| + |
AKT | up-regulates 
phosphorylation
|
PFKFB3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137241 |
Ser461 |
NPLMRRNsVTPLASP |
Homo sapiens |
|
| pmid |
sentence |
| 15896703 |
We also found that AMP activated protein kinase and protein kinases A, B, and C catalyzed the phosphorylation of Ser-460 of HBP1, and that in addition both isoforms are phosphorylated at a second, as yet undetermined site by protein kinase C. However, none of the phosphorylations had any effect on the intrinsic kinetic characteristics of either enzymatic activity, and neither did point mutation (mimicking phosphorylation), deletion, and alternative-splice modification of the HBP1 carboxy-terminal region. Instead, these phosphorylations and mutations decreased the sensitivity of the 6PF2K to a potent allosteric inhibitor, phosphoenolpyruvate, which appears to be the major regulatory mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PRKAA1 | up-regulates
phosphorylation
|
PFKFB3 |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89760 |
Ser461 |
NPLMRRNsVTPLASP |
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 12065600 |
Ipfk-2 was phosphorylated on the homologous serine (ser-461) and activated by ampk in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
AMPK | up-regulates
phosphorylation
|
PFKFB3 |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216639 |
Ser461 |
NPLMRRNsVTPLASP |
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 12065600 |
Ipfk-2 was phosphorylated on the homologous serine (ser-461) and activated by ampk in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
AKT1 | up-regulates
phosphorylation
|
PFKFB3 |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252477 |
Ser461 |
NPLMRRNsVTPLASP |
Homo sapiens |
|
| pmid |
sentence |
| 15896703 |
We also found that AMP activated protein kinase and protein kinases A, B, and C catalyzed the phosphorylation of Ser-460 of HBP1, and that in addition both isoforms are phosphorylated at a second, as yet undetermined site by protein kinase C. However, none of the phosphorylations had any effect on the intrinsic kinetic characteristics of either enzymatic activity, and neither did point mutation (mimicking phosphorylation), deletion, and alternative-splice modification of the HBP1 carboxy-terminal region. Instead, these phosphorylations and mutations decreased the sensitivity of the 6PF2K to a potent allosteric inhibitor, phosphoenolpyruvate, which appears to be the major regulatory mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APC-c | down-regulates quantity by destabilization 
ubiquitination
|
PFKFB3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271435 |
|
|
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 20080744 |
We have recently discovered that the glycolysis-promoting enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, isoform 3 (PFKFB3), is degraded by the E3 ubiquitin ligase APC/C-Cdh1, which also degrades cell-cycle proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF-1 complex | up-regulates quantity by expression
transcriptional regulation
|
PFKFB3 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267388 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11744734 |
PFKFB3, is highly induced by hypoxia and the hypoxia mimics cobalt and desferrioxamine. This induction could be replicated by the use of an inhibitor of the prolyl hydroxylase enzymes responsible for the von Hippel Lindau (VHL)-dependent destabilization and tagging of HIF-1α. The absolute dependence of the PFKFB3 gene on HIF-1 was confirmed by its overexpression in VHL-deficient cells and by the lack of hypoxic induction in mouse embryonic fibroblasts conditionally nullizygous for HIF-1α |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PFKFB3 | down-regulates quantity
chemical modification
|
β-D-fructose 6-phosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267271 |
|
|
in vitro |
|
| pmid |
sentence |
| 9404080 |
A full-length cDNA, which encodes a human placental fructose-6-phosphate,2-kinase/ fructose-2,6-bisphosphatase, was constructed and expressed in Escherichia coli. [...]The expressed enzyme was bifunctional with Vmax values of 142 and 0.2 milliunits/mg for the kinase and phosphatase activities, respectively. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
FZR1 | down-regulates quantity by destabilization
binding
|
PFKFB3 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271436 |
|
|
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 20080744 |
We have recently discovered that the glycolysis-promoting enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, isoform 3 (PFKFB3), is degraded by the E3 ubiquitin ligase APC/C-Cdh1, which also degrades cell-cycle proteins. Cdh1 promotes PFKFB3 degradation in the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PFKFB3 | up-regulates quantity
chemical modification
|
beta-D-fructofuranose 2,6-bisphosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267260 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9404080 |
A full-length cDNA, which encodes a human placental fructose-6-phosphate,2-kinase/ fructose-2,6-bisphosphatase, was constructed and expressed in Escherichia coli. [...]The expressed enzyme was bifunctional with Vmax values of 142 and 0.2 milliunits/mg for the kinase and phosphatase activities, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
3.0
PFKFB3
- 
- 