| + |
CDK2 | down-regulates 
phosphorylation
|
MYOD1 |
0.537 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176509 |
Ser200 |
YSGDSDAsSPRSNCS |
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
Cyclin e/cdk2 can phosphorylate myod at serine 200, which causes ubiquitination and degradation of this transcription factor during g1, preventing its accumulation and a commitment to differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
MYOD1 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121601 |
Ser200 |
YSGDSDAsSPRSNCS |
Homo sapiens |
|
| pmid |
sentence |
| 14749395 |
Myod is phosphorylated on ser5 and ser200 by cyclin b-cdc2, resulting in a decrease of its stability and down-regulation of both myod and p21. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176505 |
Ser200 |
YSGDSDAsSPRSNCS |
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
Phosphorylation of myod at s200 is common to other cdks, such as the mitotic cyclin b/cdk1, which may prevent inappropriate myod accumulation during mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121605 |
Ser5 |
sPPLRDVD |
Homo sapiens |
|
| pmid |
sentence |
| 14749395 |
Myod is phosphorylated on ser5 and ser200 by cyclin b-cdc2, resulting in a decrease of its stability and down-regulation of both myod and p21. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 | down-regulates
phosphorylation
|
MYOD1 |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216920 |
Ser200 |
YSGDSDAsSPRSNCS |
Homo sapiens |
Myoblast |
| pmid |
sentence |
| 14749395 |
Myod is phosphorylated on ser5 and ser200 by cyclin b-cdc2, resulting in a decrease of its stability and down-regulation of both myod and p21. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216860 |
Ser200 |
YSGDSDAsSPRSNCS |
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
Phosphorylation of myod at s200 is common to other cdks, such as the mitotic cyclin b/cdk1, which may prevent inappropriate myod accumulation during mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216924 |
Ser5 |
sPPLRDVD |
Homo sapiens |
Myoblast |
| pmid |
sentence |
| 14749395 |
Myod is phosphorylated on ser5 and ser200 by cyclin b-cdc2, resulting in a decrease of its stability and down-regulation of both myod and p21. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MAPK12 | up-regulates activity 
phosphorylation
|
MYOD1 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276274 |
Ser200 |
YSGDSDAsSPRSNCS |
Mus musculus |
C3H10T1/2 Clone 8 Cell |
| pmid |
sentence |
| 20026657 |
We determined that p38-gamma directly phosphorylated MyoD on Ser199 and Ser200, which results in enhanced occupancy of MyoD on the promoter of myogenin together with markedly decreased transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276273 |
Ser201 |
SGDSDASsPRSNCSD |
Mus musculus |
C3H10T1/2 Clone 8 Cell |
| pmid |
sentence |
| 20026657 |
We determined that p38-gamma directly phosphorylated MyoD on Ser199 and Ser200, which results in enhanced occupancy of MyoD on the promoter of myogenin together with markedly decreased transcriptional activity. Phosphorylation of MyoD by p38-γ directs the assembly of a repressive transcriptional complex at the Myogenin promoter. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
CyclinE/CDK2 | down-regulates
phosphorylation
|
MYOD1 |
0.536 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216706 |
Ser200 |
YSGDSDAsSPRSNCS |
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
Cyclin e/cdk2 can phosphorylate myod at serine 200, which causes ubiquitination and degradation of this transcription factor during g1, preventing its accumulation and a commitment to differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis |
| + |
PRKCA | down-regulates activity
phosphorylation
|
MYOD1 |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248845 |
Thr115 |
ADRRKAAtMRERRRL |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 1335366 |
FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ABL1 | down-regulates activity
phosphorylation
|
MYOD1 |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253055 |
Tyr30 |
FATTDDFyDDPCFDSP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12415271 |
We have found that c-Abl can phosphorylate MyoD at a conserved N-terminal tyrosine (Tyr30) that is located within the transactivation domain. Mutation of Tyr30 to Phe does not interfere with the function of MyoD, but theTyr30Phe mutant becomes resistant to the inhibitory effect of DNA damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling and Myogenesis |
| + |
NFIA | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263982 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 32991581 |
NFIA binds to and activates the brown-fat-specific enhancers even before differentiation and later facilitates the binding of PPARgamma|NFIA has at least three functions on the transcriptional regulation of brown fat [2]. First, NFIA activates adipogenesis per se, through activating the transcription of Pparg, which encodes PPARgamma. Second, NFIA also activates the brown-fat-specific gene expression (such as Ucp1 and Ppargc1a) independent of the degree of adipocyte differentiation, through facilitating the binding of PPARgamma to the brown-fat-specific enhancers. Third, NFIA represses myogenesis through suppression of myogenic transcription factors such as Myod1 as well as Myog, |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PAX7 | down-regulates quantity by destabilization 
|
MYOD1 |
0.615 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255637 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17548510 |
