PPM1A
Gene Ontology Biological Process
- N-terminal protein myristoylation [ISS]
- Wnt signaling pathway [IDA]
- cell cycle arrest [TAS]
- dephosphorylation [IDA]
- gene expression [TAS]
- insulin receptor signaling pathway [TAS]
- negative regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- negative regulation of NF-kappaB import into nucleus [IMP]
- negative regulation of SMAD protein complex assembly [IDA]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- negative regulation of transforming growth factor beta receptor signaling pathway [IDA]
- peptidyl-threonine dephosphorylation [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP]
- positive regulation of Wnt signaling pathway [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- protein dephosphorylation [IMP]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription, DNA-templated [TAS]
- transforming growth factor beta receptor signaling pathway [TAS]
Gene Ontology Molecular Function
CDC42BPB
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Dephosphorylation)
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
PAK is regulated by PI3K, PIX, CDC42, and PP2Calpha and mediates focal adhesion turnover in the hyperosmotic stress-induced p38 pathway.
Fractionation of brain extracts and functional biochemical assays identified PP2Calpha, a serine/threonine phosphatase, as the major biochemical activity inhibiting PAK1. PP2Calpha dephosphorylated PAK1 and p38, both of which were activated upon hyperosmotic shock with the same kinetics. In comparison to growth factors, hyperosmolality was a more potent activator of PAK1. Therefore we characterize the PAK signaling pathway in the hyperosmotic ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID