Relation Results

Summary

Name Enolase
Primary ID SIGNOR-PF74
Type protein family
Formed by ENO1, ENO2, ENO3
Relations 7
Pathways Glycolysis and Gluconeogenesis

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Type: Score: Layout: SPV 
0.4210.20.80.20.4210.8MYCEnolaseMYOD1/SWI/SNF complexphosphonatoenolpyruvateSRC2-phosphonato-D-glycerate(3-)

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Relations
Regulator
Mechanism
target
score ℹ
+ MYCup-regulates quantity img/direct-activation.png transcriptional regulation Enolase 0.421
Identifier Residue Sequence Organism Cell Line
SIGNOR-270247 Rattus norvegicus
pmid sentence
C-Myc directly transactivates genes encoding GLUT1, phosphofructokinase, and enolase and increases glucose uptake in Rat1 fibroblasts. Nuclear run-on studies confirmed that the GLUT1 transcriptional rate is elevated by c-Myc. Our findings suggest that overexpression of the c-Myc oncoprotein deregulates glycolysis through the activation of several components of the glucose metabolic pathway.
Identifier Residue Sequence Organism Cell Line
SIGNOR-267785 Rattus norvegicus
pmid sentence
C-Myc directly transactivates genes encoding GLUT1, phosphofructokinase, and enolase and increases glucose uptake in Rat1 fibroblasts. Nuclear run-on studies confirmed that the GLUT1 transcriptional rate is elevated by c-Myc. Our findings suggest that overexpression of the c-Myc oncoprotein deregulates glycolysis through the activation of several components of the glucose metabolic pathway.
Publications: 2 Organism: Rattus Norvegicus
+ MYOD1/SWI/SNF complexup-regulates quantity by expression img/indirect-activation.png transcriptional regulation Enolase 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-270249 Homo sapiens
pmid sentence
Swi/snf enzymes are necessary for myod to activate muscle gene transcription / myod increased the expression of 94 genes and decreased that of 70 genes /these 94 genes (represented by 96 array features) were analyzed for their dependence on a functional brg1-based swi/snf complex. In the presence of dominant-negative brg1, 29 genes did not achieve full activation by myod, as determined by statistical criteria (q 0.05) and a twofold or more decrease in expression level (table 1; see also table s1 in the supplemental material)
Publications: 1 Organism: Homo Sapiens
Tissue: Muscle
+ Enolaseup-regulates quantity img/direct-activation.png chemical modification phosphonatoenolpyruvate 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-266527 Homo sapiens
pmid sentence
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits.
Publications: 1 Organism: Homo Sapiens
Pathways:Glycolysis and Gluconeogenesis
+ Enolasedown-regulates quantity by repression img/direct_inhibition.png transcriptional regulation MYC 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-270308 Chlorocebus aethiops CV-1 Cell
pmid sentence
This result suggests that MBP-1 in vivo acts as a sequence-specific repressor.
Publications: 1 Organism: Chlorocebus Aethiops
+ SRCup-regulates img/direct-activation.png phosphorylation Enolase 0.421
Identifier Residue Sequence Organism Cell Line
SIGNOR-270248 Homo sapiens
pmid sentence
The present finding suggested that the tyrosine residue at position 44 in chicken alpha-enolase is the phosphorylation site by the tyrosine kinase. Our data suggest that eno1 was upregulated by caga protein through activating the src and mek/erk signal pathways
Publications: 1 Organism: Homo Sapiens
+ Enolasedown-regulates quantity img/direct_inhibition.png chemical modification 2-phosphonato-D-glycerate(3-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-266531 Homo sapiens
pmid sentence
Alpha-enolase (ENO1), also known as 2-phospho-D-glycerate hydrolase, is a metalloenzyme that catalyzes the conversion of 2-phosphoglyceric acid to phosphoenolpyruvic acid in the glycolytic pathway. Subsequent studies have shown that three types of enolase isoenzymes exist in mammals: α-enolase (ENO1) is present in almost all mature tissues; β-enolase (ENO3) exists primarily in muscle tissues; and γ-enolase (ENO2) occurs mainly in nervous and neuroendocrine tissues. All enolases are composed of two identical subunits.
Publications: 1 Organism: Homo Sapiens
Pathways:Glycolysis and Gluconeogenesis
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