PRKCI
Gene Ontology Biological Process
- Golgi vesicle budding [IDA]
- actin filament organization [ISO]
- cell migration [IMP]
- cell-cell junction organization [ISO]
- cellular protein localization [IMP]
- cellular response to insulin stimulus [IMP, ISO]
- establishment of apical/basal cell polarity [ISO]
- eye photoreceptor cell development [ISO]
- negative regulation of glial cell apoptotic process [ISO, ISS]
- negative regulation of neuron apoptotic process [ISO, ISS]
- positive regulation of NF-kappaB transcription factor activity [ISO, ISS]
- positive regulation of endothelial cell apoptotic process [ISO, ISS]
- positive regulation of establishment of protein localization to plasma membrane [ISO]
- positive regulation of glial cell proliferation [ISO, ISS]
- positive regulation of glucose import [ISO]
- positive regulation of neuron projection development [ISO, ISS]
- protein phosphorylation [IDA, ISO]
- response to interleukin-1 [IMP]
- response to peptide hormone [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Golgi membrane [IDA]
- Schmidt-Lanterman incisure [ISO]
- apical part of cell [ISO]
- apical plasma membrane [ISO]
- cell leading edge [IDA]
- cytoplasm [ISO]
- cytosol [IDA, ISO, ISS]
- extracellular vesicular exosome [ISO]
- intercellular bridge [ISO]
- microtubule cytoskeleton [ISO]
- nucleus [ISO, ISS]
- plasma membrane [IDA]
- protein complex [IDA]
- tight junction [IDA]
MBP
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Phosphorylation)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
Nerve growth factor stimulates the interaction of ZIP/p62 with atypical protein kinase C and targets endosomal localization: evidence for regulation of nerve growth factor-induced differentiation.
Atypical protein kinase Cs zeta and lambda/iota play a functional role in the regulation of NGF-induced differentiation and survival of pheochromocytoma, PC12 cells [Coleman and Wooten, 1994; Wooten et al., 1999]. Here we demonstrate an NGF-dependent interaction of aPKC with its binding protein, ZIP/p62. Although, ZIP/p62 was not a PKC-iota substrate, the formation of a ZIP/p62-aPKC complex in PC12 cells ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID