+ |
EP300 | up-regulates
acetylation
|
KPNA2 |
0.363 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-128625 |
Lys22 |
HRFKNKGkDSTEMRR |
Homo sapiens |
|
pmid |
sentence |
15342649 |
Ampk triggered the acetylation of importin alpha1 on lys(22), a process dependent on the acetylase activity of p300 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMPK | up-regulates
phosphorylation
|
KPNA2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-216449 |
Ser105 |
QAARKLLsREKQPPI |
Homo sapiens |
|
pmid |
sentence |
15342649 |
Ampk phosphorylated importin alpha1 on ser(105). Accordingly, expression of importin alpha1 proteins bearing k22r or s105a mutations failed to mediate the nuclear import of hur in intact cells. Our results point to importin alpha1 as a critical downstream target of ampk and key mediator of ampk-triggered hur nuclear import. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKAA1 | up-regulates
phosphorylation
|
KPNA2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-128629 |
Ser105 |
QAARKLLsREKQPPI |
Homo sapiens |
|
pmid |
sentence |
15342649 |
Ampk phosphorylated importin alpha1 on ser(105). Accordingly, expression of importin alpha1 proteins bearing k22r or s105a mutations failed to mediate the nuclear import of hur in intact cells. Our results point to importin alpha1 as a critical downstream target of ampk and key mediator of ampk-triggered hur nuclear import. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ORF6 | down-regulates activity
relocalization
|
KPNA2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260272 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
17596301 |
Taken together, these data support a direct interaction between KPNA2 and ORF6 in the context of virus infection.|SARS-CoV, but not SARSdeltaORF6, retains KPNA2 at the ER/Golgi membrane. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
KPNA2 | down-regulates activity
binding
|
RNMT |
0.421 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265502 |
|
|
Homo sapiens |
|
pmid |
sentence |
26942677 |
KPNA2 Inhibits RNMT Activity|We report that CDK1-cyclin B1 phosphorylates the RNMT regulatory domain on T77 during G2/M phase of the cell cycle. RNMT T77 phosphorylation activates the enzyme both directly and indirectly by inhibiting interaction with KPNA2, an RNMT inhibitor. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KPNA2 | up-regulates activity
relocalization
|
IRF3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262514 |
|
|
Homo sapiens |
|
pmid |
sentence |
32979938 |
The results from Figure 1C suggest that ORF6 inhibits IFN-β production through IRF3 or a component downstream of IRF3. Thus, we examined the effect of ORF6 on IRF3 nuclear translocation. Upon poly(I:C) treatment, IRF3 translocated to the cell nucleus in the absence of ORF6, whereas the expression of ORF6 blocked its nuclear translocation (Figure 2D). Karyopherin α 1–6 (KPNA1–6) are importing factors for nuclear translocation of cargos, including IRF3, IRF7, and STAT1 (Chook and Blobel, 2001). Co-immunoprecipitation showed that ORF6 selectively interacted with KPNA2, but not the other KPNAs (Figure 2E), suggesting that ORF6 inhibits IFN-β production by binding to KPNA2 to block IRF3 nuclear translocation (Figure 2F). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | SARS-CoV INFLAMMATORY RESPONSE |
+ |
6 | down-regulates activity
binding
|
KPNA2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262513 |
|
|
Homo sapiens |
|
pmid |
sentence |
32979938 |
The results from Figure 1C suggest that ORF6 inhibits IFN-β production through IRF3 or a component downstream of IRF3. Thus, we examined the effect of ORF6 on IRF3 nuclear translocation. Upon poly(I:C) treatment, IRF3 translocated to the cell nucleus in the absence of ORF6, whereas the expression of ORF6 blocked its nuclear translocation (Figure 2D). Karyopherin α 1–6 (KPNA1–6) are importing factors for nuclear translocation of cargos, including IRF3, IRF7, and STAT1 (Chook and Blobel, 2001). Co-immunoprecipitation showed that ORF6 selectively interacted with KPNA2, but not the other KPNAs (Figure 2E), suggesting that ORF6 inhibits IFN-β production by binding to KPNA2 to block IRF3 nuclear translocation (Figure 2F). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | SARS-CoV INFLAMMATORY RESPONSE |