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Literature summary for 2.3.2.27 extracted from

  • Gack, M.U.; Shin, Y.C.; Joo, C.H.; Urano, T.; Liang, C.; Sun, L.; Takeuchi, O.; Akira, S.; Chen, Z.; Inoue, S.; Jung, J.U.
    TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity (2007), Nature, 446, 916-920.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[RING-E3-ubiquitin-carrier protein TRIM25]-S-ubiquitinyl-L-cysteine + [RIG-I]-L-lysine Homo sapiens
-
[RING-E3-ubiquitin-carrier protein TRIM25]-L-cysteine + [RIG-I]-N6-ubiquitinyl-L-lysine the amino-terminal caspase recruitment domains CARDs of retinoic-acid-inducible gene RIG-I undergo robust ubiquitination induced by TRIM25 in mammalian cells. 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. The Lys 172 residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for mitochondrial signaling protein MAVS binding, as well as the ability of RIG-I to induce antiviral signal transduction ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q14258 isoform TRIM25
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[RING-E3-ubiquitin-carrier protein TRIM25]-S-ubiquitinyl-L-cysteine + [RIG-I]-L-lysine
-
Homo sapiens [RING-E3-ubiquitin-carrier protein TRIM25]-L-cysteine + [RIG-I]-N6-ubiquitinyl-L-lysine the amino-terminal caspase recruitment domains CARDs of retinoic-acid-inducible gene RIG-I undergo robust ubiquitination induced by TRIM25 in mammalian cells. 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. The Lys 172 residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for mitochondrial signaling protein MAVS binding, as well as the ability of RIG-I to induce antiviral signal transduction ?
[RING-E3-ubiquitin-carrier protein TRIM25]-S-ubiquitinyl-L-cysteine + [RIG-I]-L-lysine
-
Homo sapiens [RING-E3-ubiquitin-carrier protein TRIM25]-L-cysteine + [RIG-I]-N6-ubiquitinyl-L-lysine the amino-terminal caspase recruitment domains CARDs of retinoic-acid-inducible protein RIG-I undergo robust ubiquitination induced by TRIM25 in mammalian cells. 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. The Lys 172 residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for mitochondrial signaling protein MAVS binding, as well as the ability of RIG-I to induce antiviral signal transduction ?

Synonyms

Synonyms Comment Organism
TRIM25
-
Homo sapiens

General Information

General Information Comment Organism
physiological function isoform TRIM25 is essential not only for retinoic-acid-inducible protein RIG-I ubiquitination but also for RIG-I-mediated interferon-beta production and antiviral activity in response to RNA virus infection Homo sapiens