BAIT

CTNNB1

CTNNB, MRD19, armadillo, OK/SW-cl.35
catenin (cadherin-associated protein), beta 1, 88kDa
GO Process (48)
GO Function (20)
GO Component (23)

Gene Ontology Biological Process

Homo sapiens

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT.

Graham TA, Clements WK, Kimelman D, Xu W

Beta-catenin is a multifunctional protein involved in both cell adhesion and transcriptional activation. Transcription mediated by the beta-catenin/Tcf complex is involved in embryological development and is upregulated in various cancers. We have determined the crystal structure at 2.5 A resolution of a complex between beta-catenin and ICAT, a protein that prevents the interaction between beta-catenin and Tcf/Lef family transcription factors. ... [more]

Mol. Cell Sep. 01, 2002; 10(3);563-71 [Pubmed: 12408824]

Throughput

  • Low Throughput

Additional Notes

  • figure 1.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CTNNB1 CTNNBIP1
Affinity Capture-Western
Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
692073

Curated By

  • BioGRID