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Literature summary for 2.3.2.27 extracted from

  • Han, Y.; Li, R.; Gao, J.; Miao, S.; Wang, L.
    Characterisation of human RING finger protein TRIM69, a novel testis E3 ubiquitin ligase and its subcellular localisation (2012), Biochem. Biophys. Res. Commun., 429, 6-11.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ATP presence of ATP is required for catalysis Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

Protein Variants

Protein Variants Comment Organism
C61A/C64A mutation of two adjacent cysteine residues at the conserved zinc-binding position, mutant shows weak activity Homo sapiens
additional information deletion of the 82 amino acids of the N-terminus of TRIM69, which contain the RING domain, results in loss of activity Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Homo sapiens 5737
-
nucleus
-
Homo sapiens 5634
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q86WT6
-
-

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information isoform TRIM69 mediates ubiquitylation in an E2 conjugating enzyme selective fashion in vitro, leading to multiubiquitylated products. E2 enzymes UbcH6, UbcH2, UbcH5A UbcH5C, or UbcH13/UeV1a are required, no products are detected with other E2s tested, and presence of ATP is required. An intact RING finger domain is indispensible for the process. TRIM69 can mediate ubiquitination in vivo, which can be enhanced by a proteasome inhibitor Homo sapiens ?
-
?
S-ubiquinyl-[UbcH13]-L-cysteine + [acceptor protein]-L-lysine
-
Homo sapiens [UbcH13]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
?

Synonyms

Synonyms Comment Organism
TRIM69
-
Homo sapiens