Previously, we showed that Pax7 overexpression in adult primary myoblasts down-regulates MyoD and prevents myogenin induction, inhibiting myogenesis. We show that Pax7 prevents muscle differentiation independently of its transcriptional activity, affecting MyoD function. [...] Pax7 expression affects MyoD protein stability |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | NOTCH Signaling and Myogenesis, P38 Signaling and Myogenesis, Rhabdomyosarcoma |
| + |
MYOD1 | up-regulates
binding
|
SMARCA4 |
0.543 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151685 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17194702 |
Myod targets brg1 to the myogenin promoter during the initiation of myogenesis in tissue culture models for skeletal muscle differentiation /initiation of myogenin transcription is dependent upon myod, the pbx homeodomain factor, and swi/snf chromatin-remodeling enzymes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMARCD3 | up-regulates activity
binding
|
MYOD1 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238289 |
|
|
in vitro |
|
| pmid |
sentence |
| 22068056 |
We show that the muscle determination factor MyoD and the SWI/SNF subunit BAF60c interact on the regulatory elements of MyoD-target genes in myoblasts, prior to activation of transcription. BAF60c facilitates MyoD binding to target genes and marks the chromatin for signal-dependent recruitment of the SWI/SNF core to muscle genes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | P38 Signaling and Myogenesis |
| + |
MEF2A | up-regulates activity
binding
|
MYOD1 |
0.732 |
| 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 |
| + |
PAX7 | up-regulates quantity by expression 
transcriptional regulation
|
MYOD1 |
0.615 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181624 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18854138 |
Our cell-based assays and in vitro studies reveal a tight codependent partnership between foxo3 and pax3/7 to coordinately recruit rna polymerase ii and form a preinitiation complex (pic) to activate myod transcription in myoblasts. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | NOTCH Signaling and Myogenesis, P38 Signaling and Myogenesis, Rhabdomyosarcoma |
| + |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
MYOD1 |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271804 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 19319192 |
We previously showed that the level of MAFbx protein increased in skeletal muscle during aging and/or food deprivation. Immunoprecipitation of the SCFMAFbx complexes from mouse atrophic muscles exhibited ubiquitination activity by using MyoD as substrate. Food deprivation and oxidative stress–induced atrophy increase polyubiquitination by the SCFMAFbx pathway and degradation of MyoD by the proteasome |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CBP/p300 | up-regulates
binding, acetylation
|
MYOD1 |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81047 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10944526 |
Our results provide direct evidence that myod acetylation functionally activates the protein and show that both pcaf and cbp/p300 are candidate enzymes for myod acetylation in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217220 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10944526 |
Our results provide direct evidence that myod acetylation functionally activates the protein and show that both pcaf and cbp/p300 are candidate enzymes for myod acetylation in vivo. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
NfKb-p65/p50 | down-regulates
|
MYOD1 |
0.283 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255352 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20219869 |
Furthermore, NF-kB activation can cause destabilization of MyoD mRNA and degradation of MyoD protein (35, 49), which would further impede muscle differentiation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
TCF3 | up-regulates activity
binding
|
MYOD1 |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-20540 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1649701 |
In addition we demonstrate that myod, in conjunction with e12/e47-like proteins, is functioning as a regulatory nodal point for activation of several other downstream muscle regulators. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| Pathways: | P38 Signaling and Myogenesis |
| + |
FBXO32 | down-regulates quantity by destabilization
ubiquitination, binding
|
MYOD1 |
0.576 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184861 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19319192 |
Here we present evidence that mafbx targets myod for degradation in several models of skeletal muscle atrophy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271802 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 19319192 |
We previously showed that the level of MAFbx protein increased in skeletal muscle during aging and/or food deprivation. Immunoprecipitation of the SCFMAFbx complexes from mouse atrophic muscles exhibited ubiquitination activity by using MyoD as substrate. Food deprivation and oxidative stress–induced atrophy increase polyubiquitination by the SCFMAFbx pathway and degradation of MyoD by the proteasome |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Tissue: |
Skeletal Muscle |
| Pathways: | IGF and Myogenesis |
| + |
MEF2C | up-regulates activity
binding
|
MYOD1 |
0.732 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-54089 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9418854 |
Myod-e protein heterodimers interact with mef2 proteins to synergistically activate myogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis, NOTCH Signaling and Myogenesis, P38 Signaling and Myogenesis |
| + |
NR2F2 | down-regulates
binding
|
MYOD1 |
0.391 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-62248 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9826778 |
