PRKCZ
Gene Ontology Biological Process
- blood coagulation [TAS]
- establishment of cell polarity [ISS]
- long-term synaptic potentiation [ISS]
- negative regulation of insulin receptor signaling pathway [IMP]
- negative regulation of peptidyl-tyrosine phosphorylation [IMP]
- negative regulation of protein complex assembly [IMP]
- peptidyl-serine phosphorylation [IDA]
- platelet activation [TAS]
- positive regulation of ERK1 and ERK2 cascade [IMP]
- positive regulation of NF-kappaB transcription factor activity [ISS]
- positive regulation of T-helper 2 cell cytokine production [ISS]
- positive regulation of T-helper 2 cell differentiation [ISS]
- positive regulation of excitatory postsynaptic membrane potential [ISS]
- positive regulation of insulin receptor signaling pathway [ISS]
- positive regulation of interleukin-10 secretion [ISS]
- positive regulation of interleukin-13 secretion [ISS]
- positive regulation of interleukin-4 production [ISS]
- positive regulation of interleukin-5 secretion [ISS]
- protein phosphorylation [IDA]
- signal transduction [TAS]
- transforming growth factor beta receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
NUMB
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
aPKC-mediated phosphorylation regulates asymmetric membrane localization of the cell fate determinant Numb.
In Drosophila, the partition defective (Par) complex containing Par3, Par6 and atypical protein kinase C (aPKC) directs the polarized distribution and unequal segregation of the cell fate determinant Numb during asymmetric cell divisions. Unequal segregation of mammalian Numb has also been observed, but the factors involved are unknown. Here, we identify in vivo phosphorylation sites of mammalian Numb and show ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PRKCZ NUMB | Biochemical Activity Biochemical Activity 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. | Low | - | BioGRID | 864182 |
Curated By
- BioGRID