| + |
PRKCA |
phosphorylation
|
MARCKS |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248909 |
Ser101 |
AAPEAGAsPVEKEAP |
in vitro |
|
| pmid |
sentence |
| 8034575 |
Of the 7 phosphorylated serine residues identified by Edman degradation, only 1 was within the known phosphorylation domain by protein kinase C. All the other phosphorylated serine residues originated from the N-terminal half of the molecule and were immediately followed by proline. | The other phosphorylated peptides were subjected to the same analysis, and Ser45 (peptide K5), Sel-80(peptide K7), and Ser99 (peptide K8) were confirmed to be the phosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248907 |
Ser118 |
GEAAEPGsPTAAEGE |
in vitro |
|
| pmid |
sentence |
| 8034575 |
Of the 7 phosphorylated serine residues identified by Edman degradation, only 1 was within the known phosphorylation domain by protein kinase C. All the other phosphorylated serine residues originated from the N-terminal half of the molecule and were immediately followed by proline. | We conclude that the primary phosphorylation site is Ser116 | |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139906 |
Ser159 |
KKKKKRFsFKKSFKL |
Homo sapiens |
|
| pmid |
sentence |
| 16116087 |
The present experiments demonstrate that ptn stimulates phosphorylation of serines 713 and 726 in the marcks domain of _-adducin (and serine 724 in _-adducin) and serines 152 and 156 in the marcks protein itself through the activation of either pkc _ or _ and perhaps other pkc(s) isoforms. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248925 |
Ser159 |
KKKKKRFsFKKSFKL |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139910 |
Ser163 |
KRFSFKKsFKLSGFS |
Homo sapiens |
|
| pmid |
sentence |
| 16116087 |
The present experiments demonstrate that ptn stimulates phosphorylation of serines 713 and 726 in the marcks domain of _-adducin (and serine 724 in _-adducin) and serines 152 and 156 in the marcks protein itself through the activation of either pkc _ or _ and perhaps other pkc(s) isoforms. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248928 |
Ser163 |
KRFSFKKsFKLSGFS |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248931 |
Ser170 |
SFKLSGFsFKKNKKE |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248908 |
Ser46 |
VKVNGDAsPAAAESG |
in vitro |
|
| pmid |
sentence |
| 8034575 |
Of the 7 phosphorylated serine residues identified by Edman degradation, only 1 was within the known phosphorylation domain by protein kinase C. All the other phosphorylated serine residues originated from the N-terminal half of the molecule and were immediately followed by proline. | The other phosphorylated peptides were subjected to the same analysis, and Ser45 (peptide K5), Sel-80(peptide K7), and Ser99 (peptide K8) were confirmed to be the phosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248910 |
Ser81 |
AAGSGAAsPSAAEKG |
in vitro |
|
| pmid |
sentence |
| 8034575 |
Of the 7 phosphorylated serine residues identified by Edman degradation, only 1 was within the known phosphorylation domain by protein kinase C. All the other phosphorylated serine residues originated from the N-terminal half of the molecule and were immediately followed by proline. | The other phosphorylated peptides were subjected to the same analysis, and Ser45 (peptide K5), Sel-80(peptide K7), and Ser99 (peptide K8) were confirmed to be the phosphorylation sites. |
|
| Publications: |
9 |
Organism: |
In Vitro, Homo Sapiens |
| + |
PRKCD |
phosphorylation
|
MARCKS |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248924 |
Ser159 |
KKKKKRFsFKKSFKL |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248927 |
Ser163 |
KRFSFKKsFKLSGFS |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248930 |
Ser170 |
SFKLSGFsFKKNKKE |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PKN1 |
phosphorylation
|
MARCKS |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248937 |
Ser159 |
KKKKKRFsFKKSFKL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248938 |
Ser163 |
KRFSFKKsFKLSGFS |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248939 |
Ser170 |
SFKLSGFsFKKNKKE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKCA | down-regulates activity 
phosphorylation
|
MARCKS |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243192 |
Ser159 |
KKKKKRFsFKKSFKL |
in vitro |
|
| pmid |
sentence |
| 1560845 |
Here we report that MARCKS is a filamentous (F) actin crosslinking protein, with activity that is inhibited by PKC-mediated phosphorylation and by binding to calcium-calmodulin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249650 |
Ser163 |
KRFSFKKsFKLSGFS |
in vitro |
|
| pmid |
sentence |
| 1560845 |
Here we report that MARCKS is a filamentous (F) actin crosslinking protein, with activity that is inhibited by PKC-mediated phosphorylation and by binding to calcium-calmodulin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249670 |
Ser170 |
SFKLSGFsFKKNKKE |
in vitro |
|
| pmid |
sentence |
| 1560845 |
Here we report that MARCKS is a filamentous (F) actin crosslinking protein, with activity that is inhibited by PKC-mediated phosphorylation and by binding to calcium-calmodulin |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PKN1 | down-regulates activity
phosphorylation
|
MARCKS |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243199 |
Ser159 |
KKKKKRFsFKKSFKL |
in vitro |
|
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249651 |
Ser163 |
KRFSFKKsFKLSGFS |
in vitro |
|
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249671 |
Ser170 |
SFKLSGFsFKKNKKE |
in vitro |
|
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKCB |
phosphorylation
|
MARCKS |
0.663 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248923 |
Ser159 |
KKKKKRFsFKKSFKL |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248926 |
Ser163 |
KRFSFKKsFKLSGFS |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248929 |
Ser170 |
SFKLSGFsFKKNKKE |
in vitro |
|
| pmid |
sentence |
| 8422248 |
These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III. |
|
| Publications: |
3 |
Organism: |
In Vitro |
3.0
MARCKS
- 
- 