+ |
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 |
+ |
USP25 | up-regulates quantity by stabilization
deubiquitination
|
TRiC |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273583 |
|
|
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: |
1 |
Organism: |
Homo Sapiens |