| + |
PFKP | up-regulates activity 
phosphorylation
|
ATG4B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275832 |
Ser34 |
WILGRKYsIFTEKDE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33607258 |
In vitro kinase assay validated that PFKP functioning as a protein kinase phosphorylated ATG4B at S34. This phosphorylation could enhance ATG4B activity and p62 degradation. In addition, PFKP S386 phosphorylation was important to ATG4B S34 phosphorylation and autophagy in HEK293T cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OGA | up-regulates activity
deglycosylation
|
PFKP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267606 |
Ser540 |
VMVPATVsNNVPGSD |
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
|
PFKP |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267583 |
Ser540 |
VMVPATVsNNVPGSD |
Homo sapiens |
A-549 Cell |
| 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 |
| + |
CyclinD3/CDK6 | down-regulates activity
phosphorylation
|
PFKP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273033 |
Ser679 |
MQQGGAPsPFDRNFG |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 28607489 |
Here, using human cancer cells and patient-derived xenografts in mice, we show that the cyclin D3–CDK6 kinase phosphorylates and inhibits the catalytic activity of two key enzymes in the glycolytic pathway, 6-phosphofructokinase and pyruvate kinase M2.|Phosphomimicking mutants of PFKP (S679E) or PKM2 (S37E) displayed decreased catalytic activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PFKP | up-regulates quantity
chemical modification
|
beta-D-fructofuranose 1,6-bisphosphate(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266473 |
|
|
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
|
PFKP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267268 |
|
|
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 |
| + |
PFKP | down-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266469 |
|
|
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 |
3.0
PFKP
- 
- 