LATS1
Gene Ontology Biological Process
- G2/M transition of mitotic cell cycle [IDA]
- cytoplasmic sequestering of protein [IMP]
- hippo signaling [IDA, TAS]
- hormone-mediated signaling pathway [ISS]
- negative regulation of canonical Wnt signaling pathway [IMP]
- negative regulation of cyclin-dependent protein serine/threonine kinase activity [IDA]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- protein phosphorylation [IDA]
- regulation of actin filament polymerization [IDA]
- regulation of protein complex assembly [IMP]
- sister chromatid segregation [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
KIF23
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
Phosphorylation of CHO1 by Lats1/2 regulates the centrosomal activation of LIMK1 during cytokinesis.
Large tumor suppressor 1 and 2 (Lats1/2) regulate centrosomal integrity, chromosome segregation and cytokinesis. As components of the centralspindlin complex, the kinesin-like protein CHO1 and its splicing variant MKLP1 colocalize with chromosome passenger proteins and GTPases and regulate the formation of the contractile ring and cytokinesis; however, the regulatory mechanisms of CHO1/MKLP1 remain elusive. Here, we show that Lats1/2 phosphorylate ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID