+ |
TRIM21 | down-regulates activity
ubiquitination
|
SQSTM1 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278602 |
Lys7 |
kAYLLGKE |
Homo sapiens |
|
pmid |
sentence |
26942676 |
TRIM21 directly ubiquitylates p62 at residue K7 to inhibit its oligomerization and sequestration function.|TRIM21 negatively regulates p62 mediated sequestration of Keap1 and antioxidant response. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM21 | up-regulates quantity
monoubiquitination
|
TRIM5 |
0.349 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271672 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18312418 |
Here, we show that TRIM5alpha functions as a RING-finger-type E3 ubiquitin ligase both in vitro and in vivo and ubiquitinates itself in cooperation with the E2 ubiquitin-conjugating enzyme UbcH5B. Thus, the ubiquitination of TRIM5alpha is catalyzed by itself and Ro52. Unexpectedly, although TRIM5alpha is ubiquitinated, our results have revealed that the proteasome inhibitors MG115 and MG132 do not stabilize it in HeLa cells, suggesting that the ubiquitination of TRIM5alpha does not lead to proteasomal degradation. Importantly, TRIM5alpha is clearly conjugated by a single ubiquitin molecule (monoubiquitination). Our monoubiquitin-fusion assay suggests that monoubiquitination is a signal for TRIM5alpha to translocate from cytoplasmic bodies to the cytoplasm. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM21 | down-regulates quantity by destabilization
ubiquitination
|
IRF7 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278619 |
|
|
Homo sapiens |
|
pmid |
sentence |
20668674 |
Furthermore, this Ro52 mediated degradation of IRF7 was inhibited in the presence of MG132, a proteasome inhibitor, indicating that IRF7 is targeted to the proteasome for degradation (XREF_FIG).|Ro52 ubiquitinates IRF7 in a dose dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM21 | down-regulates quantity
ubiquitination
|
DDX41 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278790 |
|
|
Homo sapiens |
|
pmid |
sentence |
23222971 |
Furthermore, overexpression of TRIM21 in mDCs led to lower expression of DDX41 in these mDCs and up to 70% less IFN-beta production by mDCs in response to intracellular DNA (XREF_FIG).|Here we report that the E3 ligase TRIM21 negatively regulated the type I interferon response in myeloid dendritic cells (mDCs) and monocytes that had been induced by cytosolic double stranded DNA (dsDNA), mainly by promoting the ubiquitination and degradation of DDX41. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM21 | down-regulates quantity
ubiquitination
|
IRF8 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278791 |
|
|
Homo sapiens |
|
pmid |
sentence |
28592884 |
From these results, we concluded that TRIM21 down-regulated IRF8 and enhanced the secretion of IL-12/23p40 in BD monocytes.|IRF8 is ubiquitinated by TRIM21, which promotes secretion of IL-12/23p40 after TLR/IFN-\u03b3 stimulation xref . |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM21 | down-regulates quantity
ubiquitination
|
SHMT2 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278792 |
|
|
Homo sapiens |
|
pmid |
sentence |
30367038 |
The expression of TRIM21, but not the expression of the ligase-dead (LD) mutant TRIM21 (C16A, C31A and H33W) 36, increased SHMT2 ubiquitylation, which suggests that TRIM21 is the E3 ligase for SHMT2 and that the E3 ligase activity of TRIM21 is required for SHMT2 ubiquitylation.|We found that the overexpression of TRIM21 increased the degradation of SHMT2 in high glucose conditions by binding more K63-ubiquitin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GNAO1 | up-regulates activity
binding
|
TRIM21 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278069 |
|
|
Homo sapiens |
GSC Cell Line |
pmid |
sentence |
39580518 |
These data demonstrate that GNAO1 recruits TRIM21 and mediates CREB ubiquitination and degradation to promote GSC differentiation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM21 | down-regulates quantity by destabilization
ubiquitination
|
FASN |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267368 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27758890 |
FASN acetylation enhanced its association with the E3 ubiquitin ligase TRIM21. Acetylation destabilized FASN and resulted in decreased de novo lipogenesis and tumor cell growth. FASN acetylation was frequently reduced in human hepatocellular carcinoma samples, which correlated with increased HDAC3 expression and FASN protein levels. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
TRIM21 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271063 |
|
|
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 |
+ |
TRIM21 | down-regulates
ubiquitination
|
GMPS |
0.33 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204478 |
|
|
Homo sapiens |
|
pmid |
sentence |
24462112 |
Cytoplasmic sequestration of gmps requires ubiquitylation by trim21, a ubiquitin ligase associated with autoimmune disease. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |