BAIT
L1CAM
CAML1, CD171, HSAS, HSAS1, MASA, MIC5, N-CAM-L1, N-CAML1, NCAM-L1, S10, SPG1
L1 cell adhesion molecule
GO Process (6)
GO Function (0)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Cellular Component
Homo sapiens
PREY
ITGA5
CD49e, FNRA, VLA5A
integrin, alpha 5 (fibronectin receptor, alpha polypeptide)
GO Process (13)
GO Function (3)
GO Component (7)
Gene Ontology Biological Process
- angiogenesis [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell adhesion [TAS]
- cell-substrate adhesion [IMP]
- endodermal cell differentiation [IMP]
- extracellular matrix organization [TAS]
- heterotypic cell-cell adhesion [IMP]
- leukocyte migration [TAS]
- negative regulation of anoikis [IMP]
- positive regulation of peptidyl-tyrosine phosphorylation [IMP]
- positive regulation of vascular endothelial growth factor receptor signaling pathway [TAS]
- wound healing, spreading of epidermal cells [IEP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Plasmin-sensitive dibasic sequences in the third fibronectin-like domain of L1-cell adhesion molecule (CAM) facilitate homomultimerization and concomitant integrin recruitment.
L1 is a multidomain transmembrane neural recognition molecule essential for neurohistogenesis. While moieties in the immunoglobulin-like domains of L1 have been implicated in both heterophilic and homophilic binding, the function of the fibronectin (FN)-like repeats remains largely unresolved. Here, we demonstrate that the third FN-like repeat of L1 (FN3) spontaneously homomultimerizes to form trimeric and higher order complexes. Remarkably, these ... [more]
J. Cell Biol. Jun. 26, 2000; 149(7);1485-502 [Pubmed: 10871287]
Throughput
- Low Throughput
Curated By
- BioGRID