BAIT

TRIM32

BBS11, HT2A, LGMD2H, TATIP, RP11-67K19.1
tripartite motif containing 32
GO Process (24)
GO Function (9)
GO Component (4)
Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Characterisation of class VI TRIM RING domains: linking RING activity to C-terminal domain identity.

Stevens RV, Esposito D, Rittinger K

TRIM E3 ubiquitin ligases regulate multiple cellular processes, and their dysfunction is linked to disease. They are characterised by a conserved N-terminal tripartite motif comprising a RING, B-box domains, and a coiled-coil region, with C-terminal domains often mediating substrate recruitment. TRIM proteins are grouped into 11 classes based on C-terminal domain identity. Class VI TRIMs, TRIM24, TRIM33, and TRIM28, have ... [more]

Life Sci Alliance Dec. 01, 2018; 2(3); [Pubmed: 31028095]

Throughput

  • Low Throughput

Additional Notes

  • interaction inferred from the ability of the bait protein TRIM32 to stimulate the in vitro discharge of ubiquitin from the purified hit protein UBE2E2, resulting in a transfer of that ubiquitin from the hit protein to a free lysine

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TRIM32 UBE2E2
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.

Low-BioGRID
-
UBE2E2 TRIM32
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.

Low-BioGRID
-

Curated By

  • BioGRID