BAIT

BEGAIN

brain-enriched guanylate kinase-associated
GO Process (0)
GO Function (1)
GO Component (0)

Gene Ontology Molecular Function

Homo sapiens
PREY

BEGAIN

brain-enriched guanylate kinase-associated
GO Process (0)
GO Function (1)
GO Component (0)

Gene Ontology Molecular Function

Homo sapiens

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.

Publication

Synaptic and nuclear localization of brain-enriched guanylate kinase-associated protein.

Yao I, Iida J, Nishimura W, Hata Y

Brain-enriched guanylate kinase-associated protein (BEGAIN) interacts with postsynaptic density (PSD)-95/synapse-associated protein (SAP) 90. In immunohistochemistry and immunocytochemistry, BEGAIN was detected in nuclei and at synapses in neurons. Nuclear localization was also confirmed through subcellular fractionation. BEGAIN was localized exclusively in nuclei when expressed in epithelial cells. These findings led us to analyze the mechanism to determine the subcellular localization of ... [more]

J. Neurosci. Jul. 01, 2002; 22(13);5354-64 [Pubmed: 12097487]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BEGAIN BEGAIN
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.

Low-BioGRID
-

Curated By

  • BioGRID