+ |
PRKCB | up-regulates activity
phosphorylation
|
ILF3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168173 |
Ser647 |
RGRGRGGsIRGRGRG |
Homo sapiens |
|
pmid |
sentence |
20870937 |
Upon T cell activation, NF90 translocates from the nucleus into the cytoplasm, where it binds to the AU-rich element-containing 3' untranslated regions of IL-2 mRNA and stabilizes it.|Our results support a model in which PMA stimulation activates PKCβI to phosphorylate NF90-Ser647, and this phosphorylation triggers NF90 relocation to the cytoplasm and stabilize IL-2 mRNA. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | up-regulates activity
phosphorylation
|
ILF3 |
0.376 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252512 |
Ser647 |
RGRGRGGsIRGRGRG |
Homo sapiens |
|
pmid |
sentence |
20870937 |
Upon T cell activation, NF90 translocates from the nucleus into the cytoplasm, where it binds to the AU-rich element-containing 3' untranslated regions of IL-2 mRNA and stabilizes it.|Our previous work showed that CD28 costimulation of T cells activated AKT to phosphorylate NF90 at Ser647 and caused NF90 to undergo nuclear export and stabilize IL-2 mRNA. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT | up-regulates activity
phosphorylation
|
ILF3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-168169 |
Ser647 |
RGRGRGGsIRGRGRG |
Homo sapiens |
|
pmid |
sentence |
20870937 |
Upon T cell activation, NF90 translocates from the nucleus into the cytoplasm, where it binds to the AU-rich element-containing 3' untranslated regions of IL-2 mRNA and stabilizes it.|Our previous work showed that CD28 costimulation of T cells activated AKT to phosphorylate NF90 at Ser647 and caused NF90 to undergo nuclear export and stabilize IL-2 mRNA. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ILF3 | form complex
binding
|
NF90-NF45 |
0.591 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268488 |
|
|
in vitro |
|
pmid |
sentence |
18458058 |
Nuclear factor 90 (NF90) and its C-terminally extended isoform, NF110, have been isolated as DNA- and RNA-binding proteins together with the less-studied protein NF45. These complexes have been implicated in gene regulation, but little is known about their cellular roles and whether they are redundant or functionally distinct. We show that heterodimeric core complexes, NF90-NF45 and NF110-NF45, exist within larger complexes that are more labile and contain multiple NF90/110 isoforms and additional proteins. This study identified NF45 as an unstable regulatory subunit of NF90-NF45 complexes and uncovered their critical role in normal cell division. Furthermore, the study revealed that NF90 is functionally distinct from NF110 and is more important for cell growth. |
|
Publications: |
1 |
Organism: |
In Vitro |