The orphan nuclear receptor, coup-tf ii, inactivates myogenesis by post-transcriptional regulation of myod function: coup-tf ii directly interacts with p300 and myod. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXO3 | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181618 |
|
|
Homo sapiens |
Myoblast |
| pmid |
sentence |
| 18854138 |
Our cell-based assays and in vitro studies reveal a tight codependent partnership between foxo3 and pax3/7 to coordinately recruit rna polymerase ii and form a preinitiation complex (pic) to activate myod transcription in myoblasts. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
CDKN1A |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238529 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 10373569 |
Here we report that, at the onset of differentiation, activation by MyoD of the Rb, p21, and cyclin D3 genes occurs in the absence of new protein synthesis and with the requirement of the p300 transcriptional coactivator. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Rhabdomyosarcoma |
| + |
MYOD1 | up-regulates
binding
|
SWI/SNF complex |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217737 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17194702 |
Myod targets brg1 to the myogenin promoter during the initiation of myogenesis in tissue culture models for skeletal muscle differentiation /initiation of myogenin transcription is dependent upon myod, the pbx homeodomain factor, and swi/snf chromatin-remodeling enzymes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
MYH7 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251958 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 17111365 |
Transient transfection assays demonstrated that the calcineurin/NFATc1 signaling pathway is essential for MyHCbeta promoter activation during transformation of C2C12 myotubes but is not sufficient for complete fast MyHCIId/x promoter inhibition. Along with NFATc1, myocyte enhancer factor-2D (MEF-2D) and the myogenic transcription factor MyoD transactivated the MyHCbeta promoter in calcium-ionophore-treated myotubes in a calcineurin-dependent manner. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DIO2 | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256203 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20978344 |
The active thyroid hormone 3,5,3' triiodothyronine (T3) is a major regulator of skeletal muscle function. The deiodinase family of enzymes controls the tissue-specific activation and inactivation of the prohormone thyroxine (T4). Here we show that type 2 deiodinase (D2) is essential for normal mouse myogenesis and muscle regeneration. Indeed, D2-mediated increases in T3 were essential for the enhanced transcription of myogenic differentiation 1 (MyoD) and for execution of the myogenic program. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | down-regulates
binding
|
MYOD1 |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176527 |
|
|
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 |
| + |
ID1 | down-regulates activity
binding
|
MYOD1 |
0.49 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240265 |
|
|
Mus musculus |
Myoblast |
| pmid |
sentence |
| 8380166 |
Id1 and Id2 interacted strongly with MyoD and Myf-5.Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MYOD1 | form complex 
binding
|
MYOD/E2-2 |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241100 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16847330 |
The MyoD family of basic helix-loop-helix transcription factors function as heterodimers with members of the E-protein family to induce myogenic gene activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MYOD1 | form complex
binding
|
MYOD/HEB |
0.66 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241122 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16847330 |
The MyoD family of basic helix-loop-helix transcription factors function as heterodimers with members of the E-protein family to induce myogenic gene activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WNT7A | up-regulates activity
|
MYOD1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198922 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22944199 |
In explant cultures of mouse paraxial mesoderm, wnt1 induced expression of the mrf myf5, whereas wnt7a or wnt6 preferentially activated the mrf myod. Here we report that cells expressing wnt1 will preferentially activate myf5 while cells expressing wnt7a will preferentially activate myod |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60471 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 9753670 |
Differential activation of Myf5 and MyoD by different Wnts in explants of mouse paraxial mesoderm and the later activation of myogenesis in the absence of Myf5 |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| Tissue: |
Muscle, Skeletal Muscle |
| Pathways: | WNT Signaling and Myogenesis |
| + |
MYOD1 | up-regulates
transcriptional regulation
|
CDKN1A |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251574 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25211658 |
P21 is regulated by MyoD and myogenin in normal muscle cells and the inactivation of these factors in RMS cells contributes to the silencing of p21 in RMS cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Rhabdomyosarcoma |
| + |
Calcineurin | up-regulates
|
MYOD1 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255103 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15829723 |
Calcineurin can activate the transcription factors myocyte enhancer factor-2 and MyoD, which leads to the subsequent induction of myogenin and muscle differentiation (22). In addition, inhibition of calcineurin prevents the initiation of early stages of muscle differentiation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
RB1 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238532 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10373569 |
Here we report that, at the onset of differentiation, activation by MyoD of the Rb, p21, and cyclin D3 genes occurs in the absence of new protein synthesis and with the requirement of the p300 transcriptional coactivator. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | IGF and Myogenesis, Rhabdomyosarcoma |
| + |
FGF8 | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203148 |
|
|
Homo sapiens |
Satellite Cell |
| pmid |
sentence |
| 24209627 |
Loss of fgf signaling in fgf24 and fgf8 double-deficient zebrafish |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
MYOD1 | up-regulates
|
Differentiation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255417 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16275751 |
Together, these results support the notion that Myf5 functions toward myoblast proliferation, whereas MyoD prepares myoblasts for efficient differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| Pathways: | NOTCH Signaling |
| + |
RBPJ/NOTCH | down-regulates quantity by repression
transcriptional regulation
|
MYOD1 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219359 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10066785 |
Delta-induced Notch signaling mediated by RBP-J inhibits MyoD expression and myogenesis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
C2C12 Cell |
| Pathways: | NOTCH Signaling, NOTCH Signaling and Myogenesis |
| + |
CHD2 | up-regulates activity
binding
|
MYOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264525 |
|
|
|
|
| pmid |
sentence |
| 29962935 |
CHD2 also showed an interaction with MyoD, a master regulator of skeletal muscle differentiation, and together MyoD and CHD2 bind to myogenic gene promoters. |
|
| Publications: |
1 |
| + |
MSX1 | down-regulates quantity by repression
transcriptional regulation
|
MYOD1 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125765 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15192231 |
We found that msx1 and h1b bind to a key regulatory element of myod, a central regulator of skeletal muscle differentiation, where they induce repressed chromatin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
WNT7B | up-regulates
|
MYOD1 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198925 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22944199 |
In explant cultures of mouse paraxial mesoderm, wnt1 induced expression of the mrf myf5, whereas wnt7a or wnt6 preferentially activated the mrf myod. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
CCND3 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238526 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10373569 |
Here we report that, at the onset of differentiation, activation by MyoD of the Rb, p21, and cyclin D3 genes occurs in the absence of new protein synthesis and with the requirement of the p300 transcriptional coactivator. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
WNT4 | up-regulates
|
MYOD1 |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60373 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9753670 |
Wnt4, wnt5a and wnt6 exert an intermediate effect activating both myf5 and myod equivalently in paraxial mesoderm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
MAPK14 | up-regulates activity
|
MYOD1 |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129702 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15466486 |
Here, we show that p38 activity facilitates myod and mef2 binding at a subset of late-activated promoters, and the binding of mef2d recruits pol ii. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| Pathways: | NOTCH Signaling and Myogenesis, P38 Signaling and Myogenesis |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
MYOG |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135984 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15870273 |
We observed that the homeodomain factor pbx1, which cooperates with myod to stimulate myogenin expression, is constitutively bound to the myogenin promoter in a swi/snf-independent manner, suggesting a two-step mechanism in which myod initially interacts indirectly with the myogenin promoter and attracts chromatin-remodeling enzymes, which then facilitate direct binding by myod and other regulatory proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235009 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18676376 |
provide a novel transcriptional paradigm for the first steps of myogenesis, where a calcineurin/NFATc3 pathway regulates myogenin induction in cooperation with MyoD during myogenesis. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| Pathways: | IGF and Myogenesis, NOTCH Signaling and Myogenesis, P38 Signaling and Myogenesis, Rhabdomyosarcoma |
| + |
KAT2B | up-regulates
binding, acetylation
|
MYOD1 |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81059 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10944526 |
Our results provide direct evidence that myod acetylation functionally activates the protein and show that both pcaf and cbp/p300 are candidate enzymes for myod acetylation in vivo |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81056 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10944526 |
Our results provide direct evidence that myod acetylation functionally activates the protein and show that both pcaf and cbp/p300 are candidate enzymes for myod acetylation in vivo |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
HDAC1 | down-regulates
binding
|
MYOD1 |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111243 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11684023 |
Interaction of myod with hdac1 in undifferentiated myoblasts mediates repression of muscle-specific gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
MYOD1 | up-regulates
binding
|
SMARCD3 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-136130 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15870273 |
This suggests a novel mechanism by which myod interacts with the promoter indirectly via pbx-1 and recruits chromatin-remodeling enzymes, which then facilitate the binding of myod and other regulators. Demonstration of physical interactions between brg1 and myod and brg1 and pbx support this conclusion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling and Myogenesis |
| + |
SIRT2 | down-regulates
deacetylation
|
MYOD1 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104251 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12887892 |
Sir2-mediated deacetylation of myod can be expected to inhibit its transcriptional capabilities. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
EP300 | up-regulates
acetylation
|
MYOD1 |
0.668 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81053 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10944526 |
Our results provide direct evidence that myod acetylation functionally activates the protein and show that both pcaf and cbp/p300 are candidate enzymes for myod acetylation in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| Pathways: | IGF and Myogenesis |
| + |
TBX2 | down-regulates activity
binding
|
MYOD1 |
0.315 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251560 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24470334 |
We have found that TBX2 is highly up regulated in both ERMS and ARMS subtypes of RMS and demonstrate that TBX2 is a repressor of myogenesis by binding to MyoD and myogenin and inhibiting their activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Rhabdomyosarcoma |
| + |
PAX3 | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181621 |
|
|
Homo sapiens |
Myoblast |
| pmid |
sentence |
| 18854138 |
Our cell-based assays and in vitro studies reveal a tight codependent partnership between foxo3 and pax3/7 to coordinately recruit rna polymerase ii and form a preinitiation complex (pic) to activate myod transcription in myoblasts. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Rhabdomyosarcoma, WNT Signaling and Myogenesis |
| + |
RBL2 | down-regulates quantity
transcriptional regulation
|
MYOD1 |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241943 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10801445 |
Furthermore, muscle cells overexpressing p130 had reduced levels of the muscle-promoting factor MyoD. In addition, p130 repressed the transactivation capacity of MyoD, an effect abolished by co-transfection of pRb |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
KAT5 | up-regulates activity
binding
|
MYOD1 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-237675 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21936881 |
Tip60 regulates myoblast differentiation by enhancing the transcriptional activity of MyoD via their physical interactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PITX2 | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169107 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20978076 |
We show that pitx2 is crucial for the onset of myod gene expression in limb muscle progenitors and that it acts on the myod core enhancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| Pathways: | WNT Signaling and Myogenesis |
| + |
WWTR1 | up-regulates
binding
|
MYOD1 |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165414 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20466877 |
Taz physically interacts with myod through the ww domain and activates myod-dependent gene transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
MYOG |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255639 |
|
|
|
|
| pmid |
sentence |
| 15870273 |
We suggest that the interaction between MyoD and Pbx is necessary to initially target MyoD to the myogenin promoter |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255640 |
|
|
|
|
| pmid |
sentence |
| 12694204 |
We conclude that MyoD is the major MRF that binds to the E-box from the myogenin promoter during differentiation. |
|
| Publications: |
2 |
| Tissue: |
Skeletal Muscle |
| Pathways: | IGF and Myogenesis, NOTCH Signaling and Myogenesis, P38 Signaling and Myogenesis, Rhabdomyosarcoma |
| + |
MYOD1 | up-regulates
|
Skeletal_muscle_differentiation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37458 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8288123 |
The myogenic regulators myod, myogenin, myf5, and mrf4 share -80% amino acid identity within a basic helix-loop-helix (bHLH) motif that mediates dimerization and dna binding. [...] myogenic bHLH proteins form heterodimers with ubiquitous bHLH proteins, known as e proteins, and activate the transcription of muscle-specific genes by binding to the e-box consensus sequence (canntg) in muscle gene promoters and enhancers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis, NOTCH Signaling and Myogenesis, P38 Signaling and Myogenesis, Rhabdomyosarcoma, WNT Signaling and Myogenesis |
| + |
TEK | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241532 |
|
|
Mus musculus |
Myoblast |
| pmid |
sentence |
| 26042050 |
the effects of the angiopoietins are not specific for vascular endothelial cells, as their receptors (Tie1, Tie2) are known to be expressed in hematopoietic cells and they have also recently been shown to be expressed in skeletal muscle cellsExogenous Ang-1 enhanced myogenic (MyoD and Myogenin) mRNA in differentiating myoblasts and increased myosin heavy chain protein. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
HES1 | down-regulates quantity by repression
transcriptional regulation
|
MYOD1 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235596 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 10066785 |
Notch signaling up-regulated hes1 mrna expression within 1 h and subsequently reduced expression of myod mrna. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Muscle |
| Pathways: | NOTCH Signaling, NOTCH Signaling and Myogenesis |
| + |
SMAD3/SMAD4 | down-regulates activity
transcriptional regulation
|
MYOD1 |
0.624 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254987 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12244043 |
Taken together, these results suggest that myostatin inhibits MyoD activity and expression via Smad 3 resulting in the failure of the myoblasts to differentiate into myotubes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MDFI | down-regulates activity
binding
|
MYOD1 |
0.51 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240436 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 8797820 |
We demonstrate that I-mf inhibits the transactivation activity of the MyoD family and represses myogenesis. I-mf associates with MyoD family members and retains them in the cytoplasm by masking their nuclear localization signals. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DIO | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270306 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20978344 |
The active thyroid hormone 3,5,3' triiodothyronine (T3) is a major regulator of skeletal muscle function. The deiodinase family of enzymes controls the tissue-specific activation and inactivation of the prohormone thyroxine (T4). Here we show that type 2 deiodinase (D2) is essential for normal mouse myogenesis and muscle regeneration. Indeed, D2-mediated increases in T3 were essential for the enhanced transcription of myogenic differentiation 1 (MyoD) and for execution of the myogenic program. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STAT3 | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255416 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25194572 |
Here we show that IL-6-activated Stat3 signaling regulates satellite cell behavior, promoting myogenic lineage progression through myogenic differentiation 1 (Myod1) regulation. IL-6 stimulation promoted an increase in the mRNA levels of both Stat3 and Myod1. Stat3 mediated this effect, as IL-6–dependent Myod1 upregulation was impaired after infection with the shStat3 lentivirus. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Rhabdomyosarcoma |
| + |
MYOD1 | down-regulates quantity by repression
transcriptional regulation
|
DES |
0.242 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241762 |
|
|
Mus musculus |
Myoblast |
| pmid |
sentence |
| 25653159 |
MyoD and HDAC2 repress myogenic late genes at early times of differentiation.A time course of Ckm, Des and Acta1 gene expression demonstrated that these genes were prematurely expressed when differentiation was driven by myogenin and Mef2D1b (Figure _(Figure6A).6A). Since MyoD is not expressed under these conditions, it cannot bind to these genes; ChIP assays demonstrated that HDAC2 also was not present on the Ckm, Des and Acta1 regulatory sequences under these conditions (Figure _(Figure6B).6B). Therefore the presence of MyoD and HDAC2 prior to gene expression functions to repress late gene expression at early times of differentiation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ZFP36 | down-regulates quantity by destabilization
post transcriptional regulation
|
MYOD1 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253597 |
|
|
|
|
| pmid |
sentence |
| 25815583 |
The TTP binding site in the 3′ UTR of MyoD would permit TTP-mediated mRNA decay |
|
| Publications: |
1 |
| + |
PHB2 | down-regulates
binding
|
MYOD1 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235843 |
|
|
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 |
| + |
HES1 | down-regulates activity
transcriptional regulation
|
MYOD1 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243181 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 10066785 |
Notch signaling up-regulated HES1 mRNA expression within 1 h and subsequently reduced expression of MyoD mRNA |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | NOTCH Signaling, NOTCH Signaling and Myogenesis |
| + |
MYOD1 | up-regulates
|
CDKN1A |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235831 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 7791789 |
The upregulation of p21 occurred at the levels of mrna and protein, |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Rhabdomyosarcoma |
| + |
SUV39H1 | down-regulates quantity by repression
transcriptional regulation
|
MYOD1 |
0.524 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249600 |
|
|
Homo sapiens |
Rhabdomyosarcoma Cell Line |
| pmid |
sentence |
| 23435416 |
The methyl marks H3K9me3 on the myoD promoter and H3K27me3 on the myogenin promoter have been shown to be under the control of the histone methyl transferase KMT1A and the HDM KDM4A, respectively, during normal myogenesis. In addition, KMT1A has recently been shown to play a role in ARMS by inhibiting myogenic differentiation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
VEGFA |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257598 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 18094043 |
We further demonstrate that the myogenic transcription factor, MyoD, and its heterodimeric binding proteins E12 and E47, up-regulate the expression of endogenous VEGF through direct interaction with the VEGF promoter. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
| Pathways: | NOTCH Signaling |
| + |
CSRP3 | up-regulates activity
binding
|
MYOD1 |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241116 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 9234731 |
we found that nuclear MLP functions through a physical interaction with the muscle basic helix-loop-helix (bHLH) transcription factors MyoD, MRF4, and myogenin. we propose that it serves as a cofactor for the myogenic bHLH proteins by increasing their interaction with specific DNA regulatory elements. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
WNT6 | up-regulates
|
MYOD1 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60418 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9753670 |
In explant cultures of mouse paraxial mesoderm, wnt1 induced expression of the mrf myf5, whereas wnt7a or wnt6 preferentially activated the mrf myod. Wnt4, wnt5a and wnt6 exert an intermediate effect activating both myf5 and myod equivalently in paraxial mesoderm. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198916 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22944199 |
In explant cultures of mouse paraxial mesoderm, wnt1 induced expression of the mrf myf5, whereas wnt7a or wnt6 preferentially activated the mrf myod. Wnt4, wnt5a and wnt6 exert an intermediate effect activating both myf5 and myod equivalently in paraxial mesoderm. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
CTNNB1 | up-regulates activity
binding
|
MYOD1 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255653 |
|
|
|
|
| pmid |
sentence |
| 18316399 |
Together, these results suggest that B-Cat increases MyoD binding to E box elements |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161113 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18316399 |
We showed that beta-catenin interacts directly with myod, a basic helix-loop-helix transcription factor essential for muscle differentiation and enhances its binding to e box elements and transcriptional activity. |
|
| Publications: |
2 |
Organism: |
, Homo Sapiens |
| Tissue: |
Muscle |
| Pathways: | Rhabdomyosarcoma, WNT Signaling and Myogenesis |
| + |
WNT5A | up-regulates activity
|
MYOD1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60379 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9753670 |
Wnt4, wnt5a and wnt6 exert an intermediate effect activating both myf5 and myod equivalently in paraxial mesoderm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| Pathways: | WNT Signaling and Myogenesis |
| + |
SIRT1 | down-regulates activity
|
MYOD1 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241963 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12887892 |
Sir2 forms a complex with the acetyltransferase PCAF and MyoD and, when overexpressed, retards muscle differentiation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CyclinD/CDK4 | down-regulates
binding
|
MYOD1 |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216969 |
|
|
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, Rhabdomyosarcoma |
| + |
RB1 | up-regulates
binding
|
MYOD1 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176563 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
Cycline/cdk2 blocks myod-induced gene expression through the phosphorylation of rb, preventing rb from binding and transactivating myod, and triggering s phase entry instead of differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis, Rhabdomyosarcoma |
| + |
CREB1 | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176536 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21902831 |
Chen et al. showed that phosphorylated creb is present at high levels in cells of the dermomyotome that express pax3, myod and myf5 and that this phosphorylation is critical for the induction of these genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| Pathways: | WNT Signaling and Myogenesis |
| + |
CREBBP | up-regulates
acetylation
|
MYOD1 |
0.601 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81050 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10944526 |
Our results provide direct evidence that myod acetylation functionally activates the protein and show that both pcaf and cbp/p300 are candidate enzymes for myod acetylation in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
MYOD1 | down-regulates quantity by repression
transcriptional regulation
|
SP1 |
0.381 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241765 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 9148896 |
These data suggest a regulatory model in which MyoD activation during myogenesis causes the down-regulation of Sp1, which contributes to the repression of GLUT1 gene transcription and, therefore, leads to the reduction in GLUT1 expression and glucose transport. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PBX1 | up-regulates activity
binding
|
MYOD1 |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124834 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15149596 |
These domains are necessary for the stable binding of myod to the myogenin promoter through an interaction with an adjacent protein complex containing the homeodomain protein pbx, which appears to be constitutively bound at this site |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
ITGA7 |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241518 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 8798472 |
Only myogenin and MyoD were able to efficiently trans-activate the alpha7 promoter-CAT construct (Fig. 7). Myogenin trans-activated the promoter by _2-fold whereas MyoD was able to trans-activate by nearly 4-fold, indicating that both of these factors may play a role in alpha7 gene expression during muscle development. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SMAD3/SMAD4 | down-regulates activity
binding
|
MYOD1 |
0.624 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254986 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12244043 |
Taken together, these results suggest that myostatin inhibits MyoD activity and expression via Smad 3 resulting in the failure of the myoblasts to differentiate into myotubes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SHH | up-regulates
|
MYOD1 |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179632 |
|
|
Homo sapiens |
Satellite Cell |
| pmid |
sentence |
| 18662193 |
In addition, shh reactivation plays a regulatory role on myogenesis, as its inhibition impairs the activation of the myogenic regulatory factors myf-5 and myod, decreases the up-regulation of insulin-like growth factor (igf)-1 and reduces the number of myogenic satellite cells at injured site. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IFNG | down-regulates
|
MYOD1 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82467 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11009425 |
In contrast, in differentiated myotubes, tnf plus interferon-gamma (ifn-gamma) signaling was required for nf-kappab-dependent down-regulation of myod and dysfunction of skeletal myofibers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Myotube |
| + |
PTGS2 | up-regulates
|
MYOD1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256214 |
|
|
Homo sapiens |
Skeletal Muscle |
| pmid |
sentence |
| 20219869 |
Furthermore, COX-2 inhibition reduced MyoD expression in regenerating muscle, suggesting a role for COX-2 in modulating muscle differentiation, as well as growth |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMAD3 | down-regulates activity
binding
|
MYOD1 |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252071 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 11711431 |
We show that the TGF-beta intracellular effector Smad3, but not Smad2, mediates the inhibition of myogenic differentiation in MyoD-expressing C3H10T1/2 cells and C2C12 myoblasts by repressing the activity of the MyoD family of transcriptional factors. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FOXO | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252937 |
|
|
Homo sapiens |
Myoblast |
| pmid |
sentence |
| 18854138 |
Our cell-based assays and in vitro studies reveal a tight codependent partnership between foxo3 and pax3/7 to coordinately recruit rna polymerase ii and form a preinitiation complex (pic) to activate myod transcription in myoblasts. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MYOD1 | form complex
binding
|
MYOD/E12E47 |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241548 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 18094043 |
MyoD omodimers or heterodimers of MyoD plus E12 or E47 serve as transcription factor complexes that bind to CANNTG consensus sites in the promoter regions of genes, performing major functions in specification and differentiation of skeletl muscle precursor cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
| + |
MYOD1 | form complex
binding
|
MYOD1/SWI/SNF complex |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151682 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17194702 |
Myod targets brg1 to the myogenin promoter during the initiation of myogenesis in tissue culture models for skeletal muscle differentiation /initiation of myogenin transcription is dependent upon myod, the pbx homeodomain factor, and swi/snf chromatin-remodeling enzymes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
RNA helicases DDX5/DDX17 | up-regulates
binding
|
MYOD1 |
0.428 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17011493 |
We have found that the rna helicases p68/p72 are myod-associated proteins and that the noncoding rna sra also immunoprecipitates with myod. In vitro and in vivo experiments indicated that both p68/p72 and sra are coactivators of myod. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
EID1 | down-regulates
|
MYOD1 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253378 |
|
|
|
|
| pmid |
sentence |
| 11073990 |
Thus, EID-1 binds both Rb and p300 and is a novel repressor of MyoD function. |
|
| Publications: |
1 |
| + |
MYOD1 | up-regulates quantity by expression
transcriptional regulation
|
FST |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251727 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 15130492 |
MyoD, CREB, and NFAT Mediate the Transcriptional Activation of the Follistatin Promoter Induced by TSA |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ID2 | down-regulates activity
binding
|
MYOD1 |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240268 |
|
|
Mus musculus |
Myoblast |
| pmid |
sentence |
| 8380166 |
Id1 and Id2 interacted strongly with MyoD and Myf-5.Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ANGPT1 | up-regulates quantity by expression
transcriptional regulation
|
MYOD1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241529 |
|
|
Mus musculus |
Myoblast |
| pmid |
sentence |
| 26042050 |
Exogenous Ang-1 enhanced myogenic (MyoD and Myogenin) mRNA in differentiating myoblasts and increased myosin heavy chain protein. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MYOD1 | up-regulates quantity
transcriptional regulation
|
PJA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255718 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 28067271 |
... chromatin immunoprecipitation (ChIP) analysis showed MYOD binds to a site upstream the Pja1 promoter preferentially in C2C12 cells induced to differentiate (Fig. 2c). In addition, over-expression of MyoD in human fibroblasts is sufficient to up-regulate Pja1 expression |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
MYOD1
- 
- 