| + |
PRKCA | down-regulates activity 
phosphorylation
|
DLX3 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249096 |
Ser138 |
KPRTIYSsYQLAALQ |
in vitro |
|
| pmid |
sentence |
| 11343707 |
Dlx3 is primarily phosphorylated by PKC alpha. By deletion and mutational analysis, we show that the serine residue S(138), located in the homeodomain of Dlx3 protein, was specifically phosphorylated by PKC. The phosphorylation of purified Dlx3 proteins by PKC partially inhibited formation of complexes between Dlx3 protein and DNA. These results suggest that Dlx3 protein can be directly phosphorylated by PKC and this affects the DNA binding activity of Dlx3. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCA |
phosphorylation
|
DLX3 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249095 |
Ser138 |
KPRTIYSsYQLAALQ |
Mus musculus |
|
| pmid |
sentence |
| 11343707 |
Dlx3 is primarily phosphorylated by PKCalpha. By deletion and mutational analysis, we show that the serine residue S138, located in the homeodomain of Dlx3 protein, was specifically phosphorylated by PKC. The phosphorylation of purified Dlx3 proteins by PKC partially inhibited formation of complexes between Dlx3 protein and DNA. These results suggest that Dlx3 protein can be directly phosphorylated by PKC and this affects the DNA binding activity of Dlx3. | Since DNA binding may reveal only a part of Dlx3 protein function, we cannot rule out the influence of phosphorylation on other biological functions. Thus, the characterization of the full biological function of PKC phosphorylation of Dlx3 protein will require further studies. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKCA | up-regulates activity 
phosphorylation
|
DLX3 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249097 |
Thr134 |
KKVRKPRtIYSSYQL |
in vitro |
|
| pmid |
sentence |
| 11343707 |
Dlx3 is primarily phosphorylated by PKC alpha. By deletion and mutational analysis, we show that the serine residue S(138), located in the homeodomain of Dlx3 protein, was specifically phosphorylated by PKC. The phosphorylation of purified Dlx3 proteins by PKC partially inhibited formation of complexes between Dlx3 protein and DNA. These results suggest that Dlx3 protein can be directly phosphorylated by PKC and this affects the DNA binding activity of Dlx3. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
DLX3 | up-regulates quantity by expression 
transcriptional regulation
|
RUNX2 |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150177 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17060321 |
Here we show that bmp2 induces dlx3, a homeodomain protein that activates runx2 gene transcription. Small interfering rna knockdown studies in osteoblasts validate that dlx3 is a potent regulator of runx2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DLX3
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- 