| + |
NUAK1 | down-regulates 
phosphorylation
|
PPP1R12A |
0.522 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164747 |
Ser445 |
LGLRKTGsYGALAEI |
Homo sapiens |
|
| pmid |
sentence |
| 20354225 |
Phosphorylation of ser(445), ser(472), and ser(910) of mypt1 by nuak1 promoted the interaction of mypt1 with 14-3-3 adaptor proteins, thereby suppressing phosphatase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164751 |
Ser472 |
AGVTRSAsSPRLSSS |
Homo sapiens |
|
| pmid |
sentence |
| 20354225 |
Phosphorylation of ser(445), ser(472), and ser(910) of mypt1 by nuak1 promoted the interaction of mypt1 with 14-3-3 adaptor proteins, thereby suppressing phosphatase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22572 |
Ser910 |
SLLGRSGsYSYLEER |
Homo sapiens |
|
| pmid |
sentence |
| 20354225 |
Phosphorylation of ser(445), ser(472), and ser(910) of mypt1 by nuak1 promoted the interaction of mypt1 with 14-3-3 adaptor proteins, thereby suppressing phosphatase activity. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ILK | down-regulates activity
phosphorylation
|
PPP1R12A |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262884 |
Thr500 |
RLAYVAPtIPRRLAS |
in vitro |
|
| pmid |
sentence |
| 12030846 |
MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). ILK produced an intermediate level of inhibition |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262886 |
Thr696 |
ARQSRRStQGVTLTD |
in vitro |
|
| pmid |
sentence |
| 12030846 |
MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). ILK produced an intermediate level of inhibition |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262885 |
Thr710 |
DLQEAEKtIGRSRST |
in vitro |
|
| pmid |
sentence |
| 12030846 |
MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). ILK produced an intermediate level of inhibition |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ROCK1 | down-regulates
phosphorylation
|
PPP1R12A |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42354 |
Thr696 |
ARQSRRStQGVTLTD |
Homo sapiens |
|
| pmid |
sentence |
| 8662509 |
Rho-associated kinase (rho-kinase) phosphorylated mbs and consequently inactivated myosin phosphatase. Rho appears to inhibit myosin phosphatase through the action of rho-kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ILK | down-regulates
phosphorylation
|
PPP1R12A |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87924 |
Thr696 |
ARQSRRStQGVTLTD |
Homo sapiens |
|
| pmid |
sentence |
| 12030846 |
Mypt1 was phosphorylated by ilk and phosphorylation sites in the n- and c-terminal fragments of mypt1 were detected. From sequence analyses, three sites were identified: a primary site at thr(709), and two other sites at thr(695) and thr(495) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87928 |
Thr710 |
DLQEAEKtIGRSRST |
Homo sapiens |
|
| pmid |
sentence |
| 12030846 |
Mypt1 was phosphorylated by ilk and phosphorylation sites in the n- and c-terminal fragments of mypt1 were detected. From sequence analyses, three sites were identified: a primary site at thr(709), and two other sites at thr(695) and thr(495). phosphorylation of the various sites indicated that thr695 was the major inhibitory site, thr709 had only a slight inhibitory effect |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ROCK2 | down-regulates activity
phosphorylation
|
PPP1R12A |
0.777 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249164 |
Thr853 |
PREKRRStGVSFWTQ |
in vitro |
|
| pmid |
sentence |
| 12220642 |
Rho kinase is known to control smooth muscle contractility by phosphorylating the 110 kDa myosin-targetting subunit (MYPT1) of the myosin-associated form of protein phosphatase 1 (PP1M). Phosphorylation of MYPT1 at Thr695 has previously been reported to inhibit the catalytic activity of PP1. Here, we show that the phosphorylation of Thr850 by Rho kinase dissociates PP1M from myosin, providing a second mechanism by which myosin phosphatase activity is inhibited. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
PPP1R12A |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249034 |
Thr853 |
PREKRRStGVSFWTQ |
Mus musculus |
|
| pmid |
sentence |
| 10601309 |
Phosphorylation by Rho-kinase inhibited MP activity and this reflected a decrease in V(max). Activity of MP with different substrates also was inhibited by phosphorylation. Two major sites of phosphorylation on MYPT1 were Thr(695) and Thr(850). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
PPP1R12A
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