+ |
PKA | up-regulates activity
phosphorylation
|
PDE4D |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273939 |
Ser125 |
CRAMDRTsYAVETGH |
Chlorocebus aethiops |
|
pmid |
sentence |
12023945 |
Long PDE4 isoforms from all four sub-families can be phosphorylated by protein kinase A (PKA). This leads to an increase in their activity and may thus contribute to cellular desensitization processes in cells where these isoforms are selectively expressed.These were Ser89Ala-PDE4A8, Ser133Ala-PDE4B1, Ser13Ala-PDE4C2 and Ser126Ala-PDE4D5. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275988 |
Ser125 |
CRAMDRTsYAVETGH |
Chlorocebus aethiops |
|
pmid |
sentence |
12023945 |
Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms. |
|
Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
+ |
MAPK1 | down-regulates
phosphorylation
|
PDE4D (isoform 2) |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-77563 |
Ser579 |
YQSTIPQsPSPAPDD |
Homo sapiens |
|
pmid |
sentence |
10828059 |
The pde4d2 isoform is inhibited by erk2 phosphorylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK1 | down-regulates
phosphorylation
|
PDE4D |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-64326 |
Ser715 |
YQSTIPQsPSPAPDD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10022832 |
These straddle the target residue, ser(579), for erk2 phosphorylation of pde4d3. Mutation of either or both of these docking sites prevented erk2 from being co-immunoprecipitated with pde4d3, ablated the ability of epidermal growth factor to inhibit pde4d3 through erk2 action in transfected cos cells, and attenuated the ability of erk2 to phosphorylate pde4d3 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-149570 |
Ser715 |
YQSTIPQsPSPAPDD |
Homo sapiens |
Macrophage |
pmid |
sentence |
16973330 |
These straddle the target residue, ser(579), for erk2 phosphorylation of pde4d3. Mutation of either or both of these docking sites prevented erk2 from being co-immunoprecipitated with pde4d3, ablated the ability of epidermal growth factor to inhibit pde4d3 through erk2 action in transfected cos cells, and attenuated the ability of erk2 to phosphorylate pde4d3 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-77571 |
Ser715 |
YQSTIPQsPSPAPDD |
Homo sapiens |
|
pmid |
sentence |
10828059 |
These straddle the target residue, ser(579), for erk2 phosphorylation of pde4d3. Mutation of either or both of these docking sites prevented erk2 from being co-immunoprecipitated with pde4d3, ablated the ability of epidermal growth factor to inhibit pde4d3 through erk2 action in transfected cos cells, and attenuated the ability of erk2 to phosphorylate pde4d3 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-77574 |
|
|
Homo sapiens |
|
pmid |
sentence |
10828059 |
Long pde4d forms are inhibited by erk2 phosphorylation |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
MAPK3 | down-regulates
phosphorylation
|
PDE4D |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-77578 |
Ser715 |
YQSTIPQsPSPAPDD |
Homo sapiens |
|
pmid |
sentence |
10828059 |
These straddle the target residue, ser(579), for erk2 phosphorylation of pde4d3. Mutation of either or both of these docking sites prevented erk2 from being co-immunoprecipitated with pde4d3, ablated the ability of epidermal growth factor to inhibit pde4d3 through erk2 action in transfected cos cells, and attenuated the ability of erk2 to phosphorylate pde4d3 in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Gbeta | down-regulates
phosphorylation
|
PDE4D |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270069 |
|
|
Homo sapiens |
|
pmid |
sentence |
10828059 |
These straddle the target residue, ser(579), for erk2 phosphorylation of pde4d3. Mutation of either or both of these docking sites prevented erk2 from being co-immunoprecipitated with pde4d3, ablated the ability of epidermal growth factor to inhibit pde4d3 through erk2 action in transfected cos cells, and attenuated the ability of erk2 to phosphorylate pde4d3 in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKACA | up-regulates
phosphorylation
|
PDE4D |
0.562 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-42515 |
|
|
Homo sapiens |
|
pmid |
sentence |
8663227 |
Phosphorylation and activation of a camp-specific phosphodiesterase by the camp-dependent protein kinase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ERK1/2 | down-regulates
phosphorylation
|
PDE4D |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270174 |
|
|
Homo sapiens |
|
pmid |
sentence |
10828059 |
These straddle the target residue, ser(579), for erk2 phosphorylation of pde4d3. Mutation of either or both of these docking sites prevented erk2 from being co-immunoprecipitated with pde4d3, ablated the ability of epidermal growth factor to inhibit pde4d3 through erk2 action in transfected cos cells, and attenuated the ability of erk2 to phosphorylate pde4d3 in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK1 | up-regulates
phosphorylation
|
PDE4D |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-77559 |
|
|
Homo sapiens |
|
pmid |
sentence |
10828059 |
The short pde4d1 isoenzyme is activated by erk2 phosphorylation this signifies that erk2 phosphorylated pde4d1 at a single site, ser491, that is cognate to the single erk2 phosphorylation site (ser579) found in pde4d3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |