UniProtKB/Swiss-Prot PTM Description

Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways

Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers

Glycosylation Sites

Position Structures Description Evidence
Associated Structures: 6 global GlycoSuite
Position Structures Description Evidence
Associated Structures: 4 global GlycoSuite
Site-Specific Information

A number of glycan structures have been assigned to specific glycosylation sites

Position Structures Description Evidence
ASN-394 Associated Structures: 4 Site specific GlycoSuite

Glycan Structures


Accompanying information

Structure Format

CFG/Essentials Text Oxford



References 1

  1. Carbohydrate structure of human fibrinogen. Use of 300-MHz 1H-NMR to characterize glycosidase-treated glycopeptides.

    Townsend RR, Hilliker E, Li Y-T, Laine RA, Bell WR, Lee YC

    PubMed: 7107587 Year: 1982