+ |
PIAS1 | up-regulates
sumoylation
|
DDX5 |
0.526 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-153719 |
Lys53 |
WNLDELPkFEKNFYQ |
Homo sapiens |
|
pmid |
sentence |
17369852 |
We demonstrate that the sumo e3 ligase pias1 interacts with p68 and enhances its sumo modification in vivo / sumo modification enhances p68 transcriptional repression activity and inhibits the ability of p68 to function as a coactivator of p53. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCA | down-regulates activity
phosphorylation
|
DDX5 |
0.341 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248896 |
Ser557 |
VSAGIQTsFRTGNPT |
in vitro |
|
pmid |
sentence |
7525583 |
We report that p68 is phosphorylated by protein kinase C in vitro and binds calmodulin in a Ca(2+)-dependent manner. Both phosphorylation and calmodulin binding inhibited p68 ATPase activity | In addition, a 20-amino acid peptide corresponding to residues 549-568 of p68 was phosphorylated in a Ca- and phospholipid-dependent manner hy PKC |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PAK5 | up-regulates quantity by stabilization
phosphorylation
|
DDX5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275658 |
Thr69 |
HPDLARRtAQEVETY |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
34936874 |
PAK5 promotes RNA helicase DDX5 sumoylation and miRNA-10b processing in a kinase-dependent manner in breast cancer|The increased expression levels of PAK5 and phospho-DDX5 threonine 69 are associated with metastasis and poor clinical outcomes of patients. PAK5 facilitates the phosphorylation-dependent sumoylation of DDX5 to stabilize DDX5. Both the phosphorylation and sumoylation of DDX5 enhance the formation of a DDX5/Drosha/DGCR8 complex, thus promoting microRNA-10b processing. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ABL1 | up-regulates
phosphorylation
|
DDX5 |
0.366 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-149988 |
Tyr593 |
NGMNQQAyAYPATAA |
Homo sapiens |
|
pmid |
sentence |
17018282 |
These results suggested that p68 was phosphorylated by c-abl in ht-29 cells under stimulation of pdgf. we demonstrated that tyrosine phosphorylation of p68 at y593 mediated pdgf-stimulated epithelial-mesenchymal transition (emt). We showed that pdgf treatment led to phosphorylation of p68 at y593 in the cell nucleus. The y593-phosphorylated p68 (referred to as phosphor-p68) promotes beta-catenin nuclear translocation via a wnt-independent pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DDX5 | up-regulates
binding
|
RUNX2 |
0.466 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236974 |
|
|
Mus musculus |
C2C12 Cell |
pmid |
sentence |
17960593 |
P68 (ddx5) interacts with runx2 and regulates osteoblast differentiation. / p68 is a novel co-activator for runx2 |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
DDX5 | up-regulates
binding
|
AR |
0.326 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-181456 |
|
|
Homo sapiens |
|
pmid |
sentence |
18829551 |
P68 is a nuclear protein and interacts with ar / p68 co-occupies the active psa promoter at are regions and enhances ar transcriptional activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DDX5 | up-regulates
binding
|
TP53 |
0.691 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133341 |
|
|
Homo sapiens |
|
pmid |
sentence |
15660129 |
The dead box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DDX5 | up-regulates quantity
post transcriptional regulation
|
mir-10b |
0.4 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275660 |
|
|
|
|
pmid |
sentence |
34936874 |
Both the phosphorylation and sumoylation of DDX5 enhance the formation of a DDX5/Drosha/DGCR8 complex, thus promoting microRNA-10b processing. |
|
Publications: |
1 |
+ |
CBP/p300 | up-regulates
binding
|
DDX5 |
0.469 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97274 |
|
|
Homo sapiens |
|
pmid |
sentence |
12527917 |
Cbp/p300 interact with p68 rna helicase / the atpase activity of p68 is required for the specific transcriptional activation of cbp |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DDX5 | form complex
binding
|
RNA helicases DDX5/DDX17 |
0.434 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-149964 |
|
|
Homo sapiens |
|
pmid |
sentence |
17011493 |
We have found that the rna helicases p68/p72 are myod-associated proteins and that the noncoding rna sra also immunoprecipitates with myod. In vitro and in vivo experiments indicated that both p68/p72 and sra are coactivators of myod. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Muscle, Skeletal Muscle |
+ |
DDX5 | up-regulates activity
binding
|
Microprocessor complex |
0.713 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275659 |
|
|
|
|
pmid |
sentence |
34936874 |
Both the phosphorylation and sumoylation of DDX5 enhance the formation of a DDX5/Drosha/DGCR8 complex, thus promoting microRNA-10b processing. |
|
Publications: |
1 |
+ |
DDX5 | up-regulates
binding
|
HDAC1 |
0.401 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-153715 |
|
|
Homo sapiens |
|
pmid |
sentence |
17369852 |
Wt p68 co-immunoprecipitates efficiently with hdac1, the k53r p68 does not / sumoylation is important for the interaction of p68 with hdac1 and for transcriptional repression by p68 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
rep | up-regulates activity
binding
|
DDX5 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260250 |
|
|
Homo sapiens |
|
pmid |
sentence |
19224332 |
To our knowledge, this is the first report to show that SARS-CoV helicase can interact directly with multifunctional protein Ddx5 in cell culture and that inhibition of Ddx5 results in the suppression of viral replication. We speculate that Ddx5 may act as a coactivator by direct binding to the SARS-CoV helicase, resulting in enhanced viral genome transcription and virus proliferation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |