BAIT
TRIM2
CMT2R, RNF86
tripartite motif containing 2
GO Process (1)
GO Function (3)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Homo sapiens
PREY
UBE2W
UBC-16, UBC16
ubiquitin-conjugating enzyme E2W (putative)
GO Process (5)
GO Function (4)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Homo sapiens
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Divergent self-association properties of paralogous proteins TRIM2 and TRIM3 regulate their E3 ligase activity.
Tripartite motif (TRIM) proteins constitute a large family of RING-type E3 ligases that share a conserved domain architecture. TRIM2 and TRIM3 are paralogous class VII TRIM members that are expressed mainly in the brain and regulate different neuronal functions. Here we present a detailed structure-function analysis of TRIM2 and TRIM3, which despite high sequence identity, exhibit markedly different self-association and ... [more]
Nat Commun Dec. 08, 2022; 13(1);7583 [Pubmed: 36481767]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| UBE2W TRIM2 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | 4 | BioGRID | - |
Curated By
- BioGRID