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Information on EC 2.4.1.255 - protein O-GlcNAc transferase and Organism(s) Homo sapiens and UniProt Accession O15294
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2.4.1.255 protein O-GlcNAc transferaseIUBMB 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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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
o-linked n-acetylglucosamine transferase, ogt protein, o-glcnac protein, n-acetylglucosamine transferase, o-glcnac-transferase, human ogt, ncogt, secret agent, o-linked glcnac transferase, o-linked n-acetylglucosaminyltransferase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
O-GlcNAc transferase
-
O-linked beta-N-acetylglucosamine transferase
-
OGT
-
uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylaminyltransferase
-
mOGT
ncOGT
O-GlcNAc transferase
-
-
OGT
-
-
sOGT
additional information
-
the short isoform of OGT (sOGT) does not glycosylate any of the substrates tested, although it retains a potentially active catalytic domain
mOGT
-
contains an N-terminal mitochondrial targeting sequence, a nuclear localization motif, and 9 tetratricopeptide repeats
ncOGT
-
lacks the mitochondrial targeting motif but contains 3 additional tetratricopeptide repeats (a total of 12)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
KKKYPGGSTPVSSANMM + UDP-GlcNAc
? + UDP
peptide acceptor derived from casein kinase II
-
-
?
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
-
-
?
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 + 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 + 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 + Nup62 protein
UDP + N-acetyl-D-glucosaminyl-[Nup62 protein]
-
-
-
?
UDP-GlcNAc + PGC-1alpha
UDP + N-acetyl-D-gluosaminyl-[PGC-1alpha]
-
-
-
?
UDP-GlcNAc + YPGGSTPVSSANMM
UDP + YPGGSTPVS-3-O-(N-acetyl-D-glucosaminyl)-SANMM
-
-
-
?
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 + 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
-
-
?
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
-
-
?
KKKYPGGSTPVSSANMM + UDP-GlcNAc
UDP + ?
-
Pep-CKII, known natural substrate for OGT
-
-
?
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 + MYPT1
MYPT1-GlcNAc + UDP
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
-
-
?
UDP-GlcNAc + SAP130
SAP130-GlcNAc + UDP
-
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]
-
putative OGT binding partner interact with OGT when co-expressed in yeast (yeast two-hybrid screen)
-
-
?
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 + YSDSPSTST
YSDSP-(GlcNAc)STST + UDP
-
coupled enzyme assay of C-654
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + [Nup62 protein]-L-serine
UDP + [Nup62 protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
-
-
-
-
?
UDP-GlcNAc + TAB1 protein
UDP + N-acetyl-D-glucosaminyl-[TAB1 protein]
-
-
-
?
UDP-GlcNAc + TAB1 protein
UDP + N-acetyl-D-glucosaminyl-[TAB1 protein]
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
UDP-GlcNAc + Nup62 protein
UDP + N-acetyl-D-glucosmainyl-[Nup62 protein]
-
-
-
-
?
UDP-GlcNAc + Nup62 protein
UDP + N-acetyl-D-glucosmainyl-[Nup62 protein]
-
control substrate
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme is not able to transfer UDP-glucose or UDP-2-dehydro-alpha-D-glucose to peptide and protein substrates
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
aspartate residues far from the active site drive O-GlcNAc transferase substrate selection
-
-
-
additional information
?
-
the enzyme is quite promiscuous for its donor sugar substrates. It can endogenously modify proteins with both N-acetyl-glucosamine and glucose
-
-
-
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme transfers N-acetylglucosamine from UDP-GlcNAc to selected serine and threonine residues
-
-
?
additional information
?
-
-
regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme modifies nuclear pore proteins and transcription factors
-
-
?
additional information
?
-
-
enzyme transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine is no substrate
-
-
?
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-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
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
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme transfers N-acetylglucosamine from UDP-GlcNAc to selected serine and threonine residues
-
-
?
additional information
?
-
-
regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme modifies nuclear pore proteins and transcription factors
-
-
?
additional information
?
