ERBIN

This gene is a member of the leucine-rich repeat and PDZ domain (LAP) family. The encoded protein contains 17 leucine-rich repeats and one PDZ domain. It binds to the unphosphorylated form of the ERBB2 protein and regulates ERBB2 function and localization. It has also been shown to affect the Ras signaling pathway by disrupting Ras-Raf interaction. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.

Erbb2 Interacting Protein

Acts as an adapter for the receptor ERBB2, in epithelia. By binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may contribute to stabilize this unphosphorylated state (PubMed:16203728).

Inhibits NOD2-dependent NF-kappa-B signaling and proinflammatory cytokine secretion (PubMed:16203728).

Basal protein localization Source: UniProtKB
Cell adhesion Source: UniProtKB
Cellular response to tumor necrosis factor Source: UniProtKB
Epidermal growth factor receptor signaling pathway Source: UniProtKB
Establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
Integrin-mediated signaling pathway Source: UniProtKB
Intermediate filament cytoskeleton organization Source: UniProtKB
Negative regulation of monocyte chemotactic protein-1 production Source: Ensembl
Negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
Negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Source: UniProtKB
Positive regulation of Ras protein signal transduction Source: GO_Central
Protein targeting Source: Ensembl
Regulation of postsynaptic membrane neurotransmitter receptor levels Source: Ensembl
Response to lipopolysaccharide Source: UniProtKB
Response to muramyl dipeptide Source: UniProtKB
Signal transduction Source: GO_Central

Nucleus membrane; Basolateral cell membrane; Hemidesmosome. Found in hemidesmosomes, which are cell-substrate adhesion complexes in stratified epithelia. In transfected cells, either diffusely distributed over the cytoplasm or concentrated at the basolateral membrane. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes (By similarity).