| + |
DAPK1 | up-regulates activity 
phosphorylation
|
TPM1 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262845 |
Ser283 |
HALNDMTsI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17895359 |
We identified, for the first time, death-associated protein kinase 1 (DAP kinase 1) as the kinase that phosphorylates tropomyosin-1 in response to ERK activation by hydrogen peroxide (H(2)O(2)). We also report that the phosphorylation of tropomyosin-1 mediated by DAP kinase occurs on Ser283. Our finding that tropomyosin-1 is phosphorylated downstream of ERK and DAP kinase and that it helps regulate the formation of stress fibers will aid understanding the role of this protein in regulating the endothelial functions associated with cytoskeletal remodeling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIK3CA | up-regulates activity
phosphorylation
|
TPM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263027 |
Ser61 |
EDELDKYsEALKDAQ |
in vitro |
|
| pmid |
sentence |
| 16094730 |
Here, we demonstrate a requirement for the protein kinase activity of PI(3)K in agonist-dependent beta-adrenergic receptor (betaAR) internalization. Using PI(3)K mutants with either protein or lipid phosphorylation activity, we identify the cytoskeletal protein non-muscle tropomyosin as a substrate of PI(3)K, which is phosphorylated in a wortmannin-sensitive manner on residue Ser 61. A constitutively dephosphorylated (S61A) tropomyosin mutant blocks agonist-dependent betaAR internalization, whereas a tropomyosin mutant that mimics constitutive phosphorylation (S61D) complements the PI(3)K mutant, with only lipid phosphorylation activity reversing the defective betaAR internalization. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
TPM1
- 
- 