Crystallization (Comment) | Organism |
---|---|
crystal structure of the extended HECT domain of AREL1 (amino acids 436-823) at 2.4 A resolution. The extended HECT domain adopts an inverted, T-shaped, bilobed conformation and harbors an additional loop (aa 567-573) absent in other HECT members. The N-terminal extended region (aa 436-482) preceding the HECT domain is indispensable for its stability and activity and without this region, the HECT domain becomes inactive | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
E701A | substitution in the Arel1 HECT domain, substantially increases its autopolyubiquitination and SMAC ubiquitination activity | Homo sapiens |
additional information | deletion of the last three amino acids at the C-terminus of Arel1 completely abrogates Arel1 autoubiquitination and reduces SMAC ubiquitination | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O15033 | isoform Arel1 | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
ubiquitination | Arel1 shows autoubiquitination | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
[HECT-E3-ubiquitin-carrier protein Arel1]-S-ubiquitin-L-cysteine + [SMAC]-L-lysine | SMAC i.e. proapoptotic protein second mitochondria-derived activator of caspase | Homo sapiens | [HECT-E3-ubiquitin-carrier protein Arel1]-L-cysteine + [SMAC]-N6-ubiquinyl-L-lysine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
apoptosis-resistant E3 ligase 1 | - |
Homo sapiens |
AREL1 | - |
Homo sapiens |