SHANK2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- apical plasma membrane [ISS]
- brush border membrane [ISS]
- ciliary membrane [ISS]
- dendritic spine [ISS]
- growth cone [ISS]
- ionotropic glutamate receptor complex [ISS]
- neurofilament [ISS]
- neuron projection [ISS]
- neuronal cell body [ISS]
- photoreceptor inner segment [ISS]
- photoreceptor outer segment [ISS]
- plasma membrane [ISS]
- postsynaptic density [ISS]
- postsynaptic membrane [ISS]
DYNLL1
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [TAS]
- actin cytoskeleton organization [TAS]
- anatomical structure morphogenesis [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class II [TAS]
- apoptotic process [TAS]
- female gamete generation [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- mitotic cell cycle [TAS]
- negative regulation of phosphorylation [IDA]
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [TAS]
- substantia nigra development [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein.
NMDA receptors interact directly with postsynaptic density-95 (PSD-95), a scaffold protein that organizes a cytoskeletal- signaling complex at the postsynaptic membrane. The molecular mechanism by which the PSD-95-based protein complex is trafficked to the postsynaptic site is unknown but presumably involves specific motor proteins. Here we demonstrate a direct interaction between the PSD-95-associated protein guanylate kinase domain-associated protein (GKAP) and ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID