BAIT
LASP1
AA408629, Def-4, SH3P6, Tg(Col1a1-lacZ)1Ngma, RP23-386E10.6
LIM and SH3 protein 1
GO Process (2)
GO Function (3)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
PREY
ZYX
9530098H06Rik, R75157
zyxin
GO Process (4)
GO Function (2)
GO Component (5)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
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]
Biochem. Biophys. Res. Commun. Nov. 05, 2004; 324(1);308-16 [Pubmed: 15465019]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| LASP1 ZYX | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 0.8475 | BioGRID | 2677224 |
Curated By
- BioGRID