| + |
MAPK3 | up-regulates activity 
phosphorylation
|
IRX2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263060 |
Ser317 |
TPQGSRTsPGAPPPA |
in vitro |
|
| pmid |
sentence |
| 15133517 |
To identify the phosphorylated residue, we introduced a serine-to-alanine substitution at residues 294 and 326 and a threonine-to-alanine substitution at residue 331 in Irx2(291–356). Erk1 phosphorylated S294A and T331A, but not S326A (Fig. 4b), indicating that Ser326 is the bona fide MAP kinase target. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263061 |
Ser325 |
PGAPPPAsKPKLWSL |
in vitro |
|
| pmid |
sentence |
| 15133517 |
To identify the phosphorylated residue, we introduced a serine-to-alanine substitution at residues 294 and 326 and a threonine-to-alanine substitution at residue 331 in Irx2(291–356). Erk1 phosphorylated S294A and T331A, but not S326A (Fig. 4b), indicating that Ser326 is the bona fide MAP kinase target. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
IRX2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263052 |
Ser46 |
SASGSAFsPYPGSAA |
in vitro |
|
| pmid |
sentence |
| 15133517 |
We tested the transcriptional properties of Irx2 by dividing it into amino- and carboxy terminal parts and found that Mek1-mediated phosphorylation activates and derepresses the amino and carboxyl parts, respectively. When Ser46 and Ser65 were mutated to alanine (S46A and S65A), phosphorylation was reduced, whereas substitution of Ser83 and Ser103 (S83A and S103A) did not affect phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263053 |
Ser64 |
QAATGFGsPLQYSAD |
in vitro |
|
| pmid |
sentence |
| 15133517 |
We tested the transcriptional properties of Irx2 by dividing it into amino- and carboxy terminal parts and found that Mek1-mediated phosphorylation activates and derepresses the amino and carboxyl parts, respectively. When Ser46 and Ser65 were mutated to alanine (S46A and S65A), phosphorylation was reduced, whereas substitution of Ser83 and Ser103 (S83A and S103A) did not affect phosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
IRX2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270193 |
|
|
in vitro |
|
| pmid |
sentence |
| 15133517 |
To identify the phosphorylated residue, we introduced a serine-to-alanine substitution at residues 294 and 326 and a threonine-to-alanine substitution at residue 331 in Irx2(291–356). Erk1 phosphorylated S294A and T331A, but not S326A (Fig. 4b), indicating that Ser326 is the bona fide MAP kinase target. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
Gbeta | up-regulates activity
phosphorylation
|
IRX2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270097 |
|
|
in vitro |
|
| pmid |
sentence |
| 15133517 |
To identify the phosphorylated residue, we introduced a serine-to-alanine substitution at residues 294 and 326 and a threonine-to-alanine substitution at residue 331 in Irx2(291–356). Erk1 phosphorylated S294A and T331A, but not S326A (Fig. 4b), indicating that Ser326 is the bona fide MAP kinase target. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
IRX2 | down-regulates quantity by repression 
transcriptional regulation
|
CXCL10 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266042 |
|
|
Homo sapiens |
Hs-578T Cell |
| pmid |
sentence |
| 26560478 |
Our results imply that the IRX2 transcription factor might represent a novel metastasis associated protein that acts as a negative regulator of cellular motility and as a repressor of chemokine expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IRX2 | down-regulates quantity by repression
transcriptional regulation
|
CCL5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266043 |
|
|
Homo sapiens |
Hs-578T Cell |
| pmid |
sentence |
| 26560478 |
Our results imply that the IRX2 transcription factor might represent a novel metastasis associated protein that acts as a negative regulator of cellular motility and as a repressor of chemokine expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
IRX2
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