| + |
OGA | up-regulates activity 
deglycosylation
|
PFKM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267607 |
Ser530 |
VVIPATVsNNVPGSD |
Homo sapiens |
|
| pmid |
sentence |
| 26399441 |
Our previous investigation on O-GlcNAcylation of PFK1 has demonstrated that O-GlcNAcylation inhibits PFK1 enzyme activity|In cells, a single set of antagonistic enzymes-O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase are responsible for the addition and removal of GlcNAc moiety, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OGT | down-regulates activity 
glycosylation
|
PFKM |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267584 |
Ser530 |
VVIPATVsNNVPGSD |
Homo sapiens |
|
| pmid |
sentence |
| 26399441 |
Our previous investigation on O-GlcNAcylation of PFK1 has demonstrated that O-GlcNAcylation inhibits PFK1 enzyme activity|In cells, a single set of antagonistic enzymes-O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase are responsible for the addition and removal of GlcNAc moiety, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ULK1 | down-regulates activity
phosphorylation
|
PFKM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274035 |
Ser74 |
EATWESVsMMLQLGG |
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-274036 |
Ser762 |
YEIDLDTsDHAHLEH |
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 |
| + |
ULK2 | down-regulates activity
phosphorylation
|
PFKM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274043 |
Ser74 |
EATWESVsMMLQLGG |
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-274044 |
Ser762 |
YEIDLDTsDHAHLEH |
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 |
| + |
PFKM | up-regulates quantity
chemical modification
|
beta-D-fructofuranose 1,6-bisphosphate(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266471 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
beta-D-fructofuranose 2,6-bisphosphate | up-regulates activity
binding
|
PFKM |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267267 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19454274 |
The PFKFB enzymes synthesize fructose-2,6-bisphosphate (F2,6BP) which allosterically activates 6-phosphofructo-1-kinase (PFK-1), a rate-limiting enzyme and essential control point in the glycolytic pathway. PFK-1 is inhibited by ATP when energy stores are abundant and F2,6BP can override this inhibition and enhance glucose uptake and glycolytic flux |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
MYC | up-regulates quantity
transcriptional regulation
|
PFKM |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259988 |
|
|
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 |
| + |
PFKM | down-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266467 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051738 |
Phosphofructokinase catalyzes the rate-limiting, ATP-mediated phosphorylation of F6P to FBP. PFK is a homo- or heterotetramer with a molecular mass of approximately 380 kDa, and the enzyme is allosterically regulated, among other metabolites, by 2,3-DPG.35. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
CyclinD3/CDK6 | down-regulates activity
phosphorylation
|
PFKM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276452 |
|
|
in vitro |
|
| pmid |
sentence |
| 28607489 |
In vitro kinase reactions revealed that all three PFK1 isoforms (PFKP, PFKL, PFKM) and PKM2 were phosphorylated by cyclin D3-CDK6 (Extended Data Fig. 2a–d, Supplementary Table 4). |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
PFKM
- 
- 