Relation Results

Summary

Name TRIM22
Full Name E3 ubiquitin-protein ligase TRIM22
Synonyms 50 kDa-stimulated trans-acting factor, RING finger protein 94, RING-type E3 ubiquitin transferase TRIM22, Staf-50, Tripartite motif-containing protein 22 | RNF94, STAF50
Primary ID Q8IYM9
Links - -
Type protein
Relations 3
Function Interferon-induced antiviral protein involved in cell innate immunity. The antiviral activity could in part be mediated by TRIM22-dependent ubiquitina ...
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Type: Score: Layout: SPV 
0.20.3050.2Ub:E2TRIM22UBE2D2

Relations

Regulator
Mechanism
target
score
+ up-regulates activity img/direct-activation.png ubiquitination TRIM22 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271080 Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding TRIM22 0.305
Identifier Residue Sequence Organism Cell Line
SIGNOR-271779 Homo sapiens HEK-293 Cell
pmid sentence
 It was found that TRIM22 underwent self-ubiquitylation in vitro in combination with the E2 enzyme UbcH5B and the ubiquitylation was dependent on its RING finger domain. Further evidences showed that TRIM22 could also be self-ubiquitylated in vivo. Importantly, TRIM22 was conjugated with poly-ubiquitin chains and stabilized by the proteasome inhibitor in 293T cells, suggesting that TRIM22 targeted itself for proteasomal degradation through the poly-ubiquitylation. We also found that TRIM22 was located in the nucleus, indicating that TRIM22 might function as a nuclear E3 ubiquitin ligase.
Publications: 1 Organism: Homo Sapiens
+ down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination TRIM22 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271780 Homo sapiens HEK-293 Cell
pmid sentence
 Importantly, TRIM22 was conjugated with poly-ubiquitin chains and stabilized by the proteasome inhibitor in 293T cells, suggesting that TRIM22 targeted itself for proteasomal degradation through the poly-ubiquitylation. We also found that TRIM22 was located in the nucleus, indicating that TRIM22 might function as a nuclear E3 ubiquitin ligase.
Publications: 1 Organism: Homo Sapiens
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