| + |
MAPK14 | up-regulates activity 
phosphorylation
|
DLX5 |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255792 |
Ser34 |
MHHPSQEsPTLPESS |
Mus musculus |
|
| pmid |
sentence |
| 18056716 |
We show that Dlx5 is a novel substrate for p38 MAPK in vitro and in vivo and that Ser-34 and Ser-217 are the sites phosphorylated by p38 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DLX5 | up-regulates 
|
Neurogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265797 |
|
|
in vitro |
|
| pmid |
sentence |
| 19195802 |
DLX5 and adjacent DLX6 are homeobox genes working in neurogenesis. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Rett syndrome |
| + |
DLX5 | down-regulates activity 
binding
|
MSX2 |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240925 |
|
|
Mus musculus |
Neuronal Cell Line |
| pmid |
sentence |
| 9111364 |
We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperative DNA binding; instead, dimerization and DNA binding are mutually exclusive activities. Msx proteins act as transcriptional repressors and Dlx proteins act as activators, while in combination, Msx and Dlx proteins counteract each other's transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MSX2 | down-regulates activity
binding
|
DLX5 |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240990 |
|
|
Mus musculus |
Neuronal Cell Line |
| pmid |
sentence |
| 9111364 |
We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperative DNA binding; instead, dimerization and DNA binding are mutually exclusive activities. Msx proteins act as transcriptional repressors and Dlx proteins act as activators, while in combination, Msx and Dlx proteins counteract each other's transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DLX5 | up-regulates
|
Osteoblast_differentiation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255450 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 12000792 |
In conclusion, Dlx5 and Dlx6 are dynamic regulators of mammalian development, which are absolutely required for proper craniofacial and skeletal development and which display overlapping genetic functions in all tissues in which they are expressed. In addition, they appear to act as essential regulators of chondrogenesis and osteogenesis. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
TBX22 | down-regulates quantity by repression
transcriptional regulation
|
DLX5 |
0.315 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265566 |
|
|
Gallus gallus |
UMNSAH/DF-1 Cell |
| pmid |
sentence |
| 20033915 |
the main function of TBX22 as shown in misexpression experiments is to decrease proliferation. We subsequently uncovered three targets of TBX22, DLX5, MSX2, and TBX22 itself. All are downregulated in the presence of viral-derived hTBX22. |
|
| Publications: |
1 |
Organism: |
Gallus Gallus |
| + |
SMAD5/SMAD4 | up-regulates
transcriptional regulation
|
DLX5 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255790 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12815054 |
Over-expression of Smad1 or Smad5, mediators of BMP-signaling, also induced Dlx5 expression even in the absence of BMP-2 treatment concomitant with positive ALP staining |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DLX5 | up-regulates quantity
transcriptional regulation
|
SPP1 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245340 |
|
|
Gallus gallus |
|
| pmid |
sentence |
| 17335796 |
Dlx5 initiates a complete osteogenic differentiation in these early primary cells, by triggering Runx2, osteopontin, alkaline phosphatase, and other gene expression according to the sequential temporal sequence observed during skull osteogenesis in vivo. |
|
| Publications: |
1 |
Organism: |
Gallus Gallus |
| + |
MSX1 | down-regulates activity
binding
|
DLX5 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240987 |
|
|
Mus musculus |
NT2/D1 Cell |
| pmid |
sentence |
| 9111364 |
We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperative DNA binding; instead, dimerization and DNA binding are mutually exclusive activities. Msx proteins act as transcriptional repressors and Dlx proteins act as activators, while in combination, Msx and Dlx proteins counteract each other's transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MECP2 | down-regulates quantity by repression 
transcriptional regulation
|
DLX5 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254034 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19195802 |
Expression of DLX5 is controlled by MECP2, and defect in MECP2 induced an over-expression of DLX5 in lymphocytes as well as in the brain |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Rett syndrome |
| + |
SMAD1/4 | up-regulates
transcriptional regulation
|
DLX5 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255789 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12815054 |
Over-expression of Smad1 or Smad5, mediators of BMP-signaling, also induced Dlx5 expression even in the absence of BMP-2 treatment concomitant with positive ALP staining |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AKT | up-regulates
