+ |
PASK | up-regulates activity
phosphorylation
|
PASK |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109481 |
Thr1161 |
ERGKLFYtFCGTIEY |
in vitro |
|
pmid |
sentence |
11459942 |
We present evidence that the activity of pask is regulated by two mechanisms. Autophosphorylation at two threonine residues located within the activation loop significantly increases catalytic activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-109485 |
Thr1165 |
LFYTFCGtIEYCAPE |
in vitro |
|
pmid |
sentence |
11459942 |
We present evidence that the activity of pask is regulated by two mechanisms. Autophosphorylation at two threonine residues located within the activation loop significantly increases catalytic activity. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
PASK |
phosphorylation
|
EEF1A1 |
0.381 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-245862 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17595531 |
Kinase assays, mass spectrometry and site-directed mutagenesis revealed PASKIN auto-phosphorylation as well as eEF1A1 target phosphorylation mainly but not exclusively at Thr432. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PASK | down-regulates activity
phosphorylation
|
GYS1 |
0.523 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-245866 |
|
|
in vitro |
|
pmid |
sentence |
16275910 |
Recombinant human PASK (hPASK) phosphorylates purified muscle glycogen synthase, causing robust inactivation. Furthermore, hPASK interacts directly with glycogen synthase when expressed in cultured cells and this interaction and the phosphorylation of glycogen synthase by human PASK (hPASK) are inhibited by glycogen. |
|
Publications: |
1 |
Organism: |
In Vitro |