| + |
PDK1 | down-regulates 
phosphorylation
|
PDHA1 |
0.782 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-32977 |
Ser232 |
NRYGMGTsVERAAAS |
in vitro |
|
| pmid |
sentence |
| 7782287 |
Sites 1, 2, and 3 in the E1 mutants were phosphorylated either individually or in the presence of the other sites by the dihydrolipoamide acetyltransferase-protein X-E1 kinase indicating a site-independent mechanism of phosphorylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PDK1 | down-regulates activity
phosphorylation
|
PDHA1 |
0.782 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109547 |
Ser232 |
NRYGMGTsVERAAAS |
in vitro |
|
| pmid |
sentence |
| 11485553 |
Here we report that the four isoenzymes of protein kinase responsible for the phosphorylation and inactivation of pyruvate dehydrogenase (pdk1, pdk2, pdk3 and pdk4) differ in their abilities to phosphorylate the enzyme. Pdk1 can phosphorylate all three sites (s232, s293, s300), whereas pdk2, pdk3 and pdk4 each phosphorylate only s232 and s293. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109551 |
Ser293 |
TYRYHGHsMSDPGVS |
in vitro |
|
| pmid |
sentence |
| 11485553 |
Here we report that the four isoenzymes of protein kinase responsible for the phosphorylation and inactivation of pyruvate dehydrogenase (pdk1, pdk2, pdk3 and pdk4) differ in their abilities to phosphorylate the enzyme. Pdk1 can phosphorylate all three sites (s232, s293, s300), whereas pdk2, pdk3 and pdk4 each phosphorylate only s232 and s293. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109555 |
Ser300 |
SMSDPGVsYRTREEI |
in vitro |
|
| pmid |
sentence |
| 11485553 |
Here we report that the four isoenzymes of protein kinase responsible for the phosphorylation and inactivation of pyruvate dehydrogenase (pdk1, pdk2, pdk3 and pdk4) differ in their abilities to phosphorylate the enzyme. Pdk1 can phosphorylate all three sites (s232, s293, s300), whereas pdk2, pdk3 and pdk4 each phosphorylate only s232 and s293. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PDK1 | down-regulates
phosphorylation
|
PDHA2 |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143966 |
Ser291 |
TYRYHGHsMSDPGVS |
Homo sapiens |
|
| pmid |
sentence |
| 16436377 |
Human pdh1 and rat pdh2 were expressed previously and were shown to have different specific activities and the ability to be phosphorylated by pdk1 and pdk2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDK1 | down-regulates activity
phosphorylation
|
ITGB3 |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250264 |
Thr779 |
LYKEATStFTNITYR |
in vitro |
|
| pmid |
sentence |
| 10896934 |
PDK1 specifically phosphorylates Thr-753 in 3. Our data argue that phosphorylation of Thr-753, which is conserved in many subunits, reduces the ability of PTB-containing proteins to bind the NXX(pY) motif in 3. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PDK1 | up-regulates activity 
phosphorylation
|
PKN2 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250265 |
Thr816 |
GYGDRTStFCGTPEF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10753910 |
PDK1 phosphorylates the PRKs at their conserved activation loop threonines (Thr-774 and Thr-816 for PRK1 and PRK2, respectively) both in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGFR1 | up-regulates
phosphorylation
|
PDK1 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191719 |
Tyr136 |
AEDAKAIyDFTDTVI |
Homo sapiens |
|
| pmid |
sentence |
| 22195962 |
Mitochondrial pdhk1 is tyrosine phosphorylated and activated by fgfr1 in cancer cells further mass spectrometric analysis identified three tyrosine residues of pdhk1, including y136, y243 and y244, that are phosphorylated by fgfr1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191723 |
Tyr243 |
ARRLCDLyYINSPEL |
Homo sapiens |
|
| pmid |
sentence |
| 22195962 |
Mitochondrial pdhk1 is tyrosine phosphorylated and activated by fgfr1 in cancer cells further mass spectrometric analysis identified three tyrosine residues of pdhk1, including y136, y243 and y244, that are phosphorylated by fgfr1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193454 |
Tyr244 |
RRLCDLYyINSPELE |
Homo sapiens |
|
| pmid |
sentence |
| 22195962 |
Mitochondrial pdhk1 is tyrosine phosphorylated and activated by fgfr1 in cancer cells further mass spectrometric analysis identified three tyrosine residues of pdhk1, including y136, y243 and y244, that are phosphorylated by fgfr1 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
HIF-1 complex | up-regulates quantity by expression
transcriptional regulation
|
PDK1 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267446 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16517405 |
Activation of glycolytic genes by HIF-1 is considered critical for metabolic adaptation to hypoxia through increased conversion of glucose to pyruvate and subsequently to lactate. We found that HIF-1 also actively suppresses metabolism through the tricarboxylic acid cycle (TCA) by directly trans-activating the gene encoding pyruvate dehydrogenase kinase 1 (PDK1). PDK1 inactivates the TCA cycle enzyme, pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
HIF1A | up-regulates quantity by expression
transcriptional regulation
|
PDK1 |
0.489 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267444 |
|
|
Homo sapiens |
P493-6 Cell |
| pmid |
sentence |
| 16517405 |
Activation of glycolytic genes by HIF-1 is considered critical for metabolic adaptation to hypoxia through increased conversion of glucose to pyruvate and subsequently to lactate. We found that HIF-1 also actively suppresses metabolism through the tricarboxylic acid cycle (TCA) by directly trans-activating the gene encoding pyruvate dehydrogenase kinase 1 (PDK1). PDK1 inactivates the TCA cycle enzyme, pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF-1 complex | up-regulates quantity
transcriptional regulation
|
PDK1 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267480 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 16517405 |
We found that HIF-1 also actively suppresses metabolism through the tricarboxylic acid cycle (TCA) by directly trans-activating the gene encoding pyruvate dehydrogenase kinase 1 (PDK1). PDK1 inactivates the TCA cycle enzyme, pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl-CoA. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Glycolysis and Gluconeogenesis |
| + |
PDK1 | down-regulates activity
phosphorylation
|
PDH |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267445 |
|
|
Homo sapiens |
P493-6 Cell |
| pmid |
sentence |
| 16517405 |
PDK1 is a direct HIF-1 target gene. We found that the gene encoding pyruvate dehydrogenase kinase 1 (PDK1) is a direct target of HIF-1. PDK1 phosphorylates the pyruvate dehydrogenase (PDH) E1α subunit and inactivates the PDH enzyme complex that converts pyruvate to acetyl-coenzyme A, thereby inhibiting pyruvate metabolism via the tricarboxylic acid (TCA) cycle |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glycolysis and Gluconeogenesis |
3.0
PDK1
- 
- 