+ |
CSNK2A2 | up-regulates activity
phosphorylation
|
CDC37 |
0.503 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250982 |
Ser13 |
VWDHIEVsDDEDETH |
in vitro |
|
pmid |
sentence |
12930845 |
Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. | In this report, we demonstrate that mammalian Cdc37 is phosphorylated on Ser13 in situ in rabbit reticulocyte lysate and in cultured K562 cells and that casein kinase II is capable of quantitatively phosphorylating recombinant Cdc37 at this site. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PPP5C | down-regulates activity
dephosphorylation
|
CDC37 |
0.659 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248539 |
Ser13 |
VWDHIEVsDDEDETH |
Homo sapiens |
|
pmid |
sentence |
18922470 |
Activation of protein kinase clients by the Hsp90 system is mediated by the cochaperone protein Cdc37. Cdc37 requires phosphorylation at Ser13|PP5/Ppt1 regulates phosphorylation of Ser13-Cdc37 in vivo, directly affecting activation of protein kinase clients by Hsp90-Cdc37. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK2A1 | up-regulates activity
phosphorylation
|
CDC37 |
0.406 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250838 |
Ser13 |
VWDHIEVsDDEDETH |
in vitro |
|
pmid |
sentence |
12930845 |
Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. | In this report, we demonstrate that mammalian Cdc37 is phosphorylated on Ser13 in situ in rabbit reticulocyte lysate and in cultured K562 cells and that casein kinase II is capable of quantitatively phosphorylating recombinant Cdc37 at this site. |
|
Publications: |
1 |
Organism: |
In Vitro |