| + |
PRKACA | down-regulates activity 
phosphorylation
|
PPP1R8 |
0.496 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250032 |
Ser178 |
TAHNKRIsTLTIEEG |
in vitro |
|
| pmid |
sentence |
| 9407077 |
NIPP-1 is the RNA-binding subunit of a major species of protein phosphatase-1 in the nucleus. The purified recombinant protein was a potent (Ki = 9.9 +/- 0.3 pM) and specific inhibitor of protein phosphatase-1 and was stoichiometrically phosphorylated by protein kinases A and CK2. At physiological ionic strength, phosphorylation by these protein kinases drastically decreased the inhibitory potency of free NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250033 |
Ser199 |
PKRKRKNsRVTFSED |
in vitro |
|
| pmid |
sentence |
| 9407077 |
NIPP-1 is the RNA-binding subunit of a major species of protein phosphatase-1 in the nucleus. The purified recombinant protein was a potent (Ki = 9.9 +/- 0.3 pM) and specific inhibitor of protein phosphatase-1 and was stoichiometrically phosphorylated by protein kinases A and CK2. At physiological ionic strength, phosphorylation by these protein kinases drastically decreased the inhibitory potency of free NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSNK2A2 | up-regulates activity 
phosphorylation
|
PPP1R8 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251023 |
Ser204 |
KNSRVTFsEDDEIIN |
in vitro |
|
| pmid |
sentence |
| 9407077 |
Phosphorylation of NIPP-1 in a heterodimeric complex with the catalytic subunit of protein phosphatase-1 resulted in an activation of the holoenzyme without a release of NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A, whereas Thr161 and Ser204 were phosphorylated by protein kinase CK2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251024 |
Thr161 |
LGLPEEEtELDNLTE |
in vitro |
|
| pmid |
sentence |
| 9407077 |
Phosphorylation of NIPP-1 in a heterodimeric complex with the catalytic subunit of protein phosphatase-1 resulted in an activation of the holoenzyme without a release of NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A, whereas Thr161 and Ser204 were phosphorylated by protein kinase CK2. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSNK2A1 | up-regulates activity
phosphorylation
|
PPP1R8 |
0.482 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250930 |
Ser204 |
KNSRVTFsEDDEIIN |
in vitro |
|
| pmid |
sentence |
| 9407077 |
Phosphorylation of NIPP-1 in a heterodimeric complex with the catalytic subunit of protein phosphatase-1 resulted in an activation of the holoenzyme without a release of NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A, whereas Thr161 and Ser204 were phosphorylated by protein kinase CK2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250931 |
Thr161 |
LGLPEEEtELDNLTE |
in vitro |
|
| pmid |
sentence |
| 9407077 |
Phosphorylation of NIPP-1 in a heterodimeric complex with the catalytic subunit of protein phosphatase-1 resulted in an activation of the holoenzyme without a release of NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A, whereas Thr161 and Ser204 were phosphorylated by protein kinase CK2. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
LYN | down-regulates activity
phosphorylation
|
PPP1R8 |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251405 |
Tyr264 |
FAFSGGLyGGLPPTH |
in vitro |
|
| pmid |
sentence |
| 11104670 |
Tyrosine phosphorylation of NIPP1 by Lyn was abolished by the Tyr-264 to Asp mutation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251406 |
Tyr335 |
NEPKKKKyAKEAWPG |
in vitro |
|
| pmid |
sentence |
| 11104670 |
Lyn phosphorylates both Tyr-264 and Tyr-335, but that the phosphorylation of Tyr-335 is dependent on the association of NIPP1 with RNA. The inhibitory potency of the C-terminal site of NIPP1 was decreased by phosphorylation of Tyr-335 and by the addition of RNA. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PPP1R8 | down-regulates activity
binding
|
PPP1CA |
0.64 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255657 |
|
|
in vitro |
|
| pmid |
sentence |
| 1322907 |
We have purified two of these nuclear inhibitors of PP-1 (NIPP-1a and NIPP-1b) until homogeneity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP1R8 | up-regulates activity
binding
|
EZH2 |
0.367 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255665 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23241245 |
Recruited NIPP1 enables the net phosphorylation of EZH2 by inhibiting its dephosphorylation by PP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1R8 | down-regulates activity
binding
|
PP1 |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264673 |
|
|
in vitro |
|
| pmid |
sentence |
| 1322907 |
We have purified two of these nuclear inhibitors of PP-1 (NIPP-1a and NIPP-1b) until homogeneity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
PPP1R8
- 
- 