phosphorylation
|
DLX5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244228 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Akt, a member of the ser-ine/threonine-specific protein kinase, was found to phosphorylate osx and dlx5. akt interacts with and phosphorylates dlx5. In addition, we provide evidences that akt kinase activity is important for akt to enhance the protein stability and transcriptional activity of dlx5. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173976 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21619873 |
Akt, a member of the ser-ine/threonine-specific protein kinase, was found to phosphorylate osx and dlx5. akt interacts with and phosphorylates dlx5. In addition, we provide evidences that akt kinase activity is important for akt to enhance the protein stability and transcriptional activity of dlx5. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates
phosphorylation
|
DLX5 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195546 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Akt, a member of the ser-ine/threonine-specific protein kinase, was found to phosphorylate osx and dlx5. akt interacts with and phosphorylates dlx5. In addition, we provide evidences that akt kinase activity is important for akt to enhance the protein stability and transcriptional activity of dlx5. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252513 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21619873 |
Akt, a member of the ser-ine/threonine-specific protein kinase, was found to phosphorylate osx and dlx5. akt interacts with and phosphorylates dlx5. In addition, we provide evidences that akt kinase activity is important for akt to enhance the protein stability and transcriptional activity of dlx5. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SMAD1/5/8/SMAD4 | up-regulates
transcriptional regulation
|
DLX5 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255837 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12815054 |
Over-expression of Smad1 or Smad5, mediators of BMP-signaling, also induced Dlx5 expression even in the absence of BMP-2 treatment concomitant with positive ALP staining |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DLX5 | up-regulates quantity by expression
transcriptional regulation
|
RUNX2 |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195576 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22298955 |
Dlx5 can drive runx2 expression and osteogenic differentiation in developing cranial suture mesenchyme , indicat-ing that dlx5 can work as an upstream gene of runx2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153454 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17335796 |
Dlx5 can drive runx2 expression and osteogenic differentiation in developing cranial suture mesenchyme. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DLX5 | up-regulates quantity
transcriptional regulation
|
MYC |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241914 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19497851 |
Here we demonstrate by luciferase assay that the MYC promoter is specifically activated by overexpression of DLX5 and that two DLX5 binding sites in the MYC promoter are important for transcriptional activation of MYC. We also show that DLX5 binds to the MYC promoter both in vitro and in vivo and that transfection of a DLX5 expression plasmid promotes the expression of MYC in a dose-dependent manner in mammalian cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POU5F1 | down-regulates quantity by repression
transcriptional regulation
|
DLX5 |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254935 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17068183 |
To enhance our understanding of the molecular basis of this differentiation event in humans, we used a functional genomics approach involving RNA interference-mediated suppression of OCT4 function in a human ESC line and analysis of the resulting transcriptional profiles to identify OCT4-dependent genes in human cells. We detected altered expression of >1,000 genes, including targets regulated directly by OCT4 either positively (NANOG, SOX2, REX1, LEFTB, LEFTA/EBAF DPPA4, THY1, and TDGF1) or negatively (CDX2, EOMES, BMP4, TBX18, Brachyury [T], DKK1, HLX1, GATA6, ID2, and DLX5), as well as targets for the OCT4-associated stem cell regulators SOX2 and NANOG. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLX5 | down-regulates activity
binding
|
MSX1 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240921 |
|
|
Mus musculus |
NT2/D1 Cell |
| pmid |
sentence |
| 9111364 |
We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperative DNA binding; instead, dimerization and DNA binding are mutually exclusive activities. Msx proteins act as transcriptional repressors and Dlx proteins act as activators, while in combination, Msx and Dlx proteins counteract each other's transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
DLX5
- 
- 