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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
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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
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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-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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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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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 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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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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catalyses the O-linked attachment of single GlcNAc moieties to serine and threonine residues on many cytosolic or nuclear proteins
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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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enzyme adds a single GlcNAc to hydroxyl groups of serine and threonine residues
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enzyme catalyzes O-GlcNAc addition
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enzyme transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor
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