+ |
CSNK2A1 | up-regulates
phosphorylation
|
PDCL |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146825 |
Ser18 |
EKLQYYYsSSEDEDS |
Homo sapiens |
|
pmid |
sentence |
16717095 |
Phosducin-like protein (phlp) is a widely expressed binding partner of the g protein betagamma subunit complex (gbetagamma) that has been recently shown to catalyze the formation of the gbetagamma dimer from its nascent polypeptides. Phosphorylation of phlp at one or more of three consecutive serines (ser-18, ser-19, and ser-20) is necessary for gbetagamma dimer formation and is believed to be mediated by the protein kinase ck2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146829 |
Ser19 |
KLQYYYSsSEDEDSD |
Homo sapiens |
|
pmid |
sentence |
16717095 |
Phosducin-like protein (phlp) is a widely expressed binding partner of the g protein betagamma subunit complex (gbetagamma) that has been recently shown to catalyze the formation of the gbetagamma dimer from its nascent polypeptides. Phosphorylation of phlp at one or more of three consecutive serines (ser-18, ser-19, and ser-20) is necessary for gbetagamma dimer formation and is believed to be mediated by the protein kinase ck2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146833 |
Ser20 |
LQYYYSSsEDEDSDH |
Homo sapiens |
|
pmid |
sentence |
16717095 |
Phosducin-like protein (phlp) is a widely expressed binding partner of the g protein betagamma subunit complex (gbetagamma) that has been recently shown to catalyze the formation of the gbetagamma dimer from its nascent polypeptides. Phosphorylation of phlp at one or more of three consecutive serines (ser-18, ser-19, and ser-20) is necessary for gbetagamma dimer formation and is believed to be mediated by the protein kinase ck2. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CSNK2A1 |
phosphorylation
|
PDCL |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-146837 |
Ser25 |
SSSEDEDsDHEDKDR |
Homo sapiens |
|
pmid |
sentence |
16717095 |
Together, these data make a strong case for ck2 phosphorylation events within the serines 18-20 and 25 sites in vivo. hey also show that phosphorylation of ser-25 and ser-296 plays no additional role in g__ expression. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |