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Protein Page:
FGB (human)

Overview
FGB Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Defects in FGB are a cause of congenital afibrinogenemia (CAFBN). This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold; Cell surface; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 4q28
Cellular Component: cell surface; external side of plasma membrane; extracellular region; extracellular space; fibrinogen complex; plasma membrane
Molecular Function: cell adhesion molecule binding; chaperone binding; protein binding; receptor binding; structural molecule activity
Biological Process: blood coagulation; cell-matrix adhesion; cellular protein complex assembly; extracellular matrix organization and biogenesis; fibrinolysis; induction of bacterial agglutination; plasminogen activation; platelet degranulation; positive regulation of exocytosis; positive regulation of heterotypic cell-cell adhesion; positive regulation of protein secretion; positive regulation of vasoconstriction; protein polymerization; response to calcium ion
Disease: Afibrinogenemia, Congenital; Dysfibrinogenemia, Congenital
Reference #:  P02675 (UniProtKB)
Alt. Names/Synonyms: FGB; FIBB; Fibrinogen beta chain; fibrinogen, B beta polypeptide; fibrinogen, beta chain; Fibrinopeptide B; MGC104327; MGC120405
Gene Symbols: FGB
Molecular weight: 55,928 Da
Basal Isoelectric point: 8.54  Predict pI for various phosphorylation states
Select Structure to View Below

FGB

Protein Structure Not Found.
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