| + |
PDK1 | down-regulates 
phosphorylation
|
PDHA2 |
0.479 |
| 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 |
| + |
PDK2 | down-regulates
phosphorylation
|
PDHA2 |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143970 |
Ser291 |
TYRYHGHsMSDPGVS |
Homo sapiens |
|
| pmid |
sentence |
| 16436377 |
Kinetic and regulatory properties of recombinant human pdh2 and pdh1 were compared in this study. Site-specific phosphorylation/dephosphorylation of the three phosphorylation sites by four pdh kinases (pdk1-4) and two pdh phosphatases (pdp1-2) were investigated by substituting serines with alanine or glutamate in pdhs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDK3 | down-regulates
phosphorylation
|
PDHA2 |
0.54 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143974 |
Ser291 |
TYRYHGHsMSDPGVS |
Homo sapiens |
|
| pmid |
sentence |
| 16436377 |
Pdh2 was found to be very similar to pdh1 / in the mechanism of inactivation by phosphorylation of three sites;and (iv) in the phosphorylation of sites 1 and 2 by pdk3 / (ser-264 (site 1), ser-271 (site 2), and ser-203 (site 3) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDK4 | down-regulates
phosphorylation
|
PDHA2 |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121936 |
Ser291 |
TYRYHGHsMSDPGVS |
Homo sapiens |
|
| pmid |
sentence |
| 14966024 |
Pyruvate dehydrogenase (pdh) activity (pdha) controls the entry of carbohydrate into the tricarboxylic cycle and is regulated by pdh kinase (pdk), which phosphorylates and inactivates the enzyme, and pdh phosphatase, which dephosphorylates the enzyme to the active form |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
PDHA2 | form complex 
binding
|
PDH |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267832 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160912 |
The human (h) pyruvate dehydrogenase complex (hPDC) consists of multiple copies of several components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), dihydrolipoamide dehydrogenase (E3), E3-binding protein (BP), and specific kinases and phosphatases. Mammalian PDC has a well organized structure with an icosahedral symmetry of the central E2/BP core to which the other component proteins bind non-covalently. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACAT1 | down-regulates activity
acetylation
|
PDHA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267634 |
|
|
|
|
| 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 |
3.0
PDHA2
- 
- 