| + |
CAMK2A | down-regulates 
phosphorylation
|
CALD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22631 |
Ser643 |
CFTPKGSsLKIEERA |
Homo sapiens |
|
| pmid |
sentence |
| 2170388 |
Smooth muscle caldesmon was phosphorylated by smooth muscle calmodulin-dependent protein kinase. Ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22635 |
Ser656 |
RAEFLNKsVQKSSGV |
Homo sapiens |
|
| pmid |
sentence |
| 2170388 |
Smooth muscle caldesmon was phosphorylated by smooth muscle calmodulin-dependent protein kinase. Ii |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Smooth Muscle |
| + |
PRKCA | down-regulates
phosphorylation
|
CALD1 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36788 |
Ser643 |
CFTPKGSsLKIEERA |
Homo sapiens |
|
| pmid |
sentence |
| 8182108 |
Phosphorylation of both intact caldesmon and of its c-terminal fragment (658c), containing residues 658-756, significantly decreased their ability to inhibit acto-heavy meromyosin atpase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36792 |
Ser656 |
RAEFLNKsVQKSSGV |
Homo sapiens |
|
| pmid |
sentence |
| 8182108 |
Phosphorylation of both intact caldesmon and of its c-terminal fragment (658c), containing residues 658-756, significantly decreased their ability to inhibit acto-heavy meromyosin atpase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36796 |
Ser677 |
AIVSKIDsRLEQYTS |
Homo sapiens |
|
| pmid |
sentence |
| 8182108 |
Phosphorylation of both intact caldesmon and of its c-terminal fragment (658c), containing residues 658-756, significantly decreased their ability to inhibit acto-heavy meromyosin atpase. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
PAK3 | down-regulates
phosphorylation
|
CALD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167976 |
Ser714 |
EGVRNIKsMWEKGNV |
Homo sapiens |
|
| pmid |
sentence |
| 20858431 |
We investigated the effects of phosphorylation by p(21)-activated kinase 3 (pak) and calmodulin on the 22 kda c-terminal fragment of caldesmon (cad22). We substituted the major pak sites, ser-672 and ser-702, with either alanine or aspartic acid to mimic nonphosphorylated and constitutively phosphorylated states of caldesmon, respectively. Phosphorylation at these sites weakened ca(2+)-calmodulin binding further and reduced the inhibitory activity of cad22 in the absence of ca(2+)-calmodulin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167980 |
Ser744 |
GLKVGVSsRINEWLT |
Homo sapiens |
|
| pmid |
sentence |
| 20858431 |
We investigated the effects of phosphorylation by p(21)-activated kinase 3 (pak) and calmodulin on the 22 kda c-terminal fragment of caldesmon (cad22). We substituted the major pak sites, ser-672 and ser-702, with either alanine or aspartic acid to mimic nonphosphorylated and constitutively phosphorylated states of caldesmon, respectively. Phosphorylation at these sites weakened ca(2+)-calmodulin binding further and reduced the inhibitory activity of cad22 in the absence of ca(2+)-calmodulin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
MYLK | down-regulates
phosphorylation
|
CALD1 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166049 |
Ser744 |
GLKVGVSsRINEWLT |
Homo sapiens |
|
| pmid |
sentence |
| 20536391 |
Phosphorylation of caldesmon by myosin light chain kinase increases its binding affinity for phosphorylated myosin filaments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates
phosphorylation
|
CALD1 |
0.524 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71033 |
Ser759 |
KTPDGNKsPAPKPSD |
Homo sapiens |
|
| pmid |
sentence |
| 10514499 |
Extracellular signal-regulated kinases (erks) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-cad) at two sites (ser(759) and ser(789)) during smooth muscle stimulation. Nmr spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to f-actin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71037 |
Ser789 |
QSVDKVTsPTKV |
Homo sapiens |
|
| pmid |
sentence |
| 10514499 |
Extracellular signal-regulated kinases (erks) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-cad) at two sites (ser(759) and ser(789)) during smooth muscle stimulation. Nmr spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to f-actin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Smooth Muscle |
| + |
MAPK3 | down-regulates
phosphorylation
|
CALD1 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86741 |
Ser759 |
KTPDGNKsPAPKPSD |
Homo sapiens |
|
| pmid |
sentence |
| 11983427 |
The actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759. This phosphorylation leads to markedly diminished actin affinity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71041 |
Ser759 |
KTPDGNKsPAPKPSD |
Homo sapiens |
|
| pmid |
sentence |
| 10514499 |
Extracellular signal-regulated kinases (erks) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-cad) at two sites (ser(759) and ser(789)) during smooth muscle stimulation. Nmr spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to f-actin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71045 |
Ser789 |
QSVDKVTsPTKV |
Homo sapiens |
|
| pmid |
sentence |
| 10514499 |
Extracellular signal-regulated kinases (erks) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-cad) at two sites (ser(759) and ser(789)) during smooth muscle stimulation. Nmr spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to f-actin. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle, Smooth Muscle |
| + |
ERK1/2 | down-regulates
phosphorylation
|
CALD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270162 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10514499 |
Extracellular signal-regulated kinases (erks) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-cad) at two sites (ser(759) and ser(789)) during smooth muscle stimulation. Nmr spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to f-actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Smooth Muscle |
| + |
Gbeta | down-regulates
phosphorylation
|
CALD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270049 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10514499 |
Extracellular signal-regulated kinases (erks) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-cad) at two sites (ser(759) and ser(789)) during smooth muscle stimulation. Nmr spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to f-actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Smooth Muscle |
3.0
CALD1
- 
- 