+ |
SGK3 | up-regulates
phosphorylation
|
FLII |
0.364 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184688 |
Ser436 |
RLRRRKDsAQDDQAK |
Homo sapiens |
|
pmid |
sentence |
19293151 |
Here we show that flii is an in vivo substrate of cisk that functions downstream of pi 3-kinase. Cisk can associate with flii and phosphorylate flii at residues ser(436) and thr(818).We demonstrate here that cisk can enhance er transcription, which is dependent on its kinase activity, and mutation of cisk phosphorylation sites on flii attenuates its activity as an er co-activator. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184692 |
Thr818 |
LHRPRHAtVSRSLEG |
Homo sapiens |
|
pmid |
sentence |
19293151 |
Here we show that flii is an in vivo substrate of cisk that functions downstream of pi 3-kinase. Cisk can associate with flii and phosphorylate flii at residues ser(436) and thr(818).We demonstrate here that cisk can enhance er transcription, which is dependent on its kinase activity, and mutation of cisk phosphorylation sites on flii attenuates its activity as an er co-activator. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |