BAIT

TRIM2

CMT2R, RNF86
tripartite motif containing 2
GO Process (1)
GO Function (3)
GO Component (1)

Gene Ontology Biological Process

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.

Esposito D, Dudley-Fraser J, Garza-Garcia A, Rittinger K

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

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
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.

High4BioGRID
-

Curated By

  • BioGRID