| + |
SIRT3 | down-regulates activity 
deacetylation
|
PDHA1 |
0.488 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267636 |
Lys321 |
SDPIMLLkDRMVNSN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25152236 |
SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells|SIRT3 deacetylates PDHA1 lysine 321 (K321) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDK3 | down-regulates activity
phosphorylation
|
PDHA1 |
0.867 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109613 |
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-109609 |
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-109647 |
Ser293 |
TYRYHGHsMSDPGVS |
in vitro |
|
| pmid |
sentence |
| 11486000 |
Activity of the mammalian pyruvate dehydrogenase complex is regulated by phosphorylation-dephosphorylation of the alpha subunit of the pyruvate dehydrogenase (e1) component. Phosphorylation is carried out by four pyruvate dehydrogenase kinase (pdk) isoenzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109651 |
Ser300 |
SMSDPGVsYRTREEI |
in vitro |
|
| pmid |
sentence |
| 11486000 |
Activity of the mammalian pyruvate dehydrogenase complex is regulated by phosphorylation-dephosphorylation of the alpha subunit of the pyruvate dehydrogenase (e1) component. Phosphorylation is carried out by four pyruvate dehydrogenase kinase (pdk) isoenzymes. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PDK4 | down-regulates activity
phosphorylation
|
PDHA1 |
0.683 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109621 |
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-109617 |
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. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PDK1 | down-regulates activity
phosphorylation
|
PDHA1 |
0.786 |
| 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 |
| + |
PDK2 | down-regulates
phosphorylation
|
PDHA1 |
0.675 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33040 |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33137 |
Ser293 |
TYRYHGHsMSDPGVS |
in vitro |
|
| pmid |
sentence |
| 7782287 |
Mammalian pyruvate dehydrogenase (?2_2) (e1) is regulated by phosphorylation-dephosphorylation, catalyzed by the e1-kinase and the phospho-e1-phosphatase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33141 |
Ser300 |
SMSDPGVsYRTREEI |
in vitro |
|
| pmid |
sentence |
| 7782287 |
Mammalian pyruvate dehydrogenase (?2_2) (e1) is regulated by phosphorylation-dephosphorylation, catalyzed by the e1-kinase and the phospho-e1-phosphatase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154640 |
Ser300 |
SMSDPGVsYRTREEI |
Homo sapiens |
|
| pmid |
sentence |
| 17474719 |
Regulation of mammalian pdc activity is accomplished in large part by phosphorylation (resulting in inactivation) of the e1 component by a family of pyruvate dehydrogenase kinases (pdk 14 isozymes) and dephosphorylation (leading to activation) of phosphorylated e1 by a set of specific phosphatases (phosphopyruvate dehydrogenase phosphatase 12 isozymes) (1, 3-6). The subunit of the e1 component has three phosphorylation sites, named site 1 (ser-264), site 2 (ser-271), and site 3 (ser-203), and phosphorylation of any one of these three sites results in inactivation |
|
| Publications: |
4 |
Organism: |
In Vitro, Homo Sapiens |
| + |
PDK1 | down-regulates
phosphorylation
|
PDHA1 |
0.786 |
| 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 |
| + |
PDP1 | up-regulates activity 
dephosphorylation
|
PDHA1 |
0.728 |
| 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 |
| + |
PDK2 | down-regulates activity
phosphorylation
|
PDHA1 |
0.675 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109559 |
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-109563 |
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. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PDK4 | down-regulates
phosphorylation
|
PDHA1 |
0.683 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33197 |
Ser293 |
TYRYHGHsMSDPGVS |
in vitro |
|
| pmid |
sentence |
| 7782287 |
Mammalian pyruvate dehydrogenase (?2_2) (e1) is regulated by phosphorylation-dephosphorylation, catalyzed by the e1-kinase and the phospho-e1-phosphatase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-33201 |
Ser300 |
SMSDPGVsYRTREEI |
in vitro |
|
| pmid |
sentence |
| 7782287 |
Mammalian pyruvate dehydrogenase (?2_2) (e1) is regulated by phosphorylation-dephosphorylation, catalyzed by the e1-kinase and the phospho-e1-phosphatase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154656 |
Ser300 |
SMSDPGVsYRTREEI |
Homo sapiens |
|
| pmid |
sentence |
| 17474719 |
In mammals, pdhc is tightly regulated by phosphorylation-dephosphorylation of three serine residues in the thiamin-dependent pyruvate dehydrogenase (e1) component. In vivo, inactivation of human pdhc correlates mostly with phosphorylation of serine 264, which is located at the entrance of the substrate channel leading to the active site of e1. |
|
| Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
| + |
AMPK | up-regulates activity
phosphorylation
|
PDHA1 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276835 |
Ser295 |
RYHGHSMsDPGVSYR |
in vitro |
|
| pmid |
sentence |
| 33022274 |
In vitro kinase assay revealed that PDHA could be readily phosphorylated by active AMPK complex in a dose-dependent manner (Figure 6C). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277895 |
Ser295 |
RYHGHSMsDPGVSYR |
in vitro |
|
| pmid |
sentence |
| 33022274 |
AMPK localizes in the mitochondrial matrix and phosphorylates the catalytic alpha subunit of PDHc (PDHA) on two residues S295 and S314, which activates the enzymatic activity of PDHc and alleviates an inhibitory phosphorylation by PDHKs, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277894 |
Ser314 |
IQEVRSKsDPIMLLK |
in vitro |
|
| pmid |
sentence |
| 33022274 |
AMPK localizes in the mitochondrial matrix and phosphorylates the catalytic alpha subunit of PDHc (PDHA) on two residues S295 and S314, which activates the enzymatic activity of PDHc and alleviates an inhibitory phosphorylation by PDHKs, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276836 |
Ser314 |
IQEVRSKsDPIMLLK |
in vitro |
|
| pmid |
sentence |
| 33022274 |
In vitro kinase assay revealed that PDHA could be readily phosphorylated by active AMPK complex in a dose-dependent manner (Figure 6C). |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PRKAA1 | up-regulates activity
phosphorylation
|
PDHA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276837 |
Ser295 |
RYHGHSMsDPGVSYR |
in vitro |
|
| pmid |
sentence |
| 33022274 |
AMPKα phosphorylates PDHA subunit on Ser295 and Ser314 to activate PDH complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276839 |
Ser314 |
IQEVRSKsDPIMLLK |
in vitro |
|
| pmid |
sentence |
| 33022274 |
AMPKα phosphorylates PDHA subunit on Ser295 and Ser314 to activate PDH complex |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKAA2 | up-regulates activity
phosphorylation
|
PDHA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276840 |
Ser295 |
RYHGHSMsDPGVSYR |
in vitro |
|
| pmid |
sentence |
| 33022274 |
AMPKα phosphorylates PDHA subunit on Ser295 and Ser314 to activate PDH complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276838 |
Ser314 |
IQEVRSKsDPIMLLK |
in vitro |
|
| pmid |
sentence |
| 33022274 |
AMPKα phosphorylates PDHA subunit on Ser295 and Ser314 to activate PDH complex |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
SRC | down-regulates activity
phosphorylation
|
PDHA1 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277204 |
Tyr289 |
MELQTYRyHGHSMSD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26848621 |
Src inactivated PDH through direct phosphorylation of tyrosine-289 of PDH E1α subunit (PDHA1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDHA1 | form complex 
binding
|
PDH |
0.805 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266544 |
|
|
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 |
| + |
PDP2 | up-regulates activity
dephosphorylation
|
PDHA1 |
0.655 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251665 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20208177 |
Pyruvate dehydrogenase phosphatase (PDP) is a mitochondrial serine phosphatase that activates phosphorylated pyruvate dehydrogenase complex by dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACAT1 | down-regulates activity
acetylation
|
PDHA1 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267633 |
|
|
|
|
| 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 |
4.0
PDHA1
- 
- 