| + |
PRKCD | up-regulates 
phosphorylation
|
MYBPC3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150347 |
Ser275 |
LSAFRRTsLAGGGRR |
Homo sapiens |
|
| pmid |
sentence |
| 17075052 |
The triple aspartic acid mutation shows greater distance between the two thick myosin filaments (affects the steric arrangement of the filament distances) in heart tissue. Mutation is cardioprotective during stress (ischemia-reprofusion injury) against apoptosis similar to isoproterenol treatment. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150351 |
Ser284 |
AGGGRRIsDSHEDTG |
Homo sapiens |
|
| pmid |
sentence |
| 17075052 |
The triple aspartic acid mutation shows greater distance between the two thick myosin filaments (affects the steric arrangement of the filament distances) in heart tissue. Mutation is cardioprotective during stress (ischemia-reprofusion injury) against apoptosis similar to isoproterenol treatment. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150355 |
Ser304 |
SLLKKRDsFRTPRDS |
Homo sapiens |
|
| pmid |
sentence |
| 17075052 |
The triple aspartic acid mutation shows greater distance between the two thick myosin filaments (affects the steric arrangement of the filament distances) in heart tissue. Mutation is cardioprotective during stress (ischemia-reprofusion injury) against apoptosis similar to isoproterenol treatment. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Heart |
| + |
PRKACB | up-regulates
phosphorylation
|
MYBPC3 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163768 |
Ser275 |
LSAFRRTsLAGGGRR |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163772 |
Ser284 |
AGGGRRIsDSHEDTG |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163776 |
Ser304 |
SLLKKRDsFRTPRDS |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163780 |
Ser311 |
SFRTPRDsKLEAPAE |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation./Phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKACG | up-regulates
phosphorylation
|
MYBPC3 |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163784 |
Ser275 |
LSAFRRTsLAGGGRR |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163788 |
Ser284 |
AGGGRRIsDSHEDTG |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163792 |
Ser304 |
SLLKKRDsFRTPRDS |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163796 |
Ser311 |
SFRTPRDsKLEAPAE |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKACA | up-regulates
phosphorylation
|
MYBPC3 |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163752 |
Ser275 |
LSAFRRTsLAGGGRR |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163756 |
Ser284 |
AGGGRRIsDSHEDTG |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163760 |
Ser304 |
SLLKKRDsFRTPRDS |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163764 |
Ser311 |
SFRTPRDsKLEAPAE |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PKA | up-regulates
phosphorylation
|
MYBPC3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270128 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PDE4DIP | up-regulates
binding
|
MYBPC3 |
0.315 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173766 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21569246 |
This study ascribes a novel function to mmgl isoform 4: it meets all criteria for classification as an akap, and we show that is involved in the phosphorylation of cmybpc as well as ctni, hence mmgl is an important regulator of cardiac contractility. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MYBPC3
- 
- 