BAIT

CHORDC1

1110001O09Rik, AA409036, Chp-1, morgana
cysteine and histidine-rich domain (CHORD)-containing, zinc-binding protein 1
Mus musculus

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.

Publication

Regulation of Nod1 by Hsp90 chaperone complex.

Hahn JS

Nod1 and Nod2 proteins play important roles in mammalian innate immune responses as intracellular sensors for bacterial peptidoglycan. Nod1 and Nod2 share structural homology with many R proteins involved in plant disease resistance. It has been demonstrated that plant Hsp90 and its co-chaperone RAR1 are implicated in R-mediated disease resistance. Here the Chp-1 gene encoding a mammalian homologue of plant ... [more]

FEBS Lett. Aug. 15, 2005; 579(20);4513-9 [Pubmed: 16083881]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CHORDC1 HSP90AB1
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
-
HSP90AB1 CHORDC1
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High0.719BioGRID
2667774

Curated By

  • BioGRID