| + |
BTK | up-regulates activity 
phosphorylation
|
DDX41 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266404 |
Tyr414 |
DVIQEVEyVKEEAKM |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 25704810 |
The kinase and SH3/SH2 interaction domains of BTK bind, respectively, the DEAD-box domain of DDX41 and transmembrane region of STING. BTK phosphorylates DDX41, and its kinase activities are critical for STING-mediated IFN-β production. We show that Tyr364 and Tyr414 of DDX41 are critical for its recognition of AT-rich DNA and binding to STING, and tandem mass spectrometry identifies Tyr414 as the BTK phosphorylation site. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DDX41 | up-regulates activity
binding
|
STING1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266403 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 25704810 |
The kinase and SH3/SH2 interaction domains of BTK bind, respectively, the DEAD-box domain of DDX41 and transmembrane region of STING. BTK phosphorylates DDX41, and its kinase activities are critical for STING-mediated IFN-β production. We show that Tyr364 and Tyr414 of DDX41 are critical for its recognition of AT-rich DNA and binding to STING, and tandem mass spectrometry identifies Tyr414 as the BTK phosphorylation site. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
DDX41
- 
- 