+ |
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 |
0.311 |
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 |
+ |
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 |