Crystallization (Comment) | Organism |
---|---|
structures of Nedd4 HECT domain, alone (2.5 A) and in complex with ubiquitin (2.7 A), showing new binding modes involving two surfaces on ubiquitin and both subdomains of the HECT N-lobes, suggesting an model for the HECT-t-substrate ubiquitin transfer, in which the growing chain on the substrate is kept close to the catalytic cysteine to promote processivity HECTNedd4 displays the typical HECT fold, composed of two lobes connected by a flexible hinge. The N-lobe consists of two moieties, the large and the smal subdomains. The small domains host the E2-binding site and the large carries the catalytic cysteine | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
F707A | Nedd4 mutant, almost abolished HECTNedd4 binding to Lys 63 ubiquitin. Mutant F707A has defective chain elongation on substrate or shorter free chains | Homo sapiens |
Y605A | Nedd4 mutant, almost abolished HECTNedd4 binding to Lys 63 ubiquitin | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P46934 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine | HECT ligases directly catalyse protein ubiquitination and non-covalently interact with ubiquitin. The ubiquitin bindung surface on the HECT might act to bind a ubiquitin moiety that is already conjugated to a protein substrate, thus promoting polyubiquitination. Mutation in the ubiquitin bindung surface strongly impairs free-chain fdormation and ubiquitination of all substrates tested | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | HECT ligases directly catalyse protein ubiquitination and non-covalently interact with ubiquitin. The ubiquitin bindung surface on the HECT might act to bind a ubiquitin moiety that is already conjugated to a protein substrate, thus promoting polyubiquitination. Mutation in the ubiquitin bindung surface (F707A and Y605A) mutants strongly impairs free-chain formation and ubiquitination of all substrates tested | Homo sapiens | ? | - |
? | |
additional information | Nedd4 has a strong preference for building Lys63 ubiquitin-chains on substrates. Mutant F707A has defective chain elongation on substrate or shorter free chains | Homo sapiens | ? | - |
? | |
[HECT-E3-ubiquitin-carrier protein NEDD4]-S-ubiquitin-L-cysteine + [gamma-epithel Na+-channel]-L-lysine | His-tagged Ube2D3, in addition the reaction mixture contains purified E1 enzyme and ubiquitin | Homo sapiens | [HECT-E3-ubiquitin-carrier protein NEDD4]-L-cysteine + [gamma-epithel Na+-channel]-N6-ubiquinyl-L-lysine | - |
? | |
[ubiquitin-conjugating enzyme E2D3]-S-ubiquitin-L-cysteine + [latent membrane protein 2A LMP2A]-L-lysine | His-tagged Ube2D3, in addition the reaction mixture contains purified E1 enzyme and ubiquitin | Homo sapiens | [ubiquitin-conjugating enzyme E2D3]-L-cysteine + [latent membrane protein 2A LMP2A]-N6-ubiquitinyl-L-lysine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
E3 ligase | - |
Homo sapiens |
E3 ubiquitin-protein ligase NEDD4 | - |
Homo sapiens |
HECT ligase | - |
Homo sapiens |
Nedd4 | - |
Homo sapiens |
Nedd4 HECT | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Homo sapiens |