Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | presence of ATP is required for catalysis | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
- |
Homo sapiens |
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Homo sapiens | 5737 | - |
nucleus | - |
Homo sapiens | 5634 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q86WT6 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
testis | - |
Homo sapiens | - |
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 | Comment | Organism |
---|---|---|
TRIM69 | - |
Homo sapiens |