BAIT

NOD1

CARD4, CLR7.1, NLRC1
nucleotide-binding oligomerization domain containing 1
GO Process (33)
GO Function (6)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Homo sapiens

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

The E3 Ligase RNF34 is a Novel Negative Regulator of the NOD1 Pathway.

Zhang R, Zhao J, Song Y, Wang X, Wang L, Xu J, Song C, Liu F

Background/Aims: To identify the regulator of nucleotide-binding oligomerization domain-containing protein 1 (NOD1) and its regulatory function. Methods and Results : We performed a yeast two-hybrid screening assay and identified the E3 ligase RNF34 as a candidate partner of NOD1. Using co-immunoprecipitation (co-IP) and glutathione S transferase (GST)-pull down assays, we further confirmed that RNF34 is associated with NOD1. Western blotting ... [more]

Cell. Physiol. Biochem. Jun. 27, 2014; 33(6);1954-1962 [Pubmed: 25012219]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
NOD1 RNF34
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
-
RNF34 NOD1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
984355

Curated By

  • BioGRID