+ |
PRKACA |
phosphorylation
|
FXYD1 |
0.429 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-171184 |
Ser83 |
EEGTFRSsIRRLSTR |
Homo sapiens |
|
pmid |
sentence |
21220422 |
We conclude that phosphorylation of plm increases its oligomerization into tetramers, decreases its binding to nka, and alters the structures of both the tetramer and nka regulatory complex. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-171188 |
Ser88 |
RSSIRRLsTRRR |
Homo sapiens |
|
pmid |
sentence |
21220422 |
We conclude that phosphorylation of plm increases its oligomerization into tetramers, decreases its binding to nka, and alters the structures of both the tetramer and nka regulatory complex. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKACA | up-regulates activity
phosphorylation
|
FXYD1 |
0.429 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263117 |
Ser83 |
EEGTFRSsIRRLSTR |
in vitro |
|
pmid |
sentence |
15621037 |
PKA-dependent, alpha 1-specific NKA activation may be mediated through phosphorylation of the accessory protein PLM, rather than direct alpha1 subunit phosphorylation. we propose that phosphorylation of the small accessory protein phospholemman (PLM) by PKA at serine 68 is responsible for the observed isoform-specific activation of NKA. |
|
Publications: |
1 |
Organism: |
In Vitro |