+ |
MAPK7 | up-regulates
phosphorylation
|
MEF2A |
0.699 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236587 |
Ser355 |
SALQGFNsPGMLSLG |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10849446 |
We have previously shown that bmk1 regulates c-jun gene expression through direct phosphorylation and activation of transcription factor mef2c.Here, we demonstrate that, in addition to mef2c, bmk1 phosphorylates and activates mef2a and mef2d but not mef2b.The sites phosphorylated by activated bmk1 were mapped to ser-355, thr-312, and thr-319 of mef2a and ser-179 of mef2d both in vitro and in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236583 |
Thr312 |
QATQPLAtPVVSVTT |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10849446 |
We have previously shown that bmk1 regulates c-jun gene expression through direct phosphorylation and activation of transcription factor mef2c.Here, we demonstrate that, in addition to mef2c, bmk1 phosphorylates and activates mef2a and mef2d but not mef2b.The sites phosphorylated by activated bmk1 were mapped to ser-355, thr-312, and thr-319 of mef2a and ser-179 of mef2d both in vitro and in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236579 |
Thr319 |
TPVVSVTtPSLPPQG |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10849446 |
We have previously shown that bmk1 regulates c-jun gene expression through direct phosphorylation and activation of transcription factor mef2c.Here, we demonstrate that, in addition to mef2c, bmk1 phosphorylates and activates mef2a and mef2d but not mef2b.The sites phosphorylated by activated bmk1 were mapped to ser-355, thr-312, and thr-319 of mef2a and ser-179 of mef2d both in vitro and in vivo. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
MAPK14 |
phosphorylation
|
MEF2A |
0.646 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-98224 |
Ser408 |
SIKSEPIsPPRDRMT |
Homo sapiens |
Neuron |
pmid |
sentence |
12586839 |
A p38 mapk-induced phosphopeptide with no mapk consensus the phosphorylation site is identified as ser-408 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-98228 |
Ser453 |
PRQEMGRsPVDSLSS |
Homo sapiens |
Neuron |
pmid |
sentence |
12586839 |
Thr-312 and thr-319 are known phosphorylation sites important for the increased transcriptional activation of mef2a by p38 mapk. Ser-453 and ser-479 are phosphorylated in vitro but were not important functionally |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
Pathways: | P38 Signaling, P38 Signaling and Myogenesis |
+ |
CDK5 | down-regulates activity
phosphorylation
|
MEF2A |
0.521 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-100574 |
Ser408 |
SIKSEPIsPPRDRMT |
Homo sapiens |
Cerebral Cortical Neuron |
pmid |
sentence |
12691662 |
Cdk5-mediated inhibition of the protective effects of transcription factor mef2 in neurotoxicity-induced apoptosis.We have identified the prosurvival transcription factor mef2 as a direct nuclear target of cdk5. Cdk5 phosphorylates mef2 at a distinct serine in its transactivation domain to inhibit mef2 activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK14 | up-regulates activity
phosphorylation
|
MEF2A |
0.646 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-62780 |
Thr312 |
QATQPLAtPVVSVTT |
Homo sapiens |
|
pmid |
sentence |
9858528 |
We show that mef2a, but not mef2b or mef2d, is a substrate for p38. Threonines 312 and 319 are the key regulatory phosphorylation sites by p38 in mef2a. Phosphorylation at these sites enhances transcriptional activity of mef2a |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | P38 Signaling, P38 Signaling and Myogenesis |
+ |
MAPK14 | up-regulates
phosphorylation
|
MEF2A |
0.646 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-62784 |
Thr319 |
TPVVSVTtPSLPPQG |
Homo sapiens |
|
pmid |
sentence |
9858528 |
We show that mef2a, but not mef2b or mef2d, is a substrate for p38. Threonines 312 and 319 are the key regulatory phosphorylation sites by p38 in mef2a. Phosphorylation at these sites enhances transcriptional activity of mef2a |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | P38 Signaling, P38 Signaling and Myogenesis |
+ |
PKCtheta/Nfix | up-regulates activity
phosphorylation
|
MEF2A |
0.344 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-238022 |
|
|
Mus musculus |
C2C12 Cell |
pmid |
sentence |
20178747 |
In the case of the MCK promoter, Nfix forms a complex with PKC theta that binds, phosphorylates, and activates MEF2A. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
MEF2A | up-regulates quantity by expression
transcriptional regulation
|
SLC2A4 |
0.371 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271692 |
|
|
|
|
pmid |
sentence |
14630949 |
Neither GEF nor MEF2A alone significantly activated GLUT4 promoter activity, but increased promoter activity 4- to 5-fold when expressed together. |
|
Publications: |
1 |
+ |
CAMK2D | up-regulates
|
MEF2A |
0.43 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255956 |
|
|
Homo sapiens |
|
pmid |
sentence |
19725819 |
In response toincreases in intracellular Ca2+ levels, activated CaMKII translocates into the nucleus where it phosphorylates and deactivates HDAC4 which, as a result, dissociates from theDNA-binding domain of MEF2. This dissociation allows MEF2 to bind to its DNA-binding domain to activate transcription of the MEF2-dependent target gene products MyoD and myogenin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NFATC2 | up-regulates
binding
|
MEF2A |
0.396 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-117586 |
|
|
Homo sapiens |
|
pmid |
sentence |
11796223 |
Upon dephosphorylation by calcineurin, nfatc2, also referred to as nfatp/nfat1, translocates to the nucleus where it directly associates with mef2a and -d. Nfatc2 stimulates mef2-dependent transcription by facilitating recruitment of the p300 coactivator to mef2-response elements. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | IGF and Myogenesis |
+ |
CABIN1 | down-regulates
|
MEF2A |
0.666 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151202 |
|
|
Homo sapiens |
|
pmid |
sentence |
17172641 |
Thus, cabin1 recruits chromatin-modifying enzymes, both histone deacetylases and a histone methyltransferase, to repress mef2 transcriptional activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HDAC4 | down-regulates
binding
|
MEF2A |
0.581 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-76231 |
|
|
Homo sapiens |
|
pmid |
sentence |
10737771 |
We discovered that mef2 interacts with histone deacetylases (hdacs) 4 and 5, resulting in repression of the transcriptional activity of mef2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle |
Pathways: | IGF and Myogenesis |
+ |
PHB2 | down-regulates
binding
|
MEF2A |
0.314 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235840 |
|
|
Mus musculus |
C2C12 Cell |
pmid |
sentence |
15173318 |
Phb2 interacts with both myod and mef2, and represses both myod- and mef2-dependent gene transcription. Furthermore, binding of phb2 to both myod and mef2 significantly decreases upon myogenic differentiation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Muscle |
+ |
HDAC5 | down-regulates
binding
|
MEF2A |
0.694 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-84023 |
|
|
Homo sapiens |
|
pmid |
sentence |
11062529 |
The histone deacetylase hdac-5, upon dephosphorylation and translocation to the nucleus, directly inactivates mef2, preventing myogenesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | IGF and Myogenesis |
+ |
CARM1 | up-regulates
methylation
|
MEF2A |
0.397 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255964 |
|
|
Mus musculus |
|
pmid |
sentence |
29163212 |
The first evidence alluding to a role of PRMTs in mediating skeletal muscle plasticity, specifically myogenesis, arose from the identification of CARM1 as a glucocorticoid receptor-interacting protein 1 (GRIP1) binding protein. (Chen et al., 2000). Here, GRIP1 and MEF2 were co-expressed in the nucleus during skeletal muscle differentiation. These initial findings led to an investigation that revealed that this methyltransferase was responsible for coactivating the transcription of myocyte enhancer factor-2C (MEF2C) via GRIP1 |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Skeletal Muscle |
+ |
CDK4 | down-regulates
binding
|
MEF2A |
0.288 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176515 |
|
|
Homo sapiens |
|
pmid |
sentence |
21902831 |
In contrast to cdk2, cyclin d/cdk4 blocks myod activity through an as yet unclear mechanism that may involve direct binding. Cyclin d/cdk4 can also block the activity of myogenin and all mef2 isoforms. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MEF2A | up-regulates quantity by expression
transcriptional regulation
|
MYH2 |
0.331 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-238703 |
|
|
Mus musculus |
|
pmid |
sentence |
15728583 |
Myocyte enhancer factor-2 and serum response factor binding elements regulate fast Myosin heavy chain transcription in vivo. We show that the upstream promoter region of the gene most abundantly expressed in mouse skeletal muscles, IIb MyHC, retains binding activity and transcriptional activation for three positive transcription factors, the serum response factor, Oct-1, and myocyte enhancer factor-2, whereas the other two genes (IIa and IId/x) have nucleotide substitutions in these sites that reduce binding and transcriptional activation |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Skeletal Muscle |
