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
YWHAZ
Gene Ontology Biological Process
- Golgi reassembly [IMP]
- RNA metabolic process [TAS]
- apoptotic process [TAS]
- blood coagulation [TAS]
- establishment of Golgi localization [IMP]
- gene expression [TAS]
- intrinsic apoptotic signaling pathway [TAS]
- mRNA metabolic process [TAS]
- membrane organization [TAS]
- negative regulation of apoptotic process [TAS]
- platelet activation [TAS]
- positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway [TAS]
- signal transduction [TAS]
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
14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylation.
14-3-3 Proteins may function as adapters or scaffold in signal-transduction pathways. We found previously that protein kinase C-zeta (PKC-zeta) can phosphorylate and activate Raf-1 in a signalling complex [van Dijk, Hilkmann and van Blitterswijk (1997) Biochem. J. 325, 303-307]. We report now that PKC-zeta-Raf-1 interaction is mediated by 14-3-3 proteins in vitro and in vivo. Co-immunoprecipitation experiments in COS cells ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PRKCZ YWHAZ | Affinity Capture-MS Affinity Capture-MS 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 is identified by mass spectrometric methods. | High | - | BioGRID | - | |
| YWHAZ PRKCZ | Reconstituted Complex 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. | Low | - | BioGRID | - |
Curated By
- BioGRID