BAIT

TRIM3

BERP, HAC1, RNF22, RNF97
tripartite motif containing 3
GO Process (1)
GO Function (2)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens
PREY

UBE2D1

E2(17)KB1, SFT, UBC4/5, UBCH5, UBCH5A
ubiquitin-conjugating enzyme E2D 1
GO Process (24)
GO Function (3)
GO Component (5)
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
TRIM3 UBE2D1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
1522018
UBE2D1 TRIM3
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-BioGRID
2699591

Curated By

  • BioGRID