| + |
GSK3B | up-regulates activity 
phosphorylation
|
RCAN1 |
0.498 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249359 |
Ser163 |
PDKQFLIsPPASPPV |
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12063245 |
Consensus phosphorylation sites for p42/44 MAPK and GSK-3 are present in the SP repeat of MCIP1 at serine 112 and serine 108, respectively |Several endogenous proteins are capable of inhibiting the catalytic activity of calcineurin. Modulatory calcineurin interacting protein 1 (MCIP1) is unique among these proteins on the basis of its pattern of expression and its function in a negative feedback loop to regulate calcineurin activity. Here we show that MCIP1 can be phosphorylated by MAPK and glycogen synthase kinase-3 and that phosphorylated MCIP1 is a substrate for calcineurin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DYRK1A | up-regulates
phosphorylation
|
RCAN1 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139958 |
Ser167 |
FLISPPAsPPVGWKQ |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16126726 |
We show that rcan1 self-associates and forms multimers, and that this process is promoted by the dyrk1a-mediated phosphorylation of rcan1 at the thr(192) residue. these results suggest that the phosphorylation of rcan1 by dyrk1a stimulates the formation of insoluble aggregates upon aging. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102290 |
Ser167 |
FLISPPAsPPVGWKQ |
Homo sapiens |
|
| pmid |
sentence |
| 12809556 |
In the present study, dyrk1a is shown to directly interact with and phosphorylate rcan1 at ser112 and thr192 residues. Dyrk1a-mediated phosphorylation of rcan1 at ser112 primes the protein for the gsk3_-mediated phosphorylation of ser108. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAP3K3 | up-regulates
phosphorylation
|
RCAN1 |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138945 |
Ser167 |
FLISPPAsPPVGWKQ |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16126726 |
Essential role of mekk3 signaling in angiotensin ii-induced calcineurin/nuclear factor of activated t-cells activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102294 |
Ser167 |
FLISPPAsPPVGWKQ |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 12809556 |
Essential role of mekk3 signaling in angiotensin ii-induced calcineurin/nuclear factor of activated t-cells activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
RCAN1 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249198 |
Ser167 |
FLISPPAsPPVGWKQ |
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12063245 |
Consensus phosphorylation sites for p42/44 MAPK and GSK-3 are present in the SP repeat of MCIP1 at serine 112 and serine 108, respectively |Several endogenous proteins are capable of inhibiting the catalytic activity of calcineurin. Modulatory calcineurin interacting protein 1 (MCIP1) is unique among these proteins on the basis of its pattern of expression and its function in a negative feedback loop to regulate calcineurin activity. Here we show that MCIP1 can be phosphorylated by MAPK and glycogen synthase kinase-3 and that phosphorylated MCIP1 is a substrate for calcineurin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MAPK3 | up-regulates activity
phosphorylation
|
RCAN1 |
0.389 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249478 |
Ser167 |
FLISPPAsPPVGWKQ |
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12063245 |
Consensus phosphorylation sites for p42/44 MAPK and GSK-3 are present in the SP repeat of MCIP1 at serine 112 and serine 108, respectively |Several endogenous proteins are capable of inhibiting the catalytic activity of calcineurin. Modulatory calcineurin interacting protein 1 (MCIP1) is unique among these proteins on the basis of its pattern of expression and its function in a negative feedback loop to regulate calcineurin activity. Here we show that MCIP1 can be phosphorylated by MAPK and glycogen synthase kinase-3 and that phosphorylated MCIP1 is a substrate for calcineurin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
JUN | up-regulates quantity by expression 
transcriptional regulation
|
RCAN1 |
0.283 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253148 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 18641051 |
Taken together, our findings suggest that c-Jun, a transcription factor downstream of the JNK signaling pathway, up-regulates Adapt78 expression in response to TG-induced ER stress and contributes to protection against TG-induced cell death. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
RCAN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270149 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12063245 |
Consensus phosphorylation sites for p42/44 MAPK and GSK-3 are present in the SP repeat of MCIP1 at serine 112 and serine 108, respectively |Several endogenous proteins are capable of inhibiting the catalytic activity of calcineurin. Modulatory calcineurin interacting protein 1 (MCIP1) is unique among these proteins on the basis of its pattern of expression and its function in a negative feedback loop to regulate calcineurin activity. Here we show that MCIP1 can be phosphorylated by MAPK and glycogen synthase kinase-3 and that phosphorylated MCIP1 is a substrate for calcineurin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
HES1 | down-regulates quantity by repression 
transcriptional regulation
|
RCAN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252026 |
|
|
Mus musculus |
Keratinocyte |
| pmid |
sentence |
| 15866158 |
Increased Calcineurin/NFAT activity by Notch signaling involves downregulation of Calcipressin, an endogenous Calcineurin inhibitor, through a HES-1-dependent mechanism .... Chromatin immunoprecipitation (ChIP) analysis of keratinocytes overexpressing HES-1 showed that this protein can bind to the HES binding sites present in both distal and proximal promoters |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RCAN1 | down-regulates activity
binding
|
PPP3CA |
0.655 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252025 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12554096 |
MCIP proteins can bind to and inhibit calcineurin, a calcium/calmodulin-regulated serine/threonine protein phosphatase that is activated during cardiac hypertrophy and failure |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RCAN1 | down-regulates activity
binding
|
Calcineurin |
0.626 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252341 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12554096 |
MCIP proteins can bind to and inhibit calcineurin, a calcium/calmodulin-regulated serine/threonine protein phosphatase that is activated during cardiac hypertrophy and failure |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates activity
phosphorylation
|
RCAN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270026 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12063245 |
Consensus phosphorylation sites for p42/44 MAPK and GSK-3 are present in the SP repeat of MCIP1 at serine 112 and serine 108, respectively |Several endogenous proteins are capable of inhibiting the catalytic activity of calcineurin. Modulatory calcineurin interacting protein 1 (MCIP1) is unique among these proteins on the basis of its pattern of expression and its function in a negative feedback loop to regulate calcineurin activity. Here we show that MCIP1 can be phosphorylated by MAPK and glycogen synthase kinase-3 and that phosphorylated MCIP1 is a substrate for calcineurin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
RCAN1
- 
- 