| + |
PK | up-regulates 
phosphorylation
|
STAT3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268152 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
|
| pmid |
sentence |
| 22306293 |
Pkm2 activates transcription of mek5 by phosphorylating stat3 at y705. pkm2 regulates mek5 transcription via activation of stat3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CREB1 | up-regulates quantity by expression 
transcriptional regulation
|
PK |
0.252 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270285 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16308421 |
In fasted mammals, glucose homeostasis is maintained through induction of the camp response element-binding protein (creb) coactivator transducer of regulated creb activity 2 (torc2), which stimulates the gluconeogenic program in concert with the forkhead factor foxo1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268144 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16308421 |
In fasted mammals, glucose homeostasis is maintained through induction of the camp response element-binding protein (creb) coactivator transducer of regulated creb activity 2 (torc2), which stimulates the gluconeogenic program in concert with the forkhead factor foxo1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268145 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20577053 |
In fasted mammals, glucose homeostasis is maintained through induction of the camp response element-binding protein (creb) coactivator transducer of regulated creb activity 2 (torc2), which stimulates the gluconeogenic program in concert with the forkhead factor foxo1 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PK | up-regulates activity
phosphorylation
|
STAT3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268149 |
|
|
in vitro |
|
| pmid |
sentence |
| 22306293 |
PKM2 activates transcription of MEK5 by phosphorylating stat3 at Y705. In vitro phosphorylation assays show that PKM2 is a protein kinase using PEP as a phosphate donor |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270312 |
|
|
in vitro |
|
| pmid |
sentence |
| 22306293 |
PKM2 activates transcription of MEK5 by phosphorylating stat3 at Y705. In vitro phosphorylation assays show that PKM2 is a protein kinase using PEP as a phosphate donor |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PIM2 | up-regulates quantity by stabilization
phosphorylation
|
PK |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270287 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24142698 |
Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268151 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24142698 |
Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
EGLN3 | up-regulates activity
hydroxylation
|
PK |
0.447 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268146 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21620138 |
Interaction of PKM2 with prolyl hydroxylase 3 (PHD3) enhances PKM2 binding to HIF-1α and PKM2 coactivator function. Mass spectrometry and anti-hydroxyproline antibody assays demonstrate PKM2 hydroxylation on proline-403/408. PHD3 knockdown inhibits PKM2 coactivator function, reduces glucose uptake and lactate production, and increases O(2) consumption in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270290 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21620138 |
Interaction of PKM2 with prolyl hydroxylase 3 (PHD3) enhances PKM2 binding to HIF-1α and PKM2 coactivator function. Mass spectrometry and anti-hydroxyproline antibody assays demonstrate PKM2 hydroxylation on proline-403/408. PHD3 knockdown inhibits PKM2 coactivator function, reduces glucose uptake and lactate production, and increases O(2) consumption in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268147 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21620138 |
Interaction of PKM2 with prolyl hydroxylase 3 (PHD3) enhances PKM2 binding to HIF-1α and PKM2 coactivator function. Mass spectrometry and anti-hydroxyproline antibody assays demonstrate PKM2 hydroxylation on proline-403/408. PHD3 knockdown inhibits PKM2 coactivator function, reduces glucose uptake and lactate production, and increases O(2) consumption in cancer cells. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
Alkannin | down-regulates activity 
chemical inhibition
|
PK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270284 |
|
|
Homo sapiens |
MCF-7 Cell, A-549 Cell |
| pmid |
sentence |
| 21516121 |
Shikonin and its analogs inhibit cancer cell glycolysis by targeting tumor pyruvate kinase-M2. |Shikonin and alkannin are potent inhibitors of recombinant human PKM2|Shikonin and alkannin significantly inhibited the glycolytic rate, as manifested by cellular lactate production and glucose consumption in drug-sensitive and resistant cancer cell lines (MCF-7, MCF-7/Adr, MCF-7/Bcl-2, MCF-7/Bcl-x(L) and A549) that primarily express PKM2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PK | down-regulates quantity
chemical modification
|
phosphonatoenolpyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266539 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15996096 |
Pyruvate kinase (PK)1 is an important regulatory enzyme that is able to generate ATP under hypoxic conditions as well as regulate glucose consumption. Pyruvate kinase catalyzes the last step in glycolysis converting the substrate phosphoenolpyruvate (PEP) into pyruvate, while producing one molecule of ATP per reaction per cycle (Figure 1A). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
Shikonin | down-regulates activity
chemical inhibition
|
PK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270289 |
|
|
Homo sapiens |
MCF-7 Cell, A-549 Cell |
| pmid |
sentence |
| 21516121 |
Shikonin and its analogs inhibit cancer cell glycolysis by targeting tumor pyruvate kinase-M2. |Shikonin and alkannin are potent inhibitors of recombinant human PKM2|Shikonin and alkannin significantly inhibited the glycolytic rate, as manifested by cellular lactate production and glucose consumption in drug-sensitive and resistant cancer cell lines (MCF-7, MCF-7/Adr, MCF-7/Bcl-2, MCF-7/Bcl-x(L) and A549) that primarily express PKM2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PK | up-regulates activity
binding
|
HIF-1 complex |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270311 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21620138 |
PKM2 interacts directly with the HIF-1α subunit and promotes transactivation of HIF-1 target genes by enhancing HIF-1 binding and p300 recruitment to hypoxia response elements, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268150 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21620138 |
PKM2 interacts directly with the HIF-1α subunit and promotes transactivation of HIF-1 target genes by enhancing HIF-1 binding and p300 recruitment to hypoxia response elements, |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PIM2 | down-regulates activity
phosphorylation
|
PK |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268148 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24142698 |
Here, we identified the protein-serine/threonine kinase PIM2, a known oncogene, as a novel binding partner of PKM2. The interaction between PIM2 and PKM2 was confirmed by multiple biochemical approaches in vitro and in cultured cells. Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. Compared with wild type, PKM2 with the phosphorylation-defective mutation displayed a reduced effect on glycolysis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
L-serine | up-regulates activity
chemical activation
|
PK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270286 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23064226 |
We show that serine can bind to and activate human PKM2, and that PKM2 activity in cells is reduced in response to serine deprivation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SREBF1 | up-regulates quantity by expression
transcriptional regulation
|
PK |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270288 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16308421 |
Well-described targets of srebp-1 and the carbohydrate response element binding protein (chrebp), which include the following: fatty acid synthase (fas), acetyl coa carboxylase (acc1), and liver pyruvate kinase (l-pk) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267799 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16308421 |
Well-described targets of srebp-1 and the carbohydrate response element binding protein (chrebp), which include the following: fatty acid synthase (fas), acetyl coa carboxylase (acc1), and liver pyruvate kinase (l-pk) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PK | up-regulates quantity
chemical modification
|
pyruvate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266540 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15996096 |
Pyruvate kinase (PK)1 is an important regulatory enzyme that is able to generate ATP under hypoxic conditions as well as regulate glucose consumption. Pyruvate kinase catalyzes the last step in glycolysis converting the substrate phosphoenolpyruvate (PEP) into pyruvate, while producing one molecule of ATP per reaction per cycle (Figure 1A). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
3.0
PK