| + |
CDK5 | up-regulates activity 
phosphorylation
|
TRIM59 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272929 |
Ser308 |
LIPKMKIsPKRMSCS |
|
|
| pmid |
sentence |
| 31488827 |
Here, we identify TRIM59 as a substrate of CDK5. EGFR-activated CDK5 directly binds to and phosphorylates TRIM59, a ubiquitin ligase at serine 308, which recruits PIN1 for cis-trans isomerization of TRIM59, leading to TRIM59 binding to importin α5 and nuclear translocation. |
|
| Publications: |
1 |
| + |
TRIM59 | down-regulates activity 
|
IRF7 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260374 |
|
|
Homo sapiens |
HeLa Cell, HEK-293T Cell |
| pmid |
sentence |
| 22588174 |
TRIM59 also inhibited the phosphorylation of IRF3 and IRF7, which induces dimerization, suggesting that TRIM59 negatively regulates kinases for IRF3/7 (IKKe/TBK1) or their upstream signal |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIM59 | down-regulates quantity by destabilization 
polyubiquitination
|
MACROH2A1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272931 |
|
|
|
|
| pmid |
sentence |
| 31488827 |
Nuclear TRIM59 induces ubiquitination and degradation of the tumor suppressive histone variant macroH2A1, leading to enhanced STAT3 signaling activation and tumorigenicity. |
|
| Publications: |
1 |
| + |
TRIM59 | down-regulates activity
|
IRF3 |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260373 |
|
|
Homo sapiens |
HeLa Cell, HEK-293T Cell |
| pmid |
sentence |
| 22588174 |
TRIM59 also inhibited the phosphorylation of IRF3 and IRF7, which induces dimerization, suggesting that TRIM59 negatively regulates kinases for IRF3/7 (IKKe/TBK1) or their upstream signal |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIM59 | down-regulates activity
binding
|
ECSIT |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260369 |
|
|
Homo sapiens |
HeLa Cell, HEK-293T Cell |
| pmid |
sentence |
| 22588174 |
In this study, we showed that one of the TRIM family ubiquitin ligases, TRIM59, interacts with ECSIT as an adaptor protein required for the TLR-mediated transduction pathway. The B-box and RING domains of TRIM59 are important for interaction with ECSIT.|ECSIT enhances IPS-1-mediated IFN-Beta promoter activation.|Luciferase reporter assays using reporter plasmids including NF-kappaB responsive element, interferon beta (IFN-beta) promoter and interferon-sensitive response element (ISRE) showed that overexpression of TRIM59 repressed their transcriptional activities, whereas knockdown of TRIM59 enhanced their transcriptional activities. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
TRIM59 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271123 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
TRIM59
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