| + |
PPP2CB |
dephosphorylation
|
PPP1R1A |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248602 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PPP3CC |
dephosphorylation
|
PPP1R1A |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248524 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PPP2CA |
dephosphorylation
|
PPP1R1A |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248645 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CDK5 |
phosphorylation
|
PPP1R1A |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249194 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PPP3CA |
dephosphorylation
|
PPP1R1A |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248693 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PPP3CB |
dephosphorylation
|
PPP1R1A |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248379 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
Calcineurin |
dephosphorylation
|
PPP1R1A |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252334 |
Ser67 |
LKSTLAMsPRQRKKM |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PP2B |
dephosphorylation
|
PPP1R1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269991 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 11278334 |
In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. | However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
4.0
PPP1R1A
- 
- 