-
-
enzyme transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
3-(2-adamantanylethyl)-2-[(4-chlorophenyl)azamethylene]-4-oxo-1,3-thiazaperhydroine-6-carboxylic acid
-
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-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
-
5'-O-(hydroxy[3-[(2R,3R,4S,5R)-3,4,5-trihydroxypyrrolidin-2-yl]propyl]phosphoryl)uridine
-
5'-O-(hydroxy[3-[(2R,3R,4S,5R)-3,4,5-tris(benzyloxy)pyrrolidin-2-yl]propyl]phosphoryl)uridine
-
5'-O-[[(2-(N-acetyl-akoga-D-glucosaminopyranosyl)-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
-
5'-O-[[(2-(N-acetyl-beta-D-glucosaminopyranosyl)-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
-
5'-O-[[(2-alpha-D-glucopyranosyl-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
-
5'-O-[[(2-beta-D-glucopyranosyl-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-(N-acetyl-alpha-D-glucosaminopyranosyl)propyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-[(2R,3R)-3-(benzyloxy)pyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-[(2R,3S,4S)-3,4-bis(benzyloxy)pyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-[(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
-
5'-O-[[3-[(2S,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
-
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
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-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
(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
-
donor analogue displacement probes
3-(4-cyanobenzylthio)-1-(thiophen-2-yl)-5,6,7,8-tetrahydroisoquinoline-4-carboxylic acid
-
donor analogue displacement probes
5'-O-[hydroxy(phosphonomethyl)phosphoryl]uridine
-
non-hydrolysable alpha,beta-methylene bisphosphonate analogue with the diphosphate oxygen replaced by a methylene group
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
-
-
ethyl (R)-N-(2-((7-chloro-2-oxo-1,2-dihydroquinoline)-6-sulfonamido)-2-(2-methoxyphenyl)acetyl)-N-(thiophen-2-ylmethyl)glycinate
-
-
methyl (R)-N-(2-(2-methoxyphenyl)-2-((2-oxo-1,2-dihydroquinoline)-6-sulfonamido)acetyl)-N-(thiophen-2-ylmethyl)glycinate
-
-
phenyl 6-chloro-2-oxobenzo[d]oxazole-3(2H)-carboxylate
-
donor analogue displacement probes
UDP-1-deoxy-1-thio-N-acetyl-alpha-D-glucosamine
-
a sub-millimolar inhibitor of hOGT and substrate binding probe
uridine 5'-[[(2-acetylamino-5-hydroxymethyl-benzyl)-phosphono]phosphate]
-
designed to mimic the transition state of the natural donor involved in the enzymatic reaction. The analogue shows low activity as an inhibitor
additional information
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ataxin-10
-
encoded by the SCA10 (spinocerebellar ataxia type 10) gene, interacts with O-GlcNAc transferase OGT in pancreatic beta cells
-
hyperglycemia
-
increases O-GlcNAc levels in pancreatic beta cells, which appears to interfere with beta-cell function
-
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of O-GlcNAcase, increase of the level of O-GlcNAc modifications
additional information
-
beginning 12 h after treatment, glucose deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mM)
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic experiments using recombinant hOGT/XcOGT
-
0.0022
UDP-GlcNAc
using calcium/calmodulin-dependent kinase IV as cosubstrate, at 37°C, pH not specified in the publication
0.0047
UDP-GlcNAc
using CARM1 protein as cosubstrate, at 37°C, pH not specified in the publication
0.0058
UDP-GlcNAc
using Nup62 protein as cosubstrate, at 37°C, pH not specified in the publication
0.007
UDP-GlcNAc
using TAB1 protein as cosubstrate, at 37°C, pH not specified in the publication
0.1757
UDP-N-acetyl-alpha-D-glucosamine
37°C, pH not specified in the publication, enzyme form without O-GlcNAcylation
0.1805
UDP-N-acetyl-alpha-D-glucosamine
37°C, pH not specified in the publication, O-GlcNAcylated enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000073
UDP-GlcNAc
using CARM1 as cosubstrate, at 37°C, pH not specified in the publication
0.000077
UDP-GlcNAc
using calcium/calmodulin-dependent kinase IV as cosubstrate, at 37°C, pH not specified in the publication
0.00057
UDP-GlcNAc
using TAB1 as cosubstrate, at 37°C, pH not specified in the publication
0.00093
UDP-GlcNAc
using Nup62 as cosubstrate, at 37°C, pH not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
UDP-GlcNAc
using CARM1 protein as cosubstrate, at 37°C, pH not specified in the publication
0.035
UDP-GlcNAc
using calcium/calmodulin-dependent kinase IV as cosubstrate, at 37°C, pH not specified in the publication
0.08
UDP-GlcNAc
using TAB1 protein as cosubstrate, at 37°C, pH not specified in the publication
0.16
UDP-GlcNAc
using Nup62 protein as cosubstrate, at 37°C, pH not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.001
1-(4-acetamidophenyl)-4-(diphenylhydroxymethyl)-1H-1,2,3-triazole
Homo sapiens
pH 7.4, 37°C
0.0667
1-(4-acetamidophenyl)-4-(naphthalen-2-yl)-1H-1,2,3-triazole
Homo sapiens
pH 7.4, 37°C
0.139
1-(4-acetamidophenyl)-4-([1,1'-biphenyl]-4-yl)-1H-1,2,3-triazole
Homo sapiens
pH 7.4, 37°C
0.0893
1-(4-chloroacetamidophenyl)-4-(diphenylhydroxymethyl)-1H-1,2,3-triazole
Homo sapiens
pH 7.4, 37°C
0.0717
1-(4-chloroacetamidophenyl)-4-(naphthalen-2-yl)-1H-1,2,3-triazole
Homo sapiens
pH 7.4, 37°C
0.0912
1-(4-chloroacetamidophenyl)-4-([1,1'-biphenyl]-4-yl)-1H-1,2,3-triazole
Homo sapiens
pH 7.4, 37°C
0.018
2,4,5,6-tetraoxypyrimidine
Homo sapiens
pH and temperature not specified in the publication
0.053
3-(2-adamantanylethyl)-2-[(4-chlorophenyl)azamethylene]-4-oxo-1,3-thiazaperhydroine-6-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.01
4-methoxyphenyl 6-acetyl-2-oxobenzo[d]oxazole-3(2H)-carboxylate
Homo sapiens
pH and temperature not specified in the publication
2.218
5'-O-(hydroxy[3-[(2R,3R)-3-hydroxypyrrolidin-2-yl]propyl]phosphoryl)uridine
Homo sapiens
pH and temperature not specified in the publication
1.814
5'-O-(hydroxy[3-[(2R,3R,4S,5R)-3,4,5-trihydroxypyrrolidin-2-yl]propyl]phosphoryl)uridine
Homo sapiens
pH and temperature not specified in the publication
0.102
5'-O-(hydroxy[3-[(2R,3R,4S,5R)-3,4,5-tris(benzyloxy)pyrrolidin-2-yl]propyl]phosphoryl)uridine
Homo sapiens
pH and temperature not specified in the publication
0.589
5'-O-[[(2-(N-acetyl-akoga-D-glucosaminopyranosyl)-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
0.231
5'-O-[[(2-(N-acetyl-beta-D-glucosaminopyranosyl)-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
1.048
5'-O-[[(2-alpha-D-glucopyranosyl-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
1.439
5'-O-[[(2-beta-D-glucopyranosyl-2,3-dihydro-1H-1,2,3-triazol-4-yl)methyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
4.769
5'-O-[[3-(N-acetyl-alpha-D-glucosaminopyranosyl)propyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
0.718
5'-O-[[3-[(2R,3R)-3-(benzyloxy)pyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
1.14
5'-O-[[3-[(2R,3S,4S)-3,4-bis(benzyloxy)pyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
1.804
5'-O-[[3-[(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
5.452
5'-O-[[3-[(2S,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]propyl](hydroxy)phosphoryl]uridine
Homo sapiens
pH and temperature not specified in the publication
0.03 - 0.053
(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
0.06
3-(4-cyanobenzylthio)-1-(thiophen-2-yl)-5,6,7,8-tetrahydroisoquinoline-4-carboxylic acid
Homo sapiens
-
sOGT
additional information
3-(4-cyanobenzylthio)-1-(thiophen-2-yl)-5,6,7,8-tetrahydroisoquinoline-4-carboxylic acid
Homo sapiens
-
for ncOGT IC50 value is about 100-150 microM
0.03
(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
Homo sapiens
-
sOGT
0.053
(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
Homo sapiens
-
ncOGT
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
674603, 692070, 721254, 721485, 721991, 722007, 722455, 722752, 722803, 723250, 723251, 723266, 735642, 735732, 736684, 736868, 737097, 737111, 758767, 758856, 759071, 759309, 759410, 759411, 759496, 759542, 759599, 760142
UniProt
O-linked N-acetylglucosamine transferase is encoded by a single gene that yields nucleocytosolic and mitochondrial isoforms
UniProt
UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase 110 kDa subunit
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the level of total O-GlcNAcylation or O-GlcNAc transferase protein is increased in hepatocellular carcinoma
-
infected with the asexual intraerythrocytic stage of the malaria parasite, Plasmodium falciparum. Comparison of O-glycosylation in Plasmodium falciparum-infected and uninfected erythrocytes
-
expression of OGT shows no significant influence on NFkappaB activity
activity is also elevated in HeLa cells transfected with the human cDNA
enzyme observed in all tissues, but the highest levels in pancreas
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
amino acids residues 451-453 (DFP) are characterised as the nuclear localisation signal of the enzyme. Tne enzyme binds the importin alpha5 protein, and this association is abolished when the DFP motif of the enzyme is mutated or deleted. O-GlcNAcylation of Ser389, which resides in the tetratricopeptide repeats, plays an important role in the nuclear localisation of the enzyme
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
silencing of OGT results in impaired activation of T and B lymphocytes
metabolism
-
O-GlcN acylation affects such diverse cellular processes as transcription, translation, organelle targeting, and protein-protein interactions,1 and is believed to play a role in a variety of signaling cascades that mediate glucose homeostasis and stress responses
physiological function
malfunction
enzyme knockdown results in nuclear factor-kappaB reporter activation in the cells treated with 10 ng/ml tumor necrosis factor-alpha
malfunction
knockdown of O-GlcNAc transferase and host cell factor C1 decreases gluconeogenesis
malfunction
dysregulation of O-GlcNAcylation in response to high glucose or O-GlcNAc transferase expression has been implicated in metabolic diseases and cancer. Knockdown of O-GlcNAc transferase suppresses cell growth and stem-like cell potential of hepatoma cell
malfunction
O-GlcNAc transferase knockout is embryonic lethal in a range of animal models
malfunction
reducing endogenous mOGT expression leads to alterations in mitochondrial structure and function, including Drp1-dependent mitochondrial fragmentation, reduction in mitochondrial membrane potential, and a significant loss of mitochondrial content in the absence of mitochondrial ROS
metabolism
host cell factor C1 recruits the enzyme to O-linked beta-N-acetylglucosaminate PGC-1alpha, and O-linked beta-N-acetylglucosamination facilitates the binding of the deubiquitinase BAP1, thus protecting PGC-1alpha from degradation and promoting gluconeogenesis
metabolism
the enzyme mediates glucose-induced production of MIP-1 cytokines at the transcriptional level. The enzyme is a transcriptional co-regulator for MIP-1 gene promoters
metabolism
the enzyme probably plays a senior role in determining O-linked N-acetylglucosamine levels
metabolism
the enzyme uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins
physiological function
a post-translational modification enzyme that adds an O-linked beta-N-acetylglucosamine monosaccharide to serine or threonine residues of various proteins
physiological function
aberrant OGlcNAcylation by the enzyme is linked to insulin resistance, diabetic complications, cancer and neurodegenerative diseases including Alzheimer's disease
physiological function
endogenous mitochondrial isoform 2 of OGT is not detected in a range of human cell lines, experiments suggest the expression of only a single OGT isoform. Overexpression of the nucleocytoplasmic OGT isoform leads to increased O-GlcNAcylation of mitochondrial proteins, nucleocytoplasmic OGT is necessary and sufficient for the generation of the O-GlcNAc mitochondrial proteome
physiological function
key enzyme involved in dynamic O-GlcNAcylation of nuclear and cytoplasmic proteins
physiological function
mitochondrial O-GlcNAc transferase regulates mitochondrial structure, function, and survival in HeLa cell
physiological function
O-GlcNAc modification is abundant, essential and involved in fundamental biological processes
physiological function
O-GlcNAcylation catalysed by O-GlcNAc transferase is a reversible posttranslational modification. O-GlcNAcylation participates in transcription, epigenetic regulation, and intracellular signalling
physiological function
O-N-acetylglucosamine (O-GlcNAc) transferase is the only one enzyme responsible for O-GlcNAc glycosylation in more than 1000 proteins and plays an extremely significant role in biochemical processes
physiological function
the enzyme activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E
physiological function
the enzyme is responsible for all nucleocytoplasmic O-GlcN acylation. Aspartate residues far from the active site drive O-GlcNAc transferase substrate selection
physiological function
-
central factor for T- and B-lymphocytes activation. Overexpression of OGT and the use of inhibitors of the antagonistic enzyme O-GlcNAcase sensitizes T and B cells toward activation. SiRNAmediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFjB
physiological function
-
O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), interact with the Agamma-globin promoter at the -566 GATA repressor site. O-GlcNAcylation is a mechanism of gamma-globin gene regulation, mediated by modulating the assembly of the GATA-1/FOG-1/Mi2beta repressor complex at the -566 GATA motif within the promoter. Inhibition of OGA by thiamet-G leads to increased occupancy of OGT, OGA and Mi2beta at the Agamma-globin promoter and decreased gamma-globin transcription level. Both OGT and OGA can interact with Mi2beta, GATA-1 and FOG-1, and Mi2beta is OGlcNAcylated
physiological function
transfection of human EOGT cDNA causes O-GlcNAcylation of Drosphila N, Dl and Ser EGF repeats. EOGT requires a conserved DXD motif for optimal activity, and it is primarily responsible for the transfer of OGlcNAc to high molecular weight proteins, including Dp, in Drosophila larvae. In vivo, the human EOGT cDNA fully rescues homozygotes of a P-element excision mutation of EOGT
physiological function
-
the enzyme is responsible for all nucleocytoplasmic glycosylation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OGT1_HUMAN
1046
0
116925
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
78000
103000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
three-dimensional structure of the protein domains I and II, conserved amino acid sequences
additional information
-
OGT is a bipartite protein consisting of a C-terminal glycosyltransferase (Gtf) domain and an N-terminal protein-protein interaction domain comprised of 12 tetratricopeptide (TPR) repeats
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
O-GlcNAcylation of Ser389 in nucleocytoplasmic O-GlcNAc transferase affects its nuclear translocation in HeLa cells. Six O-GlcNAc sites are identified in the tetratricopeptide repeat domain in short-form of O-GlcNAc transferase, with Thr12 and Ser56 being two key sites. Thr12 is a dominant O-GlcNAcylation site. The modification of Ser56 plays a role in regulating short-form of O-GlcNAc transferase. O-GlcNAcylation does not affect activity of O-GlcNAc transferase but alters its substrate selectivity
additional information
additional information
-
dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a binary complex with UDP and a ternary complex with UDP and peptide substrate YPGGSTPVSSANMM, hanging drop vapor diffusion method
cocrystallization of identified substrate peptides with OGT, derived from retinoblastoma-like protein 2 (RBL2411-422, KENPAVTPVSTA), proto-oncogene tyrosine protein kinase receptor Ret (Ret660-672, AQAFPVSYSSSGA), keratin-7 (KER77-19, SPVFTSRSAAFSC) and lamin B1 (LAMIN179-191, KLSPSPSSRVTVS). The peptide is tethered into a common binding mode by a combination of van der Waals interactions and hydrogen bonds that restrict torsional freedom in the -3 to +2 subsites only
hybrid quantum mechanics/molecular mechanics analysis of reaction paths using alpha-phosphate and Asp554 as the catalytic bases. The mechanism with alpha-phosphate acting as the base is favorable. The reaction has a rate-limiting free energy barrier of 23.5 kcal/mol, whereas reactions utilizing Asp554 and water-assisted alpha-phosphate have barriers of 41.7 and 40.9 kcal/mol, respectively
in complex with inhibitor goblin1, to 3.15 A resolution. UDP adopts the same conformation as observed in the OGT Michaelis complex and the peptide occupies the -4 to +2 subsites with a similar backbone conformation. The three-carbon linker connects the two components without introducing any strain, allowing both the UDP moiety and the peptide part of the inhibitor to adopt the optimal position in the binding site, mimicking the natural substrates
three-dimensional structure of the protein domains I and II, conserved amino acid sequences
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
C917A
-
mutant efficiently transfers diazirine-modified GlcNDAz and has altered substrate specificity, preferring to transfer GlcNDAz rather than GlcNAc to protein substrates
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
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
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
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
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
K898A
-
active site mutant, Lys898, which is involved in uracil binding, mutation results in a protein with no apparent activity
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
ncOGT
-
long OGT isoform, nucleocytoplasmic OGT, microinjected into immature oocytes prior to progesterone incubation
sOGT
-
N-terminally truncated isoform, short OGT, microinjected into immature oocytes prior to progesterone incubation
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
Y841A
-
active site mutant, lowers specific activity to 24% compared to wild-type
additional information
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
analysis of more than 50 of human cDNA clones and other ESTs suggest that the mammalian ogt gene encodes several splice variants
-
full length and functional human mOGT is difficult to be expressed in Escherichia coli, truncated mOGT recombinant (C-654) is constructed and expressed
-
ncOGT, mOGT, and sOGT constructs are cloned into a modified pET-24b vector for expression as C-terminal His8 fusions. Expression in Escherichia coli
-
the mitochondrial version of human OGT is subcloned into the pSos vector in-frame with the human Sos protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
the neurodegenerative disease protein ataxin-10 (Atx-10) is associated with cytoplasmic OGT p110 in the brain
analysis
-
metabolic labeling method to introduce the diazirine photocross-linking functional group onto O-GlcNAc residues in mammalian cells. Cells are engineered to produce diazirine-modified UDP-GlcNAc (UDP-Glc-NDAz), which is transferred to substrate proteins by endogenous OGT, producing O-GlcNDAz. Modified proteins can be covalently cross-linked to their binding partners, providing information about O-GlcNAc-dependent interactions
medicine
-
pharmacological inhibition of OGT in breast cancer cells has similar anti-growth and anti-invasion effects. OGT may represent novel therapeutic targets for breast cancer
analysis
application of a high-throughput OGT assay to a library of peptides
analysis
peptide microarray approach to discover novel OGT substrates and study its specificity
analysis
single-well OGT enzyme assay that utilizes His6-tagged substrates, a chemoselective chemical reaction, and unpurified OGT. The high-throughput Ni-nitrilotriacetic acid plate OGT assay facilitates discovery of OGT-specific inhibitors on versatile substrates and the characterization of new enzyme variants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
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
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
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
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)
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
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)
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
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
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
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
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
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
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
Gross, B.J.; Kraybill, B.C.; Walker, S.
Discovery of O-GlcNAc transferase inhibitors
J. Am. Chem. Soc.
127
14588-14589
2005
Homo sapiens
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
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
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
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
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
Sakabe, K.; Hart, G.W.
O-GlcNAc transferase regulates mitotic chromatin dynamics
J. Biol. Chem.
285
34460-34468
2010
Homo sapiens
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
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)
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)
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)
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)
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
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)
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
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)
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
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)
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
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)
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
-
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
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
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
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)
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)
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)
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)
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
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)
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)
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)
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
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
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)
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)
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)
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)
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)
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
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)
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