| + |
PDP1 | up-regulates activity 
dephosphorylation
|
PDHA1 |
0.722 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252055 |
Ser232 |
NRYGMGTsVERAAAS |
in vitro |
|
| pmid |
sentence |
| 7782287 |
Sites 1, 2, and 3 were dephosphorylated either individually or in the presence of the other sites by the phospho-E1-phosphatase resulting in complete reactivation of the E1. The rates of dephosphorylation and reactivation were similar for sites 1, 2, and 3, indicating a random dephosphorylation mechanism |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252054 |
Ser293 |
TYRYHGHsMSDPGVS |
in vitro |
|
| pmid |
sentence |
| 7782287 |
Sites 1, 2, and 3 were dephosphorylated either individually or in the presence of the other sites by the phospho-E1-phosphatase resulting in complete reactivation of the E1. The rates of dephosphorylation and reactivation were similar for sites 1, 2, and 3, indicating a random dephosphorylation mechanism |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252056 |
Ser300 |
SMSDPGVsYRTREEI |
in vitro |
|
| pmid |
sentence |
| 7782287 |
Sites 1, 2, and 3 were dephosphorylated either individually or in the presence of the other sites by the phospho-E1-phosphatase resulting in complete reactivation of the E1. The rates of dephosphorylation and reactivation were similar for sites 1, 2, and 3, indicating a random dephosphorylation mechanism |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251664 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20208177 |
Pyruvate dehydrogenase phosphatase (PDP) is a mitochondrial serine phosphatase that activates phosphorylated pyruvate dehydrogenase complex by dephosphorylation |
|
| Publications: |
4 |
Organism: |
In Vitro, Homo Sapiens |
| + |
ABL1 | down-regulates activity 
phosphorylation
|
PDP1 |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276641 |
Tyr94 |
SILKANEySFKVPEF |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 24962578 |
Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FGFR1 | down-regulates activity
phosphorylation
|
PDP1 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276640 |
Tyr94 |
SILKANEySFKVPEF |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 24962578 |
Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
JAK2 | down-regulates activity
phosphorylation
|
PDP1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276642 |
Tyr94 |
SILKANEySFKVPEF |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 24962578 |
Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ACAT1 | down-regulates activity
acetylation
|
PDP1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267635 |
|
|
|
|
| pmid |
sentence |
| 34289383 |
We previously reported that the mitochondrial fraction of FLT3 activates acetyl-CoA acetyltransferase ACAT1 in mitochondria via Y407 phosphorylation to acetylate and inhibit mitochondrial pyruvate dehydrogenase A (PDHA) and PDH phosphatase 1 (PDP1) |
|
| Publications: |
1 |
| + |
PDP1 | down-regulates
dephosphorylation
|
SMAD1 |
0.245 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144876 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16510868 |
We show that the mammalian pdps are important in dephosphorylation of bmp-activated smad1 but not tgf-beta-activated smad2 or smad3. Thus, pdps specifically inactivate smads in the bmp/dpp pathway. [...] These observations suggest that pdp1 and pdp2 are important for dephosphorylation of smad1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PDP1
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