Aliases for FN1 Gene
External Ids for FN1 Gene
Previous GeneCards Identifiers for FN1 Gene
This gene encodes fibronectin, a glycoprotein present in a soluble dimeric form in plasma, and in a dimeric or multimeric form at the cell surface and in extracellular matrix. The encoded preproprotein is proteolytically processed to generate the mature protein. Fibronectin is involved in cell adhesion and migration processes including embryogenesis, wound healing, blood coagulation, host defense, and metastasis. The gene has three regions subject to alternative splicing, with the potential to produce 20 different transcript variants, at least one of which encodes an isoform that undergoes proteolytic processing. The full-length nature of some variants has not been determined. [provided by RefSeq, Jan 2016]
GeneCards Summary for FN1 Gene
FN1 (Fibronectin 1) is a Protein Coding gene. Diseases associated with FN1 include Glomerulopathy With Fibronectin Deposits 2 and Spondylometaphyseal Dysplasia, Corner Fracture Type. Among its related pathways are ERK Signaling and Simplified Interaction Map Between LOXL4 and Oxidative Stress Pathway. Gene Ontology (GO) annotations related to this gene include heparin binding and protease binding. An important paralog of this gene is TNC.
UniProtKB/Swiss-Prot for FN1 Gene
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.
Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.