+ |
TRIM25 | down-regulates quantity by destabilization
polyubiquitination
|
MAVS |
0.761 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272042 |
Lys10 |
FAEDKTYkYICRNFS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22626058 |
We report here that RLR activation triggers MAVS ubiquitination on lysine 7 and 10 by the E3 ubiquitin ligase TRIM25 and marks it for proteasomal degradation concomitantly with downstream signaling. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272041 |
Lys7 |
kTYKYICR |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22626058 |
We report here that RLR activation triggers MAVS ubiquitination on lysine 7 and 10 by the E3 ubiquitin ligase TRIM25 and marks it for proteasomal degradation concomitantly with downstream signaling. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
TRIM25 | down-regulates activity
ubiquitination
|
FBXW7 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277457 |
Lys412 |
VWSAVTGkCLRTLVG |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
31186535 |
This newly stabilized TRIM25 then directly ubiquitinates Lys412 of FBXW7α, a core subunit of the SKP1-Cullin-F-box (SCF) ubiquitin ligase complex involved in Myc ubiquitination, thereby stabilizing Myc. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAP3K13 | up-regulates quantity by stabilization
phosphorylation
|
TRIM25 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277456 |
Ser12 |
CPLAEELsCSICLEP |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
31186535 |
Mechanistically, MAP3K13 phosphorylates the E3 ubiquitin ligase TRIM25 at Ser12 to decrease its polyubiquitination and proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SRC | up-regulates activity
phosphorylation
|
TRIM25 |
0.274 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277405 |
Tyr278 |
NSKFDTIyQILLKKK |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
30100205 |
Here, we demonstrated that TRIM25 interacted with c-Src and underwent tyrosine phosphorylation by c-Src kinase upon viral infection and the phosphorylation is required for the complete activation of RIG-I signaling. Analysis using a c-Src inhibitor and TRIM25 mutant, in which tyrosine 278 is substituted by phenylalanine (Y278F), suggested that the phosphorylation positively regulates K63-linked polyubiquitination of RIG-I and subsequent antiviral signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM25 | down-regulates quantity by destabilization
ubiquitination
|
SFN |
0.589 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271548 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
12075357 |
Here we show that Efp is a RING-finger-dependent ubiquitin ligase (E3) that targets proteolysis of 14-3-3 sigma, a negative cell cycle regulator that causes G2 arrest. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
TRIM25 | down-regulates quantity by destabilization
polyubiquitination
|
AMFR |
0.372 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272176 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24810856 |
We further demonstrate that TRIM25 ubiquitylates gp78 and that overexpression of TRIM25 accelerates the degradation of gp78. Our data suggest that TRIM25 not only cooperates with gp78 in polyubiquitylation of AMF but also gauges the steady-state level of gp78. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM25 | down-regulates quantity by destabilization
polyubiquitination
|
KLF5 |
0.495 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271908 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
21542805 |
The oestrogen-inducible E3 ligase EFP (oestrogen-responsive finger protein) was identified as a key player in oestrogen-mediated degradation of KLF5, as knockdown and overexpression of EFP increased and decreased KLF5 protein levels respectively, and the decrease continued even when protein synthesis was blocked. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
TRIM25 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271155 |
|
|
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 |
+ |
LUBAC | down-regulates quantity by destabilization
polyubiquitination
|
TRIM25 |
0.48 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271859 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21292167 |
HOIL-1L/HOIP LUBAC induces TRIM25 ubiquitination and degradation.Upon detection of viral RNA, retinoic acid-inducible gene I (RIG-I) undergoes TRIM25-mediated K63-linked ubiquitination, leading to type I interferon (IFN) production. In this study, we demonstrate that the linear ubiquitin assembly complex (LUBAC), comprised of two RING-IBR-RING (RBR)-containing E3 ligases, HOIL-1L and HOIP, independently targets TRIM25 and RIG-I to effectively suppress virus-induced IFN production. RBR E3 ligase domains of HOIL-1L and HOIP bind and induce proteasomal degradation of TRIM25, whereas the NZF domain of HOIL-1L competes with TRIM25 for RIG-I binding. Consequently, both actions by the HOIL-1L/HOIP LUBAC potently inhibit RIG-I ubiquitination and antiviral activity, but in a mechanistically separate manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM25 | down-regulates quantity by destabilization
polyubiquitination
|
ZFHX3 |
0.463 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272048 |
|
|
Homo sapiens |
CWR22-Rv1 Cell |
pmid |
sentence |
22452784 |
In the present study we show that EFP (oestrogen-responsive finger protein) is an E3 ubiquitin ligase mediating oestrogen-induced ATBF1 protein degradation. Knockdown of EFP increases ATBF1 protein levels, whereas overexpression of EFP decreases ATBF1 protein levels. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM25 | down-regulates quantity by destabilization
ubiquitination
|
GPI |
0.253 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272178 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24810856 |
Gp78 is a ubiquitin ligase that plays a vital role in endoplasmic reticulum (ER)-associated degradation (ERAD). Here we report that autocrine motility factor (AMF), also known as phosphoglucose isomerase (PGI), is a novel substrate of gp78. We show that polyubiquitylation of AMF requires cooperative interaction between gp78 and the ubiquitin ligase TRIM25 (tripartite motif-containing protein 25). While TRIM25 mediates the initial round of ubiquitylation, gp78 catalyzes polyubiquitylation of AMF. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM25 | up-regulates activity
polyubiquitination
|
DDX58 |
0.795 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271645 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17392790 |
The carboxy-terminal SPRY domain of TRIM25 interacts with the N-terminal CARDs of RIG-I; this interaction effectively delivers the Lys 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, resulting in a marked increase in RIG-I downstream signalling activity. Thus, we demonstrate that TRIM25 E3 ubiquitin ligase induces the Lys 63-linked ubiquitination of RIG-I, which is crucial for the cytosolic RIG-I signalling pathway to elicit host antiviral innate immunity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |