| + |
PRKACA |
phosphorylation
|
MBP |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250010 |
Ser141 |
MASQKRPsQRHGSKY |
in vitro |
|
| pmid |
sentence |
| 2413024 |
Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250011 |
Ser146 |
RPSQRHGsKYLATAS |
in vitro |
|
| pmid |
sentence |
| 2413024 |
Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250012 |
Ser190 |
RGAPKRGsGKDSHHP |
in vitro |
|
| pmid |
sentence |
| 2413024 |
Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-162 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250013 |
Ser266 |
FGYGGRAsDYKSAHK |
in vitro |
|
| pmid |
sentence |
| 2413024 |
Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-163 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250014 |
Ser295 |
FKLGGRDsRSGSPMA |
in vitro |
|
| pmid |
sentence |
| 2413024 |
Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-164 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250015 |
Thr169 |
FLPRHRDtGILDSIG |
in vitro |
|
| pmid |
sentence |
| 2413024 |
Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-165 |
|
| Publications: |
6 |
Organism: |
In Vitro |
| + |
PRKCA |
phosphorylation
|
MBP |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248869 |
Ser141 |
MASQKRPsQRHGSKY |
in vitro |
|
| pmid |
sentence |
| 2413024 |
MBP was phosphorylated by either protein kinase A or C | Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 at various reaction velocities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248870 |
Ser146 |
RPSQRHGsKYLATAS |
in vitro |
|
| pmid |
sentence |
| 2413024 |
MBP was phosphorylated by either protein kinase A or C | Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 at various reaction velocities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248871 |
Ser190 |
RGAPKRGsGKDSHHP |
in vitro |
|
| pmid |
sentence |
| 2413024 |
MBP was phosphorylated by either protein kinase A or C | Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 at various reaction velocities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248872 |
Ser249 |
GLSLSRFsWGAEGQR |
in vitro |
|
| pmid |
sentence |
| 2413024 |
MBP was phosphorylated by either protein kinase A or C | Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 at various reaction velocities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248873 |
Ser266 |
FGYGGRAsDYKSAHK |
in vitro |
|
| pmid |
sentence |
| 2413024 |
MBP was phosphorylated by either protein kinase A or C | Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 at various reaction velocities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248874 |
Ser285 |
VDAQGTLsKIFKLGG |
in vitro |
|
| pmid |
sentence |
| 2413024 |
MBP was phosphorylated by either protein kinase A or C | Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 at various reaction velocities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248875 |
Ser295 |
FKLGGRDsRSGSPMA |
in vitro |
|
| pmid |
sentence |
| 2413024 |
MBP was phosphorylated by either protein kinase A or C | Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 at various reaction velocities. |
|
| Publications: |
7 |
Organism: |
In Vitro |
| + |
UHMK1 | down-regulates 
phosphorylation
|
MBP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78895 |
Ser299 |
GRDSRSGsPMARR |
Homo sapiens |
|
| pmid |
sentence |
| 10880969 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. Mass spectrometry and peptide sequencing allowed us to identify serine 164 of mbp as the unique site phosphorylated by kis. Phosphorylation of synthetic peptides indicated the importance of the proline residue at position +1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143485 |
Ser299 |
GRDSRSGsPMARR |
Homo sapiens |
|
| pmid |
sentence |
| 16401070 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. Mass spectrometry and peptide sequencing allowed us to identify serine 164 of mbp as the unique site phosphorylated by kis. Phosphorylation of synthetic peptides indicated the importance of the proline residue at position +1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
MAPK1 |
phosphorylation
|
MBP |
0.575 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249419 |
Thr229 |
HFFKNIVtPRTPPPS |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 12760422 |
Thr94 in bovine myelin basic protein is a second phosphorylation site for 42-kDa mitogen-activated protein kinase (ERK2). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates
phosphorylation
|
MBP |
0.575 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22420 |
Thr232 |
KNIVTPRtPPPSQGK |
Homo sapiens |
|
| pmid |
sentence |
| 1939237 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143477 |
Thr232 |
KNIVTPRtPPPSQGK |
Homo sapiens |
|
| pmid |
sentence |
| 16401070 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
MAPK3 | down-regulates
phosphorylation
|
MBP |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143481 |
Thr232 |
KNIVTPRtPPPSQGK |
Homo sapiens |
|
| pmid |
sentence |
| 16401070 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22424 |
Thr232 |
KNIVTPRtPPPSQGK |
Homo sapiens |
|
| pmid |
sentence |
| 1939237 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
MBP | up-regulates 
|
Myelination |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269230 |
|
|
|
|
| pmid |
sentence |
| 31066630 |
Myelin basic protein (MBP) is essential for the compaction of the two adjacent cytoplasmic membrane surfaces into the major dense line of myelin. |
|
| Publications: |
1 |
| + |
ERK1/2 | down-regulates
phosphorylation
|
MBP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270195 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16401070 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CNP | down-regulates activity
|
MBP |
0.475 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269269 |
|
|
|
|
| pmid |
sentence |
| 28076777 |
We provide evidence that CNP directly associates with and organizes the actin cytoskeleton, thereby providing an intracellular strut that counteracts membrane compaction by myelin basic protein (MBP). |
|
| Publications: |
1 |
| + |
SMO | up-regulates quantity
transcriptional regulation
|
MBP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269226 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 35082605 |
We show that GSA-10 promotes Gli2 upregulation, MBP and MAL/OPALIN expression via Smo/AMPactivated Protein Kinase (AMPK) signaling, and efficiently increases the number of axonal contact/ensheathment for each oligodendroglial cell. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RXRG | up-regulates quantity
transcriptional regulation
|
MBP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269266 |
|
|
|
|
| pmid |
sentence |
| 31390799 |
RXRγ gene silencing reduces the ability of the drugs to promote MBP expression. |
|
| Publications: |
1 |
| + |
Gbeta | down-regulates
phosphorylation
|
MBP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270100 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16401070 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
3.0
MBP
- 
- 