Unique identifier for interactor A | uniprotkb:O15037 |
Unique identifier for interactor B | uniprotkb:Q15843 |
Alternative identifier for interactor A | intact:EBI-6148525 uniprotkb:Q86TZ6 uniprotkb:Q8IUQ2 uniprotkb:Q96BA9 ensembl:ENSP00000251343.5 ensembl:ENSP00000450799.1 ensembl:ENSP00000451106.1 |
Alternative identifier for interactor B | intact:EBI-716247 uniprotkb:Q3SXN8 uniprotkb:Q6LES6 ensembl:ENSP00000250495.5 ensembl:ENSP00000496420.1 |
Aliases for A | psi-mi:khnyn_human(display_long) uniprotkb:KHNYN(gene name) psi-mi:KHNYN(display_short) uniprotkb:KH and NYN domain-containing protein(gene name synonym) uniprotkb:KIAA0323(gene name synonym) |
Aliases for B | psi-mi:nedd8_human(display_long) uniprotkb:Ubiquitin-like protein Nedd8(gene name synonym) uniprotkb:Neddylin(gene name synonym) uniprotkb:Neural precursor cell expressed developmentally down-regulated protein 8(gene name synonym) uniprotkb:NEDD8(gene name) psi-mi:NEDD8(display_short) |
Interaction detection methods | psi-mi:"MI:0096"(pull down) |
First author | Castagnoli et al. (2019) |
Identifier of the publication | pubmed:30659753 imex:IM-26819 |
NCBI Taxonomy identifier for interactor A | taxid:9606(human) taxid:9606(Homo sapiens) |
NCBI Taxonomy identifier for interactor B | taxid:9606(human) taxid:9606(Homo sapiens) |
Interaction types | psi-mi:"MI:0407"(direct interaction) |
Source databases and identifiers | psi-mi:"MI:0471"(MINT) |
Interaction identifier(s) in the corresponding source database | intact:EBI-21222635 imex:IM-26819-77 |
Confidence score | intact-miscore:0.70 |
Complex expansion | - |
Biological role A | Unspecified role |
Biological role B | Unspecified role |
Experimental role A | Prey |
Experimental role B | Bait |
Interactor type A | Protein |
Interactor type B | Protein |
Annotations for the interaction | figure legend:fig 11b comment:"\"To confirm our model, we mutated residues Glu31 and Glu32 in NEDD8 by substituting them with the corresponding residues in ubiquitin (Glu31Gln and Glu32Asp) or with an opposite charge (Glu31Lys and Glu32Lys). These mutants, together with the Ile44Ala and the Ala72Arg mutants, were assayed in a pull‐down experiment against the purified CUBAN domain (Fig. 11B). As shown, there is a clear loss of binding when mutating the hydrophobic patch key residue Ile44, while the Ala72Arg mutation reduces the binding efficiency as previously shown. In addition, there is a reduction in binding efficiency when using the mutants H25F and R38E, but not K26D and R33E, in the electrostatic binding surface of CUBAN domain (Fig. 11C).\"" curation depth:imex curation full coverage:Only protein-protein interactions |
NCBI Taxonomy identifier for the host organism | taxid:-1(in vitro) taxid:-1(In vitro) |
Parameters of the interaction | - |
Creation date | 2019/02/19 |
Update date | 2024/11/14 |
negative Boolean value | false |
Feature(s) for interactor A | binding-associated region:598-678 |
Feature(s) for interactor B | glutathione s tranferase tag:?-? mutation increasing interaction:31-31 mutation disrupting interaction:44-44 mutation decreasing interaction:72-72 mutation decreasing interaction:31-32 mutation decreasing interaction:31-31 mutation decreasing interaction:31-31 mutation decreasing interaction:32-32 mutation disrupting interaction:31-32 |
Stoichiometry for interactor A | - |
Stoichiometry for interactor B | - |
Participant identification method for interactor A | Western blot |
Participant identification method for interactor B | Western blot |