BAIT

PRKACA

PKCD, Pkaca
protein kinase, cAMP dependent, catalytic, alpha
GO Process (20)
GO Function (10)
GO Component (16)
Mus musculus

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.

Keicher C, Gambaryan S, Schulze E, Marcus K, Meyer HE, Butt E

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]

Biochem. Biophys. Res. Commun. Nov. 05, 2004; 324(1);308-16 [Pubmed: 15465019]

Throughput

  • Low Throughput

Curated By

  • BioGRID