| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.95136815 |
| Co immunoprecipitation analysis demonstrates that NF 90 , NF 45 , and PKR form a complex in both nuclear and cytosolic extracts , and both proteins serve as substrates for PKR in vitro . 0.95136815^^^ Originally identified in complex with nuclear factor 45 ( NF 45 ) as a sequence specific DNA binding protein , NF 90 contains two double stranded RNA binding motifs ( dsRBMs ) and interacts with highly structured RNAs as well as the dsRNA activated protein kinase , PKR . 0.69518798^^^ NF 90 binds to PKR through two independent mechanisms : an RNA independent interaction occurs between the N terminus of NF 90 and the C terminal region of PKR , and an RNA dependent interaction is mediated by the dsRBMs of the two proteins . 0.57958352^^^ |
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| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.0 |
| DRBP 76 , a double stranded RNA binding nuclear protein , is phosphorylated by the interferon induced protein kinase , PKR . ^^^ DRBP 76 was also cloned by the yeast two hybrid screening of a cDNA library using a mutant PKR as bait . ^^^ DsRNA and PKR interactions of DRBP 76 were confirmed by analysis of in vitro translated and purified native proteins . ^^^ Cellular expression of an epitope tagged DRBP 76 demonstrated its nuclear localization , and its co immunoprecipitation with PKR demonstrated that the two proteins interact in vivo . ^^^ Finally , purified DRBP 76 was shown to be a substrate of PKR in vitro , indicating that this protein ' s cellular activities may be regulated by PKR mediated phosphorylation . . ^^^ |
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| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.0 |
| The NFAR gene ( nuclear factor associated with dsRNA ) encodes a putative transcription associated factor that we have shown is a substrate for the interferon inducible , dsRNA dependent protein kinase , PKR . ^^^ |
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| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.0 |
| Characterization of two evolutionarily conserved , alternatively spliced nuclear phosphoproteins , NFAR 1 and 2 , that function in mRNA processing and interact with the double stranded RNA dependent protein kinase , PKR . ^^^ We report here the isolation and characterization of two proteins , NFAR 1 and 2 , which were isolated through their ability to interact with the dsRNA dependent protein kinase , PKR . ^^^ Both NFAR 1 and 2 are phosphorylated by PKR , reciprocally co immunoprecipitate with PKR , and colocalize with the kinase in a diffuse nuclear pattern within the cell . ^^^ |
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| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.0 |
| Furthermore , NF 90 was phosphorylated in a double stranded RNA dependent manner likely by the interferon induced , double stranded RNA dependent protein kinase , PKR . ^^^ |
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| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.0 |
| As NF 90 can bind to double stranded RNA ( dsRNA ) and be phosphorylated by the dsRNA dependent protein kinase , PKR , we investigated whether accumulation of dsRNA in 10 infected cells could regulate IL 2 gene expression . ^^^ |
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| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q12906 and P19525 |
Pubmed |
SVM Score :0.0 |
| NA |
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