Pathways: | IGF and Myogenesis |
+ |
CyclinD/CDK4 | down-regulates
binding
|
MEF2A |
0.271 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-216960 |
|
|
Homo sapiens |
|
pmid |
sentence |
21902831 |
In contrast to cdk2, cyclin d/cdk4 blocks myod activity through an as yet unclear mechanism that may involve direct binding. Cyclin d/cdk4 can also block the activity of myogenin and all mef2 isoforms. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | IGF and Myogenesis |
+ |
SMAD2 | up-regulates
binding
|
MEF2A |
0.398 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235846 |
|
|
Mus musculus |
C2C12 Cell |
pmid |
sentence |
11160896 |
Our studies indicate that smad2 and 4 (smad2/4) complexes cooperate with mef2 regulatory proteins in a gal4-based one-hybrid reporter gene assay. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Myotube |
+ |
EP300 | up-regulates
binding
|
MEF2A |
0.855 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-232165 |
|
|
Homo sapiens |
|
pmid |
sentence |
11796223 |
Once released from associated repressors, MEF2 is bound by the p300 coactivator, which possesses histone acetyltransferase activity. Thus, the net result of CaMK signaling to MEF2 complexes is increased histone acetylation (Ac), which relaxes chromatin and stimulates MEF2 target gene transcription. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | IGF and Myogenesis |
+ |
MEF2A | up-regulates quantity by expression
transcriptional regulation
|
MYF6 |
0.573 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-238709 |
|
|
Mus musculus |
|
pmid |
sentence |
7739551 |
Myogenin and MEF2 function synergistically to activate the MRF4 promoter during myogenesis. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | IGF and Myogenesis |
+ |
MEF2A | up-regulates quantity by expression
transcriptional regulation
|
MYH1 |
0.362 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-238748 |
|
|
Mus musculus |
|
pmid |
sentence |
15728583 |
Myocyte enhancer factor-2 and serum response factor binding elements regulate fast Myosin heavy chain transcription in vivo. We show that the upstream promoter region of the gene most abundantly expressed in mouse skeletal muscles, IIb MyHC, retains binding activity and transcriptional activation for three positive transcription factors, the serum response factor, Oct-1, and myocyte enhancer factor-2, whereas the other two genes (IIa and IId/x) have nucleotide substitutions in these sites that reduce binding and transcriptional activation |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | IGF and Myogenesis |
+ |
MEF2A | up-regulates
|
Myoblast_fusion |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255957 |
|
|
Homo sapiens |
|
pmid |
sentence |
19725819 |
In response to increases in intracellular Ca2+ levels, activated CaMKII translocates into the nucleus where it phosphorylates and deactivates HDAC4 which, as a result, dissociates from theDNA-binding domain of MEF2. This dissociation allows MEF2 to bind to its DNA-binding domain to activate transcription of the MEF2-dependent target gene products MyoD and myogenin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MEF2A | up-regulates activity
binding
|
MYOD1 |
0.733 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-54086 |
|
|
Homo sapiens |
|
pmid |
sentence |
9418854 |
Myod-e protein heterodimers interact with mef2 proteins to synergistically activate myogenesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle, Skeletal Muscle |
Pathways: | IGF and Myogenesis, P38 Signaling and Myogenesis |
+ |
MEF2A | up-regulates quantity by expression
transcriptional regulation
|
MYH10 |
0.323 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-238763 |
|
|
Mus musculus |
|
pmid |
sentence |
15728583 |
Myocyte enhancer factor-2 and serum response factor binding elements regulate fast Myosin heavy chain transcription in vivo. We show that the upstream promoter region of the gene most abundantly expressed in mouse skeletal muscles, IIb MyHC, retains binding activity and transcriptional activation for three positive transcription factors, the serum response factor, Oct-1, and myocyte enhancer factor-2, whereas the other two genes (IIa and IId/x) have nucleotide substitutions in these sites that reduce binding and transcriptional activation |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Skeletal Muscle |