PPP2R4
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- mitotic spindle organization in nucleus [IBA]
- negative regulation of phosphoprotein phosphatase activity [IDA]
- negative regulation of protein dephosphorylation [IDA]
- positive regulation of apoptotic process [IDA]
- positive regulation of phosphoprotein phosphatase activity [IDA]
- positive regulation of protein dephosphorylation [IDA]
- protein peptidyl-prolyl isomerization [IBA]
- regulation of phosphoprotein phosphatase activity [IDA]
Gene Ontology Molecular Function- ATP binding [IDA]
- ATPase activity [IDA]
- peptidyl-prolyl cis-trans isomerase activity [IBA]
- protein heterodimerization activity [TAS]
- protein homodimerization activity [IDA]
- protein phosphatase 2A binding [IDA]
- protein phosphatase type 2A regulator activity [IDA, TAS]
- protein tyrosine phosphatase activator activity [IDA]
- receptor binding [IPI]
- ATP binding [IDA]
- ATPase activity [IDA]
- peptidyl-prolyl cis-trans isomerase activity [IBA]
- protein heterodimerization activity [TAS]
- protein homodimerization activity [IDA]
- protein phosphatase 2A binding [IDA]
- protein phosphatase type 2A regulator activity [IDA, TAS]
- protein tyrosine phosphatase activator activity [IDA]
- receptor binding [IPI]
Gene Ontology Cellular Component
MAPT
Gene Ontology Biological Process
- apoptotic process [TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- generation of neurons [NAS]
- microtubule cytoskeleton organization [IDA]
- positive regulation of axon extension [IDA]
- positive regulation of microtubule polymerization [IDA]
- regulation of autophagy [IGI]
- regulation of microtubule polymerization [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PCA
A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.
Publication
?-Aminobutyric acid type A (GABAA) receptor activation modulates tau phosphorylation.
Abnormal phosphorylation and aggregation of the microtubule-associated protein Tau are hallmarks of various neurodegenerative diseases, such as Alzheimer disease. Molecular mechanisms that regulate Tau phosphorylation are complex and currently incompletely understood. We have developed a novel live cell reporter system based on protein-fragment complementation assay to study dynamic changes in Tau phosphorylation status. In this assay, fusion proteins of Tau ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PPP2R4 MAPT | 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 | 823359 | |
| PPP2R4 MAPT | 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 | 2618418 |
Curated By
- BioGRID