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malfunction
gain and loss of ogt function produced the same range of defects
malfunction
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silencing of OGT results in impaired activation of T and B lymphocytes
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
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siRNA-mediated knockdown of the enzyme enhances 26S proteasome assembly and activity
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
loss of function of SECRET AGENT, leads to an early flowering phenotype. This results from reduced histone H3 lysine 4 trimethylation (H3K4me3) of FLOWERING LOCUS C (FLC) locus, which encodes a key negative regulator of flowering
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
malfunction
several EOGT mutations that may affect putative N-glycosylation consensus sites are recorded in the cancer database
metabolism
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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
metabolism
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enzyme activation of by UDP-GlcNAc blocks compound C-induced increases in 26S proteasome assembly and activation
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
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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
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
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the enzyme plays a major role in AMPK regulation of the proteasome
physiological function
an OGT deletion mutant exhibits several phenotypes. Without agitation, mutant cells aggregate and settle out of the medium. The mutant cells have higher free inorganic phosphate levels, wider thylakoid lumen, and differential accumulation of electron-dense inclusion bodies
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
Eogt may regulate protein functions by O-GlcNAc modification of their EGF repeats, and cellular metabolism by affecting pyrimidine synthesis and catabolism. Eogt knock-down in the wing leads to metabolic and signaling perturbations that increase cytosolic uracil levels, thereby causing wing blister formation
physiological function
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increased extracellular glucose decreases mitochondrial motility in hippocampal axons, and OGT overexpression reduces axonal mitochondrial motility and density. The 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
physiological function
mutants of OGT are pupal lethal. Postpupal Drosophila development can proceed with negligible OGT catalysis, while early embryonic development is OGT activity-dependent. A severely hypomorphic OGT mutant complements sxc pupal lethality. The hypomorphic OGT mutant-rescued progeny do not produce F2 adults, because a set of Hox genes is de-repressed in F2 embryos, resulting in homeotic phenotypes
physiological function
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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
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 catalyzes the post-translational modification of proteins. the enzyme (SEC) activates ARABIDOPSIS HOMOLOG OF TRITHORAX1 (ATX1), a histone lysine methyltransferase (HKMT), through O-GlcNAc modification to augment ATX1-mediated H3K4me3 histone modification at FLC locus. SEC transfers an O-GlcNAc group on Ser947 of ATX1, which resides in the SET domain, thereby activating ATX1
physiological function
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the enzyme is responsible for all nucleocytoplasmic glycosylation
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
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an OGT deletion mutant exhibits several phenotypes. Without agitation, mutant cells aggregate and settle out of the medium. The mutant cells have higher free inorganic phosphate levels, wider thylakoid lumen, and differential accumulation of electron-dense inclusion bodies
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