| + |
VRK2 | down-regulates quantity by destabilization 
phosphorylation
|
DTNBP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277403 |
Ser297 |
ELRAKPPsSSSTCTD |
in vitro |
|
| pmid |
sentence |
| 30062698 |
We show that VRK2 phosphorylates Ser 297 and Ser 299 of dysbindin using in vitro kinase assay. In addition, we found that VRK2-mediated phosphorylation of dysbindin enhanced ubiquitination of dysbindin and consequently resulted in the decrease in its protein stability through western blotting. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277404 |
Ser299 |
RAKPPSSsSTCTDSA |
in vitro |
|
| pmid |
sentence |
| 30062698 |
We show that VRK2 phosphorylates Ser 297 and Ser 299 of dysbindin using in vitro kinase assay. In addition, we found that VRK2-mediated phosphorylation of dysbindin enhanced ubiquitination of dysbindin and consequently resulted in the decrease in its protein stability through western blotting. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
VRK2 | up-regulates 
phosphorylation
|
NFATC2 |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199263 |
Ser31 |
PQDELDFsILFDYEY |
Homo sapiens |
|
| pmid |
sentence |
| 23105117 |
We demonstrate that vrk2 directly interacts and phosphorylates nfat1 in ser-32 within its n-terminal transactivation domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VRK2 | down-regulates
phosphorylation
|
BANF1 |
0.517 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143368 |
Ser4 |
sQKHRDFV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16371512 |
We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. Coexpression of vrk1 and gfp-baf greatly diminishes the association of baf with the nuclear chromatin/matrix and leads to its dispersal throughout the cell |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144795 |
Ser4 |
sQKHRDFV |
Homo sapiens |
|
| pmid |
sentence |
| 16495336 |
We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. Coexpression of vrk1 and gfp-baf greatly diminishes the association of baf with the nuclear chromatin/matrix and leads to its dispersal throughout the cell |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144799 |
Thr2 |
tTSQKHRD |
Homo sapiens |
|
| pmid |
sentence |
| 16495336 |
Herein, we demonstrate that b1, vrk1, and vrk2 efficiently phosphorylate the extreme n' terminus of the baf protein. We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144803 |
Thr3 |
tSQKHRDF |
Homo sapiens |
|
| pmid |
sentence |
| 16495336 |
We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. Coexpression of vrk1 and gfp-baf greatly diminishes the association of baf with the nuclear chromatin/matrix and leads to its dispersal throughout the cell |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
VRK2 | down-regulates activity
phosphorylation
|
USP25 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273579 |
Ser745 |
PEYLEQPsRSDFSKH |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25755282 |
Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2. USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates. Notably, USP25 deubiquitinating activity was suppressed when VRK2 phosphorylated the Thr(680), Thr(727), and Ser(745) residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273580 |
Thr680 |
QPLVGIEtLPPDLRD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25755282 |
Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2. USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates. Notably, USP25 deubiquitinating activity was suppressed when VRK2 phosphorylated the Thr(680), Thr(727), and Ser(745) residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273578 |
Thr727 |
QKLRESEtSVTTAQA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25755282 |
Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2. USP25 catalyzed deubiquitination of the TRiC protein and stabilized the chaperonin, thereby reducing accumulation of misfolded polyglutamine protein aggregates. Notably, USP25 deubiquitinating activity was suppressed when VRK2 phosphorylated the Thr(680), Thr(727), and Ser(745) residues. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
VRK2 | down-regulates quantity by destabilization
binding
|
TRiC |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272875 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24298020 |
Here, we propose that vaccinia-related kinase 2 (VRK2) is a critical enzyme that negatively regulates TRiC. In mammalian cells, overexpression of wild-type VRK2 decreased endogenous TRiC protein levels by promoting TRiC ubiquitination, but a VRK2 kinase-dead mutant did not.The VRK2-mediated reduction of TRiC protein levels was subsequent to the recruitment of COP1 E3 ligase. Among the members of the COP1 E3 ligase complex, VRK2 interacted with RBX1 and increased E3 ligase activity on TRiC in vitro. Taken together, these results demonstrate that VRK2 is crucial to regulate the ubiquitination-proteosomal degradation of TRiC, which controls folding of polyglutamine proteins involved in Huntington's disease.COP1 functions as an E3 ligase by forming a supercomplex that also includes heterodimeric substrate receptor DET1, adaptor DDB1, scaffold Cul4A, and RBX1 to recruit the E2 enzyme.The results suggest that VRK2 enables the COP1 complex to efficiently attach ubiquitin on the CCT4 by providing a close interaction between CCT4 and the COP1 complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VRK2 | up-regulates activity
binding
|
DCX DET1-COP1 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272874 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24298020 |
Here, we propose that vaccinia-related kinase 2 (VRK2) is a critical enzyme that negatively regulates TRiC. In mammalian cells, overexpression of wild-type VRK2 decreased endogenous TRiC protein levels by promoting TRiC ubiquitination, but a VRK2 kinase-dead mutant did not.The VRK2-mediated reduction of TRiC protein levels was subsequent to the recruitment of COP1 E3 ligase. Among the members of the COP1 E3 ligase complex, VRK2 interacted with RBX1 and increased E3 ligase activity on TRiC in vitro. Taken together, these results demonstrate that VRK2 is crucial to regulate the ubiquitination-proteosomal degradation of TRiC, which controls folding of polyglutamine proteins involved in Huntington's disease.COP1 functions as an E3 ligase by forming a supercomplex that also includes heterodimeric substrate receptor DET1, adaptor DDB1, scaffold Cul4A, and RBX1 to recruit the E2 enzyme |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
VRK2
- 
- 