| + |
ULK2 | down-regulates activity 
phosphorylation
|
ENO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274038 |
Ser115 |
ANAILGVsLAVCKAG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274037 |
Ser282 |
QLADLYKsFIKDYPV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ULK1 | down-regulates activity
phosphorylation
|
ENO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274030 |
Ser115 |
ANAILGVsLAVCKAG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274029 |
Ser282 |
QLADLYKsFIKDYPV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27153534 |
Here, we demonstrate that, during deprivation of amino acid and growth factors, ULK1/2 directly phosphorylate key glycolytic enzymes including hexokinase (HK), phosphofructokinase 1 (PFK1), enolase 1 (ENO1), and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBP1).Phosphorylation of these enzymes leads to enhanced HK activity to sustain glucose uptake but reduced activity of FBP1 to block the gluconeogenic route and reduced activity of PFK1 and ENO1 to moderate drop of glucose-6-phosphate and to repartition more carbon flux to pentose phosphate pathway (PPP), maintaining cellular energy and redox homeostasis at cellular and organismal levels.Similar results were also obtained using ULK2 as the kinase (data not shown). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates 
phosphorylation
|
ENO1 |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205092 |
Tyr44 |
SGASTGIyEALELRD |
Homo sapiens |
|
| pmid |
sentence |
| 24841372 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-30126 |
Tyr44 |
SGASTGIyEALELRD |
Homo sapiens |
|
| pmid |
sentence |
| 7629021 |
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: |
2 |
Organism: |
Homo Sapiens |
| + |
ENO1 | down-regulates quantity by repression
transcriptional regulation
|
MYC |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261594 |
|
|
Chlorocebus aethiops |
CV-1 Cell |
| pmid |
sentence |
| 2005901 |
This result suggests that MBP-1 in vivo acts as a sequence-specific repressor. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
MYC | up-regulates quantity
transcriptional regulation
|
ENO1 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259989 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 10823814 |
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: |
1 |
Organism: |
Rattus Norvegicus |
| + |
ENO1 | up-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266524 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29767008 |
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 |
| + |
ENO1 | down-regulates quantity
chemical modification
|
2-phosphonato-D-glycerate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266528 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29767008 |
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 |
3.0
ENO1
- 
- 