CSNK2A1
Gene Ontology Biological Process
- axon guidance [TAS]
- chaperone-mediated protein folding [TAS]
- mitotic cell cycle [TAS]
- mitotic spindle checkpoint [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- positive regulation of Wnt signaling pathway [IMP]
- positive regulation of cell growth [IDA]
- positive regulation of cell proliferation [IDA]
- positive regulation of protein catabolic process [IDA]
- protein phosphorylation [IDA]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HSPA4
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
C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances.
Heat shock proteins Hsp90 and Hsp70 facilitate protein folding but can also direct proteins for ubiquitin-mediated degradation. The mechanisms regulating these opposite activities involve Hsp binding to co-chaperones including CHIP and HOP at their C-termini. We demonstrated that the extreme C-termini of Hsp70 and Hsp90 contain phosphorylation sites targeted by kinases including CK1, CK2 and GSK3-β in vitro. The phosphorylation ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID