wild type
Y387A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I, mutation is not included for enzymatic analysis, because not sufficient amounts of protein could be produced
Y434A
-
site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
Y539A
-
significant inhibitory effect on OGT enzyme activity, site-directed mutagenesis to target potentially important amino acid residues within the conserved catalytic domain CD I
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
DELTA2.5OGT
-
Baculovirus-produced recombinant, is partially active toward the OID protein substrate, but is fully active toward the CKII peptide substrate
DELTA5.5OGT
-
Baculovirus-produced recombinant
full-length OGT
-
Baculovirus-produced recombinant
G350D
mutation corresponds to G570D mutation in Arabidopsis thaliana, results in plants with altered hormone responses, does not rescue the settling phenotype of the OGT deletion strain
H280A
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
K445A
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
G350D
-
mutation corresponds to G570D mutation in Arabidopsis thaliana, results in plants with altered hormone responses, does not rescue the settling phenotype of the OGT deletion strain
-
H280A
-
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
-
K445A
-
mutation in residue corresponding to His residue in the human enzyme predicted to be important in the transfer of GlcNAc to substrates, does not rescue the settling phenotype of the OGT deletion strain
-
C917A
active site mutant
C917A
-
mutant efficiently transfers diazirine-modified GlcNDAz and has altered substrate specificity, preferring to transfer GlcNDAz rather than GlcNAc to protein substrates
D925A
-
active site mutant
D925A
single-point mutation, UDP-GlcNAc-binding mutant
K842A
active site mutant
K842A
-
active site mutant, low specific activity
K898A
-
active site mutant, Lys898, which is involved in uracil binding, mutation results in a protein with no apparent activity
K898A
single-point mutation, UDP-GlcNAc-binding mutant
T921A
active site mutant
T921A
-
active site mutant, 18% activity compared to wild-type
Y841A
-
active site mutant, lowers specific activity to 24% compared to wild-type
Y841A
the mutation has no effect compared with wild type enzyme
additional information
-
deletional or disrupting mutation of the Spindly SPY locus affects the enzyme and the plant signaling, e.g. increased gibberillin signaling, altered phenotypes
additional information
deletion mapping and site-directed mutagenesis identified three threonine and a serine located near the N-terminus of PPV-CP that are modified by SEC
additional information
deletion mapping and site-directed mutagenesis identified three threonine and a serine located near the N-terminus of PPV-CP that are modified by SEC
additional information
-
deletion mapping and site-directed mutagenesis identified three threonine and a serine located near the N-terminus of PPV-CP that are modified by SEC
additional information
plum pox virus is able to infect the Arabidopsis OGT mutants sec-1, sec-2, and spy-3, but at early times of the infection, both rate of virus spread and accumulation are reduced in sec-1 and sec-2 relative to spy-3 and wild-type plants
additional information
plum pox virus is able to infect the Arabidopsis OGT mutants sec-1, sec-2, and spy-3, but at early times of the infection, both rate of virus spread and accumulation are reduced in sec-1 and sec-2 relative to spy-3 and wild-type plants
additional information
-
plum pox virus is able to infect the Arabidopsis OGT mutants sec-1, sec-2, and spy-3, but at early times of the infection, both rate of virus spread and accumulation are reduced in sec-1 and sec-2 relative to spy-3 and wild-type plants
additional information
sec-1, Wassilewskija background, T-DNA is inserted into the tetratricopeptide repeat domain, no obvious phenotype
additional information
sec-1, Wassilewskija background, T-DNA is inserted into the tetratricopeptide repeat domain, no obvious phenotype
additional information
-
sec-1, Wassilewskija background, T-DNA is inserted into the tetratricopeptide repeat domain, no obvious phenotype
additional information
sec-2, Columbia (Col-0) background. T-DNA is inserted into an intron adjacent to exons coding for the putative catalytic region of the protein, no obvious phenotype
additional information
sec-2, Columbia (Col-0) background. T-DNA is inserted into an intron adjacent to exons coding for the putative catalytic region of the protein, no obvious phenotype
additional information
-
sec-2, Columbia (Col-0) background. T-DNA is inserted into an intron adjacent to exons coding for the putative catalytic region of the protein, no obvious phenotype
additional information
-
following mutations are not included for enzymatic analysis, because not sufficient amounts of protein could be produced: Y387A, F439A, D505A, W536A, Y539A, D549A, D554A, and E556A
additional information
-
site-directed mutagenesis to target potentially important amino acid residues within the two conserved catalytic domains of OGT (CD I and CD II), followed by an in vitro glycosylation assay to evaluate N-acetylglucosaminyltransferase activity after bacterial expression
additional information
-
deletion mutants of OGT variant A-G. Deletions in the highly conserved C-terminus result in a complete loss of activity. The N-terminal tetratricopeptide repeat domain is required for optimal recognition of substrates. Removal of the first three tetratricopeptide repeats greatly reduces the O-GlcNAc addition to macromolecular substrates
additional information
-
deletion of the first 3 tetratricopeptide repeats in clone B results in a significant loss of activity (58%) for Nup 62
additional information
-
removal of the first 6 tetratricopeptide repeats in clone C results in an almost complete loss of activity toward Nup 62 as a substrate
additional information
shorter OGT p78 splice form
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Haltiwanger, R.S.; Blomberg, M.A.; Hart, G.W.
Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase
J. Biol. Chem.
267
9005-9013
1992
Rattus norvegicus
brenda
Kreppel, L.K.; Blomberg, M.A.; Hart, G.W.
Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
J. Biol. Chem.
272
9308-9315
1997
Rattus norvegicus (P56558)
brenda
Roos, M.D.; Hanover, J.A.
Structure of O-linked GlcNAc transferase: Mediator of glycan-dependent signaling
Biochem. Biophys. Res. Commun.
271
275-280
2000
Arabidopsis thaliana, Homo sapiens, no activity in Saccharomyces cerevisiae, no activity in Escherichia coli, Rhodobacter sp.
brenda
Lubas, W.A.; Hanover, J.A.
Functional expression of O-linked GlcNAc transferase: domain structure and substrate specificity
J. Biol. Chem.
275
10983-10988
2000
Homo sapiens
brenda
Konrad, R.J.; Tolar, J.F.; Hale, J.E.; Knierman, M.D.; Becker, G.W.; Kudlow, J.E.
Purification of the O-glycosylated protein p135 and identification as O-GlcNAc transferase
Biochem. Biophys. Res. Commun.
288
1136-1140
2001
Rattus norvegicus
brenda
Andrali, S.S.; Marz, P.; Ozcan, S.
Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic beta cells
Biochem. Biophys. Res. Commun.
337
149-153
2005
Homo sapiens
brenda
Akimoto, Y.; Comer, F.I.; Cole, R.N.; Kudo, A.; Kawakami, H.; Hirano, H.; Hart, G.W.
Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex
Brain Res.
966
194-205
2003
Rattus norvegicus
brenda
Zachara, N.E.; O'Donnell, N.; Cheung, W.D.; Mercer, J.J.; Marth, J.D.; Hart, G.W.
Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress: A survival response of mammalian cells
J. Biol. Chem.
279
30133-30142
2004
Chlorocebus aethiops
brenda
Wells, L.; Kreppel, L.K.; Comer, F.I.; Wadzinski, B.E.; Hart, G.W.
O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits
J. Biol. Chem.
279
38466-38470
2004
Rattus norvegicus
brenda
Lazarus, B.D.; Roos, M.D.; Hanover, J.A.
Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase
J. Biol. Chem.
280
35537-35544
2005
Homo sapiens
brenda
Chen, D.; Juarez, S.; Hartweck, L.; Alamillo, J.M.; Simon-Mateo, C.; Perez, J.J.; Fernandez-Fernandez, M.R.; Olszewski, N.E.; Garcia, J.A.
Identification of secret agent as the O-GlcNAc transferase that participates in Plum pox virus infection
J. Virol.
79
9381-9387
2005
Nicotiana benthamiana, Arabidopsis thaliana (Q96301), Arabidopsis thaliana (Q9M8Y0), Arabidopsis thaliana
brenda
Scott, C.L.; Hartweck, L.M.; de Jesus Perez, J.; Chen, D.; Garcia, J.A.; Olszewski, N.E.
SECRET AGENT, an Arabidopsis thaliana O-GlcNAc transferase, modifies the Plum pox virus capsid protein
FEBS Lett.
580
5829-5835
2006
Arabidopsis thaliana (Q96301), Arabidopsis thaliana (Q9M8Y0), Arabidopsis thaliana
brenda
Maerz, P.; Stetefeld, J.; Bendfeldt, K.; Nitsch, C.; Reinstein, J.; Shoeman, R.L.; Dimitriades-Schmutz, B.; Schwager, M.; Leiser, D.; Ozcan, S.; Otten, U.; Ozbek, S.
Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain
J. Biol. Chem.
281
20263-20270
2006
Homo sapiens (O15294), Rattus norvegicus (P56558)
brenda
Dehennaut, V.; Hanoulle, X.; Bodart, J.F.; Vilain, J.P.; Michalski, J.C.; Landrieu, I.; Lippens, G.; Lefebvre, T.
Microinjection of recombinant O-GlcNAc transferase potentiates Xenopus oocytes M-phase entry
Biochem. Biophys. Res. Commun.
369
539-546
2008
Homo sapiens
brenda
Clarke, A.J.; Hurtado-Guerrero, R.; Pathak, S.; Schuettelkopf, A.W.; Borodkin, V.; Shepherd, S.M.; Ibrahim, A.F.; van Aalten, D.M.
Structural insights into mechanism and specificity of O-GlcNAc transferase
EMBO J.
27
2780-2788
2008
Xanthomonas campestris, Homo sapiens (O15294)
brenda
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
brenda
Martinez-Fleites, C.; Macauley, M.S.; He, Y.; Shen, D.L.; Vocadlo, D.J.; Davies, G.J.
Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
Nat. Struct. Mol. Biol.
15
764-765
2008
Homo sapiens, Xanthomonas campestris
brenda
Akimoto, Y.; Kreppel, L.K.; Hirano, H.; Hart, G.W.
Hyperglycemia and the O-GlcNAc transferase in rat aortic smooth muscle cells: elevated expression and altered patterns of O-GlcNAcylation
Arch. Biochem. Biophys.
389
166-175
2001
Rattus norvegicus (P56558)
brenda
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
brenda
Yang, W.H.; Park, S.Y.; Ji, S.; Kang, J.G.; Kim, J.-E.; Song, H.; Mook-Jung, I.; Choe, K.-M.; Cho, J.W.
O-GlcNAcylation regulates hyperglycemia-induced GPX1 activation
Biochem. Biophys. Res. Commun.
391
756-761
2010
Homo sapiens
brenda
Zhang, L.; Ren, F.; Li, J.; Ma, X.; Wang, P.
A modified coupled enzyme method for O-linked GlcNAc transferase activity assay
Biol. Proced. Online
11
170-183
2009
Homo sapiens
brenda
Webster, D.M.; Teo, C.F.; Sun, Y.; Wloga, D.; Gay, S.; Klonowski, K.D.; Wells, L.; Dougan, S.T.
O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development
BMC Dev. Biol.
9
28
2009
Danio rerio (Q5GA10), Danio rerio (Q5GA12)
brenda
Akimoto, Y.; Kreppel, L.K.; Hirano, H.; Hart, G.W.
Localization of the O-linked N-acetylglucosamine transferase in rat pancreas
Diabetes
48
2407-2413
1999
Rattus norvegicus (P56558)
brenda
Golks, A.; Tran, T.T.; Goetschy, J.F.; Guerini, D.
Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation
EMBO J.
26
4368-4379
2007
Homo sapiens
brenda
Dieckmann-Schuppert, A.; Bause, E.; Schwarz, R.T.
Studies on O-glycans of Plasmodium-falciparum-infected human erythrocytes. Evidence for O-GlcNAc and O-GlcNAc-transferase in malaria parasites
Eur. J. Biochem.
216
779-788
1993
Homo sapiens
brenda
Hartweck, L.M.; Scott, C.L.; Olszewski, N.E.
Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development
Genetics
161
1279-1291
2002
Arabidopsis thaliana (Q9M8Y0), Arabidopsis thaliana
brenda
Lazarus, B.D.; Love, D.C.; Hanover, J.A.
Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates
Glycobiology
16
415-421
2006
Homo sapiens
brenda
Lima, V.V.; Giachini, F.R.; Carneiro, F.S.; Carneiro, Z.N.; Saleh, M.A.; Pollock, D.M.; Fortes, Z.B.; Carvalho, M.H.; Ergul, A.; Webb, R.C.; Tostes, R.C.
O-GlcNAcylation contributes to augmented vascular reactivity induced by endothelin 1
Hypertension
55
180-188
2010
Rattus norvegicus
brenda
Gross, B.J.; Kraybill, B.C.; Walker, S.
Discovery of O-GlcNAc transferase inhibitors
J. Am. Chem. Soc.
127
14588-14589
2005
Homo sapiens
brenda
Kreppel, L.K.; Hart, G.W.
Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
J. Biol. Chem.
274
32015-32022
1999
Rattus norvegicus
brenda
Gao, Y.; Wells, L.; Comer, F.I.; Parker, G.J.; Hart, G.W.
Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain
J. Biol. Chem.
276
9838-9845
2001
Bos taurus
brenda
Iyer, S.P.; Hart, G.W.
Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
J. Biol. Chem.
278
24608-24616
2003
Rattus norvegicus
brenda
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
brenda
Taylor, R.P.; Parker, G.J.; Hazel, M.W.; Soesanto, Y.; Fuller, W.; Yazzie, M.J.; McClain, D.A.
Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase
J. Biol. Chem.
283
6050-6057
2008
Homo sapiens
brenda
Okuyama, R.; Marshall, S.
UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme
J. Neurochem.
86
1271-1280
2003
Rattus norvegicus
brenda
Caldwell, S.A.; Jackson, S.R.; Shahriari, K.S.; Lynch, T.P.; Sethi, G.; Walker, S.; Vosseller, K.; Reginato, M.J.
Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
Oncogene
29
2831-2842
2010
Homo sapiens
brenda
Dorfmueller, H.C.; Borodkin, V.S.; Blair, D.E.; Pathak, S.; Navratilova, I.; van Aalten, D.M.
Substrate and product analogues as human O-GlcNAc transferase inhibitors
Amino Acids
40
781-972
2011
Homo sapiens
brenda
Dorfmueller, H.C.; Borodkin, V.S.; Blair, D.E.; Pathak, S.; Navratilova, I.; van Aalten, D.M.
Substrate and product analogues as human O-GlcNAc transferase inhibitors
Amino Acids
40
781-792
2010
Xanthomonas campestris pv. campestris
brenda
Lubas, W.A.; Frank, D.W.; Krause, M.; Hanover, J.A.
O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
J. Biol. Chem.
272
9316-9324
1997
Caenorhabditis elegans, Oryctolagus cuniculus, Homo sapiens (O15294), Homo sapiens
brenda
Sakabe, K.; Hart, G.W.
O-GlcNAc transferase regulates mitotic chromatin dynamics
J. Biol. Chem.
285
34460-34468
2010
Homo sapiens
brenda
Zhang, F.; Snead, C.M.; Catravas, J.D.
Hsp90 regulates O-linked beta-N-acetylglucosamine transferase: a novel mechanism of modulation of protein O-linked beta-N-acetylglucosamine modification in endothelial cells
Am. J. Physiol. Cell Physiol.
302
C1786-C1796
2012
Bos taurus, Homo sapiens (O15294), Homo sapiens
brenda
Chikanishi, T.; Fujiki, R.; Hashiba, W.; Sekine, H.; Yokoyama, A.; Kato, S.
Glucose-induced expression of MIP-1 genes requires O-GlcNAc transferase in monocytes
Biochem. Biophys. Res. Commun.
394
865-870
2010
Homo sapiens (O15294)
brenda
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
brenda
Ruan, H.B.; Han, X.; Li, M.D.; Singh, J.P.; Qian, K.; Azarhoush, S.; Zhao, L.; Bennett, A.M.; Samuel, V.T.; Wu, J.; Yates, J.R.; Yang, X.
O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1alpha stability
Cell Metab.
16
226-237
2012
Homo sapiens (O15294)
brenda
Capotosti, F.; Guernier, S.; Lammers, F.; Waridel, P.; Cai, Y.; Jin, J.; Conaway, J.W.; Conaway, R.C.; Herr, W.
O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1
Cell
144
376-388
2011
Homo sapiens (O15294)
brenda
Tvaroska, I.; Kozmon, S.; Wimmerova, M.; Koca, J.
Substrate-assisted catalytic mechanism of O-GlcNAc transferase discovered by quantum mechanics/molecular mechanics investigation
J. Am. Chem. Soc.
134
15563-15571
2012
Homo sapiens (O15294)
brenda
Shen, D.L.; Gloster, T.M.; Yuzwa, S.A.; Vocadlo, D.J.
Insights into O-linked N-acetylglucosamine (O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates
J. Biol. Chem.
287
15395-15408
2012
Homo sapiens (O15294), Homo sapiens
brenda
Gawlowski, T.; Suarez, J.; Scott, B.; Torres-Gonzalez, M.; Wang, H.; Schwappacher, R.; Han, X.; Yates, J.R.; Hoshijima, M.; Dillmann, W.
Modulation of dynamin-related protein 1 (DRP1) function by increased O-linked-beta-N-acetylglucosamine modification (O-GlcNAc) in cardiac myocytes
J. Biol. Chem.
287
30024-30034
2012
Rattus norvegicus (P56558)
brenda
Iwashita, Y.; Fukuchi, N.; Waki, M.; Hayashi, K.; Tahira, T.
Genome-wide repression of NF-kappaB target genes by transcription factor MIBP1 and its modulation by O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase
J. Biol. Chem.
287
9887-9900
2012
Homo sapiens (O15294)
brenda
Jiang, J.; Lazarus, M.B.; Pasquina, L.; Sliz, P.; Walker, S.
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
Nat. Chem. Biol.
8
72-77
2012
Homo sapiens (O15294), Homo sapiens
brenda
Lazarus, M.B.; Jiang, J.; Gloster, T.M.; Zandberg, W.F.; Whitworth, G.E.; Vocadlo, D.J.; Walker, S.
Structural snapshots of the reaction coordinate for O-GlcNAc transferase
Nat. Chem. Biol.
8
966-968
2012
Homo sapiens (O15294)
brenda
Lazarus, M.; Nam, Y.; Jiang, J.; Sliz, P.; Walker, S.
Structure of human O-GlcNAc transferase and its complex with a peptide substrate
Nature
469
564-569
2011
Homo sapiens (O15294), Homo sapiens
brenda
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
brenda
Liu, Y.; Li, X.; Yu, Y.; Shi, J.; Liang, Z.; Run, X.; Li, Y.; Dai, C.L.; Grundke-Iqbal, I.; Iqbal, K.; Liu, F.; Gong, C.X.
Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain
PLoS ONE
7
e43724
2012
Rattus norvegicus (P56558)
brenda
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
brenda
Borodkin, V.S.; Schimpl, M.; Gundogdu, M.; Rafie, K.; Dorfmueller, H.C.; Robinson, D.A.; van Aalten, D.M.
Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors
Biochem. J.
457
497-502
2014
Homo sapiens (O15294)
brenda
Trapannone, R.; Mariappa, D.; Ferenbach, A.T.; van Aalten, D.M.
Nucleocytoplasmic human O-GlcNAc transferase is sufficient for O-GlcNAcylation of mitochondrial proteins
Biochem. J.
473
1693-1702
2016
Homo sapiens (O15294), Homo sapiens
brenda
Kim, E.J.; Abramowitz, L.K.; Bond, M.R.; Love, D.C.; Kang, D.W.; Leucke, H.F.; Kang, D.W.; Ahn, J.S.; Hanover, J.A.
Versatile O-GlcNAc transferase assay for high-throughput identification of enzyme variants, substrates, and inhibitors
Bioconjug. Chem.
25
1025-1030
2014
Homo sapiens (O15294)
brenda
Im, J.
Synthesis of a benzene-containing C1-phosphonate analogue of UDP-GlcNAc for the inhibition of O-GlcNAc transferase
Bull. Korean Chem. Soc.
37
7-12
2016
Homo sapiens
-
brenda
Pekkurnaz, G.; Trinidad, J.C.; Wang, X.; Kong, D.; Schwarz, T.L.
Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase
Cell
158
54-68
2014
Rattus norvegicus
brenda
Liu, X.; Li, L.; Wang, Y.; Yan, H.; Ma, X.; Wang, P.G.; Zhang, L.
A peptide panel investigation reveals the acceptor specificity of O-GlcNAc transferase
FASEB J.
28
3362-3372
2014
Homo sapiens
brenda
Sokol, K.A.; Olszewski, N.E.
The putative eukaryote-like O-GlcNAc transferase of the cyanobacterium Synechococcus elongatus PCC 7942 hydrolyzes UDP-GlcNAc and is involved in multiple cellular processes
J. Bacteriol.
197
354-361
2015
Synechococcus elongatus (Q31S86), Synechococcus elongatus PCC 7942 (Q31S86)
brenda
Shi, W.W.; Jiang, Y.L.; Zhu, F.; Yang, Y.H.; Shao, Q.Y.; Yang, H.B.; Ren, Y.M.; Wu, H.; Chen, Y.; Zhou, C.Z.
Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins
J. Biol. Chem.
289
20898-20907
2014
Streptococcus pneumoniae TIGR4 (A0A0H2URG7), Streptococcus pneumoniae TIGR4 ATCC BAA-334 (A0A0H2URG7)
brenda
Rodriguez, A.C.; Yu, S.H.; Li, B.; Zegzouti, H.; Kohler, J.J.
Enhanced transfer of a photocross-linking N-acetylglucosamine (GlcNAc) analog by an O-GlcNAc transferase mutant with converted substrate specificity
J. Biol. Chem.
290
22638-22648
2015
Homo sapiens
brenda
Zhang, Z.; Costa, F.C.; Tan, E.P.; Bushue, N.; DiTacchio, L.; Costello, C.E.; McComb, M.E.; Whelan, S.A.; Peterson, K.R.; Slawson, C.
O-GlcNAc transferase and O-GlcNAcase interact with Mi2beta at the Agamma-globin promoter
J. Biol. Chem.
291
15628-15640
2016
Homo sapiens
brenda
Kumari, M.; Kozmon, S.; Kulhanek, P.; Stepan, J.; Tvaroska, I.; Koca, J.
Exploring reaction pathways for O-GlcNAc transferase catalysis. A string method study
J. Phys. Chem. B
119
4371-4381
2015
Homo sapiens (O15294)
brenda
Pathak, S.; Alonso, J.; Schimpl, M.; Rafie, K.; Blair, D.; Borodkin, V.; Schttelkopf, A.; Albarbarawi, O.; Van Aalten, D.
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
Nat. Struct. Mol. Biol.
22
744-749
2015
Homo sapiens (O15294)
brenda
Mariappa, D.; Zheng, X.; Schimpl, M.; Raimi, O.; Ferenbach, A.; Mller, H.; Van Aalten, D.
Dual functionality of O-GlcNAc transferase is required for Drosophila development
Open Biology
5
15023
2015
Drosophila melanogaster (Q7KJA9)
brenda
Shi, J.; Sharif, S.; Ruijtenbeek, R.; Pieters, R.J.
Activity based high-throughput screening for novel O-GlcNAc transferase substrates using a dynamic peptide microarray
PLoS ONE
11
e0151085
2016
Homo sapiens (O15294)
brenda
Mueller, R.; Jenny, A.; Stanley, P.
The EGF repeat-specific O-GlcNAc-transferase Eogt interacts with notch signaling and pyrimidine metabolism pathways in Drosophila
PLoS ONE
8
e62835
2013
Homo sapiens (Q5NDL2), Drosophila melanogaster (Q9VQB7)
brenda
Ma, X.; Liu, P.; Yan, H.; Sun, H.; Liu, X.; Zhou, F.; Li, L.; Chen, Y.; Muthana, M.M.; Chen, X.; Wang, P.G.; Zhang, L.
Substrate specificity provides insights into the sugar donor recognition mechanism of O-GlcNAc transferase (OGT)
PLoS ONE
8
e63452
2013
Homo sapiens (O15294), Homo sapiens
brenda
Trapannone, R.; Rafie, K.; van Aalten, D.M.
O-GlcNAc transferase inhibitors current tools and future challenges
Biochem. Soc. Trans.
44
88-93
2016
Homo sapiens (O15294)
brenda
She, N.; Zhao, Y.; Hao, J.; Xie, S.; Wang, C.
Uridine diphosphate release mechanism in O-N-acetylglucosamine (O-GlcNAc) transferase catalysis
Biochim. Biophys. Acta Gen. Subj.
1863
609-622
2019
Homo sapiens (O15294)
brenda
Ghirardello, M.; Perrone, D.; Chinaglia, N.; Sadaba, D.; Delso, I.; Tejero, T.; Marchesi, E.; Fogagnolo, M.; Rafie, K.; van Aalten, D.M.F.; Merino, P.
UDP-GlcNAc analogues as inhibitors of O-GlcNAc transferase (OGT) spectroscopic, computational, and biological studies
Chemistry
24
7264-7272
2018
Homo sapiens (O15294)
brenda
Xing, L.; Liu, Y.; Xu, S.; Xiao, J.; Wang, B.; Deng, H.; Lu, Z.; Xu, Y.; Chong, K.
Arabidopsis O-GlcNAc transferase SEC activates histone methyltransferase ATX1 to regulate flowering
EMBO J.
37
e98115
2018
Arabidopsis thaliana (Q9M8Y0)
brenda
Constable, S.; Lim, J.M.; Vaidyanathan, K.; Wells, L.
O-GlcNAc transferase regulates transcriptional activity of human Oct4
Glycobiology
27
927-937
2017
Homo sapiens (O15294), Homo sapiens
brenda
Martin, S.E.S.; Tan, Z.W.; Itkonen, H.M.; Duveau, D.Y.; Paulo, J.A.; Janetzko, J.; Boutz, P.L.; Toerk, L.; Moss, F.A.; Thomas, C.J.; Gygi, S.P.; Lazarus, M.B.; Walker, S.
Structure-based evolution of low nanomolar O-GlcNAc transferase inhibitors
J. Am. Chem. Soc.
140
13542-13545
2018
Homo sapiens
brenda
Levine, Z.G.; Fan, C.; Melicher, M.S.; Orman, M.; Benjamin, T.; Walker, S.
O-GlcNAc transferase recognizes protein substrates using an asparagine ladder in the tetratricopeptide repeat (TPR) superhelix
J. Am. Chem. Soc.
140
3510-3513
2018
Homo sapiens (O15294)
brenda
Darabedian, N.; Gao, J.; Chuh, K.N.; Woo, C.M.; Pratt, M.R.
The metabolic chemical reporter 6-azido-6-deoxy-glucose further reveals the substrate promiscuity of O-GlcNAc transferase and catalyzes the discovery of intracellular protein modification by O-glucose
J. Am. Chem. Soc.
140
7092-7100
2018
Homo sapiens (O15294)
brenda
Joiner, C.M.; Levine, Z.G.; Aonbangkhen, C.; Woo, C.M.; Walker, S.
Aspartate residues far from the active site drive O-GlcNAc transferase substrate selection
J. Am. Chem. Soc.
141
12974-12978
2019
Homo sapiens (O15294)
brenda
Sacoman, J.L.; Dagda, R.Y.; Burnham-Marusich, A.R.; Dagda, R.K.; Berninsone, P.M.
Mitochondrial O-GlcNAc transferase (mOGT) regulates mitochondrial structure, function, and survival in HeLa cells
J. Biol. Chem.
292
4499-4518
2017
Homo sapiens (O15294)
brenda
Liu, L.; Li, L.; Ma, C.; Shi, Y.; Liu, C.; Xiao, Z.; Zhang, Y.; Tian, F.; Gao, Y.; Zhang, J.; Ying, W.; Wang, P.G.; Zhang, L.
O-GlcNAcylation of Thr12/Ser56 in short-form O-GlcNAc transferase (sOGT) regulates its substrate selectivity
J. Biol. Chem.
294
16620-16633
2019
Homo sapiens (O15294)
brenda
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
brenda
Cao, B.; Duan, M.; Xing, Y.; Liu, C.; Yang, F.; Li, Y.; Yang, T.; Wei, Y.; Gao, Q.; Jiang, J.
O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E
J. Cell. Mol. Med.
23
2384-2398
2019
Homo sapiens (O15294), Homo sapiens
brenda
Wang, Y.; Zhu, J.; Zhang, L.
Discovery of cell-permeable O-GlcNAc transferase inhibitors via tethering in situ click chemistry
J. Med. Chem.
60
263-272
2017
Homo sapiens (O15294)
brenda
Seo, H.G.; Kim, H.B.; Kang, M.J.; Ryum, J.H.; Yi, E.C.; Cho, J.W.
Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation
Sci. Rep.
6
34614
2016
Homo sapiens (O15294)
brenda