| + |
CREBBP | down-regulates activity 
acetylation
|
DDX21 |
0.247 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275904 |
Lys137 |
PKKMKKEkEMNGETR |
|
|
| pmid |
sentence |
| 28790157 |
Significantly, the activity of DDX21 is regulated by acetylation. Acetylation by CBP inhibits DDX21 activity, while deacetylation by SIRT7 augments helicase activity and overcomes R-loop-mediated stalling of RNA polymerases.|acetylation of K18, K137, and K600 impairs the helicase activity of DDX21. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275902 |
Lys18 |
LESDTAMkKGETLRK |
|
|
| pmid |
sentence |
| 28790157 |
Significantly, the activity of DDX21 is regulated by acetylation. Acetylation by CBP inhibits DDX21 activity, while deacetylation by SIRT7 augments helicase activity and overcomes R-loop-mediated stalling of RNA polymerases.|acetylation of K18, K137, and K600 impairs the helicase activity of DDX21. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275906 |
Lys600 |
HFKQSAEkLIEEKGA |
|
|
| pmid |
sentence |
| 28790157 |
Significantly, the activity of DDX21 is regulated by acetylation. Acetylation by CBP inhibits DDX21 activity, while deacetylation by SIRT7 augments helicase activity and overcomes R-loop-mediated stalling of RNA polymerases.|acetylation of K18, K137, and K600 impairs the helicase activity of DDX21. |
|
| Publications: |
3 |
| + |
SIRT7 | up-regulates activity 
deacetylation
|
DDX21 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275903 |
Lys137 |
PKKMKKEkEMNGETR |
|
|
| pmid |
sentence |
| 28790157 |
Significantly, the activity of DDX21 is regulated by acetylation. Acetylation by CBP inhibits DDX21 activity, while deacetylation by SIRT7 augments helicase activity and overcomes R-loop-mediated stalling of RNA polymerases.|acetylation of K18, K137, and K600 impairs the helicase activity of DDX21. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275901 |
Lys18 |
LESDTAMkKGETLRK |
|
|
| pmid |
sentence |
| 28790157 |
Significantly, the activity of DDX21 is regulated by acetylation. Acetylation by CBP inhibits DDX21 activity, while deacetylation by SIRT7 augments helicase activity and overcomes R-loop-mediated stalling of RNA polymerases.|acetylation of K18, K137, and K600 impairs the helicase activity of DDX21. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275905 |
Lys600 |
HFKQSAEkLIEEKGA |
|
|
| pmid |
sentence |
| 28790157 |
Significantly, the activity of DDX21 is regulated by acetylation. Acetylation by CBP inhibits DDX21 activity, while deacetylation by SIRT7 augments helicase activity and overcomes R-loop-mediated stalling of RNA polymerases.|acetylation of K18, K137, and K600 impairs the helicase activity of DDX21. |
|
| Publications: |
3 |
| + |
DDX21 | up-regulates activity
binding
|
TICAM1 |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260192 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21703541 |
We demonstrated here that DDX1-DDX21-DHX36 represents a dsRNA sensor that uses the adaptor molecule TRIF to activate the NF-κB pathway and type I IFN responses in dendritic cells. Our study suggests that the DDX1-DDX21-DHX36 complex represents this missing poly I:C sensor, which uses DDX1 to bind poly I:C and uses DDX21 and DXH36 to bind TRIF. Poly I:C is a synthetic form of RNA that mimics double-stranded viral RNA. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV INNATE RESPONSE TO dsRNA |
| + |
DDX21 | up-regulates activity
binding
|
JUN |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260977 |
|
|
Homo sapiens |
HEK-293 Cell, HT-1080 Cell |
| pmid |
sentence |
| 11823437 |
C-Jun and RHII/Gu proteins interact in human cells at their endogenous level of expression. The helicase activity of RHII/Gu specifically facilitates c-Jun-mediated transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DDX1 | up-regulates activity
binding
|
DDX21 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260191 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21703541 |
We demonstrated here that DDX1-DDX21-DHX36 represents a dsRNA sensor that uses the adaptor molecule TRIF to activate the NF-κB pathway and type I IFN responses in dendritic cells. Our study suggests that the DDX1-DDX21-DHX36 complex represents this missing poly I:C sensor, which uses DDX1 to bind poly I:C and uses DDX21 and DXH36 to bind TRIF. Poly I:C is a synthetic form of RNA that mimics double-stranded viral RNA. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | COVID-19 Causal Network, Innate Immune Response, SARS-CoV INNATE RESPONSE TO dsRNA |
| + |
DDX21 | form complex 
binding
|
B-WICH complex |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268824 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21559432 |
The B-WICH complex is an extended form of WICH [26], and is involved in both RNA pol I and RNA pol III transcription [20], [21]. In addition to the three core proteins, WSTF, SNF2h, and nuclear myosin (NM1); the myb binding protein 1b, RNA helicase II/DXX21, and SAP155 all also associate via RNA species [21]. The subunit SNF2h is an ISWI ATPase, which slides nucleosomes in an ATP-dependent manner [27]. WSTF is a component of several complexes: two SNF2h complexes, B-WICH [21] and WICH [26], and one SWI/SNF type of chromatin remodelling complex, the WINAC complex, which is involved in vitamin D-mediated RNA pol II transcription |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DDX21
- 
- 