PRKG1
Gene Ontology Biological Process
- cGMP-mediated signaling [IMP]
- cell growth involved in cardiac muscle cell development [ISO]
- dendrite development [IMP]
- forebrain development [IMP]
- negative regulation of glutamate secretion [ISO]
- negative regulation of heart contraction [ISO]
- negative regulation of inositol phosphate biosynthetic process [ISO]
- negative regulation of platelet aggregation [ISO]
- negative regulation of smooth muscle cell migration [ISO]
- negative regulation of smooth muscle contraction [IMP]
- neuron migration [IMP]
- positive regulation of circadian rhythm [ISO]
- positive regulation of cytosolic calcium ion concentration [ISO]
- positive regulation of large conductance calcium-activated potassium channel activity [ISO]
- positive regulation of vasodilation [ISO]
- protein phosphorylation [IDA, ISO]
- regulation of GTPase activity [ISO]
- regulation of testosterone biosynthetic process [ISO]
- relaxation of vascular smooth muscle [IMP]
- signal transduction [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
LASP1
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 mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase.
LIM and SH3 domain protein (LASP-1) is a specific focal adhesion protein involved in cell migration. Overlay studies demonstrate that LASP-1 directly binds to the proline-rich domains of zyxin, lipoma preferred partner (LPP), and vasodilator-stimulated phosphoprotein (VASP), with zyxin being the most prominent interacting partner. Despite the LIM/zinc-finger domain, hypothesized to be involved in homodimerization, LASP-1 exists as a monomer. ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID