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
UBE2E1
UBCH6
ubiquitin-conjugating enzyme E2E 1
GO Process (14)
GO Function (4)
GO Component (4)
Gene Ontology Biological Process
- ISG15-protein conjugation [IDA]
- anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process [TAS]
- cytokine-mediated signaling pathway [TAS]
- histone H2B ubiquitination [IDA]
- histone monoubiquitination [IDA]
- mitotic cell cycle [TAS]
- mitotic spindle assembly checkpoint [TAS]
- negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- protein K48-linked ubiquitination [IDA]
- protein polyubiquitination [IDA]
- protein ubiquitination [IDA]
- regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [TAS]
- ubiquitin-dependent protein catabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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 |
---|---|---|---|---|---|---|
UBE2E1 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