| + |
PRKCB | down-regulates quantity
phosphorylation
|
MEP1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263173 |
Ser687 |
KKYRERMsSNRPNLT |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12941954 |
These findings suggest that activation of a protein kinase, presumably PKC, mediates PMA-induced hmeprinβ shedding. By labeling COS-1 cells transfected with mutant constructs lacking the potential phosphorylation sites, we identified Ser687 as the main 32P-acceptor. These data provide evidence that the cytoplasmic domain of hmeprinβ can function as a PKC substrate. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKCA | down-regulates quantity
phosphorylation
|
MEP1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263172 |
Ser687 |
KKYRERMsSNRPNLT |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12941954 |
These findings suggest that activation of a protein kinase, presumably PKC, mediates PMA-induced hmeprinβ shedding. By labeling COS-1 cells transfected with mutant constructs lacking the potential phosphorylation sites, we identified Ser687 as the main 32P-acceptor. These data provide evidence that the cytoplasmic domain of hmeprinβ can function as a PKC substrate. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKCD | down-regulates quantity
phosphorylation
|
MEP1B |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263171 |
Ser687 |
KKYRERMsSNRPNLT |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12941954 |
These findings suggest that activation of a protein kinase, presumably PKC, mediates PMA-induced hmeprinβ shedding. By labeling COS-1 cells transfected with mutant constructs lacking the potential phosphorylation sites, we identified Ser687 as the main 32P-acceptor. These data provide evidence that the cytoplasmic domain of hmeprinβ can function as a PKC substrate. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |