| + |
AURKB | down-regulates 
phosphorylation
|
DES |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100107 |
Ser12 |
YSSSQRVsSYRRTFG |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. In the present study, we found aurora-b phosphorylates desmin at ser-11, thr-16, and ser-59, in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100111 |
Ser60 |
VYQVSRTsGGAGGLG |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. In the present study, we found aurora-b phosphorylates desmin at ser-11, thr-16, and ser-59, in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100115 |
Thr17 |
RVSSYRRtFGGAPGF |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. In the present study, we found aurora-b phosphorylates desmin at ser-11, thr-16, and ser-59, in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ROCK1 | down-regulates
phosphorylation
|
DES |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100177 |
Thr17 |
RVSSYRRtFGGAPGF |
in vitro |
|
| pmid |
sentence |
| 12686604 |
The sites phosphorylated by Aurora-B; Thr-7/Ser-13/Ser-38 of GFAP, and Thr-16 of desmin are common with those related to Rho-associated kinase (Rho-kinase), which has been reported to phosphorylate GFAP and desmin at cleavage furrow during cytokinesis. Rho-kinase was found to phosphorylate desmin at Thr-16, Thr-75, and Thr-76 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ROCK1 |
phosphorylation
|
DES |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249032 |
Thr17 |
RVSSYRRtFGGAPGF |
Homo sapiens |
SAOS-2 Cell |
| pmid |
sentence |
| 10574968 |
We developed antibodies specifically recognizing the kinase-dependent phosphorylation of desmin at Thr-16, Thr-75, and Thr-76. With these antibodies, phosphorylation of desmin was observed specifically at the cleavage furrow in late mitotic Saos-2 cells. We then found that treatment of the interphase cells with calyculin A revealed phosphorylation at all the three sites of desmin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249031 |
Thr76 |
LRASRLGtTRTPSSY |
Homo sapiens |
SAOS-2 Cell |
| pmid |
sentence |
| 10574968 |
We developed antibodies specifically recognizing the kinase-dependent phosphorylation of desmin at Thr-16, Thr-75, and Thr-76. With these antibodies, phosphorylation of desmin was observed specifically at the cleavage furrow in late mitotic Saos-2 cells. We then found that treatment of the interphase cells with calyculin A revealed phosphorylation at all the three sites of desmin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249033 |
Thr77 |
RASRLGTtRTPSSYG |
Homo sapiens |
SAOS-2 Cell |
| pmid |
sentence |
| 10574968 |
We developed antibodies specifically recognizing the kinase-dependent phosphorylation of desmin at Thr-16, Thr-75, and Thr-76. With these antibodies, phosphorylation of desmin was observed specifically at the cleavage furrow in late mitotic Saos-2 cells. We then found that treatment of the interphase cells with calyculin A revealed phosphorylation at all the three sites of desmin |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MYF5 | up-regulates quantity by expression 
transcriptional regulation
|
DES |
0.243 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241494 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 8382796 |
Desmin, the muscle specific intermediate filament (IF) protein, is expressed at low levels in myoblasts and at the onset of differentiation its expression increases several fold. In an effort to explore the mechanism involved in the tissue-specific and developmentally regulated expression of desmin, we have isolated the mouse desmin gene.Co-transfection of myoD, myogenin, MRF4 and Myf5, with the desmin-CAT construct into 10T-1/2 cells demonstrated that all these factors could transactivate desmin gene expression |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MYF6 | up-regulates quantity by expression
transcriptional regulation
|
DES |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241497 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 8382796 |
Desmin, the muscle specific intermediate filament (IF) protein, is expressed at low levels in myoblasts and at the onset of differentiation its expression increases several fold. In an effort to explore the mechanism involved in the tissue-specific and developmentally regulated expression of desmin, we have isolated the mouse desmin gene.Co-transfection of myoD, myogenin, MRF4 and Myf5, with the desmin-CAT construct into 10T-1/2 cells demonstrated that all these factors could transactivate desmin gene expression |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MYOG | up-regulates quantity by expression 
transcriptional regulation
|
DES |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241501 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 25653159 |
Ectopic expression of myogenin and a specific Mef2 isoform induced myogenic differentiation without activating endogenous MyoD expression. Under these conditions, the regulatory sequences of late gene loci were not in close proximity, and these genes were prematurely activated. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
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 |
| + |
MEF2D | up-regulates quantity by expression
transcriptional regulation
|
DES |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241504 |
|
|
Mus musculus |
Myoblast |
| pmid |
sentence |
| 25653159 |
Ectopic expression of myogenin and a specific Mef2 isoform induced myogenic differentiation without activating endogenous MyoD expression. Under these conditions, the regulatory sequences of late gene loci were not in close proximity, and these genes were prematurely activated. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
DES
- 
- 