+ |
PDK2 | down-regulates activity
phosphorylation
|
PDHA1 |
0.667 |
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 |
+ |
PDK2 | down-regulates
phosphorylation
|
PDHA1 |
0.667 |
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 |
+ |
PDK2 | down-regulates
phosphorylation
|
PDHA2 |
0.529 |
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 |
+ |
PDK2 | up-regulates activity
phosphorylation
|
AKT1 |
0.74 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249630 |
Ser473 |
RPHFPQFsYSASGTA |
|
|
pmid |
sentence |
19951971 |
PIP3 recruits PDK1 and AKT to the plasma membrane, where PDK1 phosphorylates AKT on Thr308 in the activation loop of the kinase domain. The phosphorylation of AKT on Ser473 by PDK2 acts as a gain control for AKT and regulates its degree of activation. The sirolimus-insensitive mTORC2 complex exhibits PDK2 activity |
|
Publications: |
1 |