L1CAM
Gene Ontology Biological Process
Gene Ontology Cellular Component
ITGAV
Gene Ontology Biological Process
- ERK1 and ERK2 cascade [ISS]
- angiogenesis [IEP]
- antigen processing and presentation of exogenous peptide antigen via MHC class I [TAS]
- antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [TAS]
- antigen processing and presentation of peptide antigen via MHC class I [TAS]
- apolipoprotein A-I-mediated signaling pathway [IMP]
- axon guidance [TAS]
- blood coagulation [TAS]
- calcium ion transmembrane transport [IDA]
- cell adhesion [IDA]
- cell growth [IMP]
- cell migration [IMP]
- cell-matrix adhesion [IDA, IMP, NAS]
- cell-substrate adhesion [IMP]
- endodermal cell differentiation [IMP]
- entry of symbiont into host cell by promotion of host phagocytosis [NAS]
- extracellular matrix organization [TAS]
- extrinsic apoptotic signaling pathway in absence of ligand [ISS]
- heterotypic cell-cell adhesion [IMP]
- integrin-mediated signaling pathway [NAS]
- leukocyte migration [TAS]
- negative chemotaxis [IMP]
- negative regulation of entry of bacterium into host cell [IDA]
- negative regulation of extrinsic apoptotic signaling pathway [IMP]
- negative regulation of lipid storage [IMP]
- negative regulation of lipid transport [IMP]
- negative regulation of lipoprotein metabolic process [IMP]
- negative regulation of low-density lipoprotein particle receptor biosynthetic process [IMP]
- negative regulation of macrophage derived foam cell differentiation [IMP]
- positive regulation of cell adhesion [IDA]
- positive regulation of cell proliferation [IDA]
- regulation of apoptotic cell clearance [ISS]
- regulation of phagocytosis [IDA]
- substrate adhesion-dependent cell spreading [IDA]
- viral entry into host cell [IMP, TAS]
Gene Ontology Molecular Function- extracellular matrix binding [IDA]
- extracellular matrix protein binding [IDA]
- fibronectin binding [IDA]
- insulin-like growth factor I binding [IDA]
- opsonin binding [ISS]
- protease binding [IDA]
- protein binding [IPI]
- protein kinase C binding [ISS]
- transforming growth factor beta binding [ISS]
- voltage-gated calcium channel activity [IDA]
- extracellular matrix binding [IDA]
- extracellular matrix protein binding [IDA]
- fibronectin binding [IDA]
- insulin-like growth factor I binding [IDA]
- opsonin binding [ISS]
- protease binding [IDA]
- protein binding [IPI]
- protein kinase C binding [ISS]
- transforming growth factor beta binding [ISS]
- voltage-gated calcium channel activity [IDA]
Gene Ontology Cellular Component
- alphav-beta3 integrin-IGF-1-IGF1R complex [IDA]
- cell surface [IDA, ISS]
- extracellular vesicular exosome [IDA]
- filopodium membrane [IDA]
- focal adhesion [IDA]
- integral component of plasma membrane [NAS]
- integrin alphav-beta3 complex [IDA]
- integrin alphav-beta5 complex [IDA]
- integrin alphav-beta8 complex [IDA]
- integrin complex [IDA, NAS]
- lamellipodium membrane [IDA]
- membrane [ISS]
- microvillus membrane [IDA]
- phagocytic vesicle [TAS]
- plasma membrane [IDA, TAS]
- ruffle membrane [IDA]
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
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]
Throughput
- Low Throughput
Curated By
- BioGRID