BAIT
ERBB2IP
ERBIN, HEL-S-78, LAP2
erbb2 interacting protein
GO Process (9)
GO Function (4)
GO Component (8)
Gene Ontology Biological Process
- basal protein localization [NAS]
- cell adhesion [NAS]
- cell cycle [NAS]
- cell growth [NAS]
- epidermal growth factor receptor signaling pathway [TAS]
- establishment or maintenance of epithelial cell apical/basal polarity [NAS]
- integrin-mediated signaling pathway [NAS]
- intermediate filament cytoskeleton organization [NAS]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
KCNA5
ATFB7, HCK1, HK2, HPCN1, KV1.5, PCN1
potassium voltage-gated channel, shaker-related subfamily, member 5
GO Process (10)
GO Function (7)
GO Component (6)
Gene Ontology Biological Process
- atrial cardiac muscle cell action potential [IMP]
- membrane hyperpolarization [IMP]
- potassium ion export [IDA, IMP]
- potassium ion transport [IDA]
- regulation of atrial cardiac muscle cell membrane repolarization [IMP]
- regulation of heart rate by cardiac conduction [IMP]
- regulation of insulin secretion [TAS]
- regulation of membrane potential [IDA]
- regulation of potassium ion transport [IMP]
- synaptic transmission [TAS]
Gene Ontology Molecular Function- alpha-actinin binding [IPI]
- delayed rectifier potassium channel activity [IDA, IMP]
- outward rectifier potassium channel activity [IDA, IMP]
- protein binding [IPI]
- protein kinase binding [IPI]
- scaffold protein binding [IPI]
- voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization [IMP]
- alpha-actinin binding [IPI]
- delayed rectifier potassium channel activity [IDA, IMP]
- outward rectifier potassium channel activity [IDA, IMP]
- protein binding [IPI]
- protein kinase binding [IPI]
- scaffold protein binding [IPI]
- voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization [IMP]
Gene Ontology Cellular Component
Homo sapiens
Protein-peptide
An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.
Publication
An improved method for the synthesis of cellulose membrane-bound peptides with free C termini is useful for PDZ domain binding studies.
SPOT synthesis permits parallel synthesis and screening of thousands of cellulose membrane-bound peptides to study protein-protein interactions in a proteomic context. Recognition of C-terminal residues is one of the most common binding features of PDZ domains. Unfortunately, most solid support-bound peptide libraries lack a free C terminus due to C-terminal fixation on the solid support. To overcome this restriction, we ... [more]
Chem. Biol. Apr. 01, 2004; 11(4);449-59 [Pubmed: 15123239]
Throughput
- Low Throughput
Curated By
- BioGRID