+ |
CSNK2A1 | up-regulates
phosphorylation
|
PTGES3 |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123594 |
Ser113 |
WKDWEDDsDEDMSNF |
Homo sapiens |
|
pmid |
sentence |
15040786 |
Several lines of evidence suggest that a cpges-activating protein kinase is ck-ii (casein kinase ii). Recombinant cpges was phosphorylated directly by and associated with ck-ii in vitro, resulting in marked reduction of the k m for the substrate pgh2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123598 |
Ser118 |
DDSDEDMsNFDRFSE |
Homo sapiens |
|
pmid |
sentence |
15040786 |
Cpges-activating protein kinase is ck-ii (casein kinase ii). Mutations of either of two predicted ck-ii phosphorylation sites on cpges (ser113 and ser118) abrogated its phosphorylation and activation both in vitro and in vivo. Hypoxia induced the mitogen-activated protein kinase-mediated phosphorylation of a single serine residue, ser(122), in the protein, and site-directed mutagenesis demonstrated that ser(122) phosphorylation was necessary for hypoxic acceleration of tal1 turnover. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PTGES3 | up-regulates activity
binding
|
HSP90AA1 |
0.913 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262831 |
|
|
in vitro |
|
pmid |
sentence |
9817749 |
The mutant Hsp90 proteins tested are defective in the binding and ATP hydrolysis-dependent cycling of the co-chaperone p23, which is thought to regulate the binding and release of substrate polypeptide from Hsp90. |
|
Publications: |
1 |
Organism: |
In Vitro |