| + |
NFATC2 | up-regulates activity 
binding
|
NF90-NF45 |
0.251 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268492 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 33555115 |
Herein, we demonstrate that NFAT, a key regulator of the immune response, translocates from cytoplasm to nucleolus and interacts with NF45/NF90 complex to collaboratively promote rDNA transcription via triggering the directly binding of NF45/NF90 to the ARRE2-like sequences in rDNA promoter upon T-cell activation in vitro. NF45/NF90‐mediated rDNA transcription contributes to T‐cell activation by interacting with NFATc2 in the nucleolus |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NF90-NF45 | down-regulates quantity by repression 
|
CDKN1A |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268491 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 25566957 |
In the present study, we investigated the expression profiles of NF45 in the sciatic nerve of adult rats following crush injury. in the TNF-α-induced Schwann cell proliferation assay, protein level of NF45 and cyclin E was elevated while expression of p21 was down-regulated. Further, when NF45 was knocked down, Schwann cell proliferation was interrupted and the expression of cyclin E was attenuated, while the expression of p21 was up-regulated. To repress the expression of p21 is one of the basic mechanisms for NF45-regulated cell proliferation. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
ILF3 | form complex 
binding
|
NF90-NF45 |
0.578 |
| 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 |
| + |
NF90-NF45 | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268490 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21969602 |
The NF90/NF45 complex participates in DNA break repair via nonhomologous end joining |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NF90-NF45 | up-regulates activity
binding
|
DNA-PK |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268489 |
|
|
in vitro |
|
| pmid |
sentence |
| 9442054 |
These proteins are NF90 and NF45, which are the 90- and 45-kDa subunits of a protein known to bind specifically to the antigen receptor response element of the interleukin 2 promoter, and the alpha, beta, and gamma subunits of eukaryotic translation initiation factor eIF-2. We also show that NF90, NF45, and eIF-2 beta are substrates for DNA-PK in vitro. In addition, recombinant NF90 promotes formation of a complex between DNA-PKcs, Ku, and DNA, and antibodies to recombinant NF90 or recombinant NF45 immunoprecipitate DNA-PKcs in vitro. Together, our data suggest that NF90, in complex with NF45, interacts with DNA-PKcs and Ku on DNA and that NF90 and NF45 may be important for the function of DNA-PK. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ILF2 | form complex
binding
|
NF90-NF45 |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268487 |
|
|
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 |
3.0
NF90-NF45