Fibrinogen beta chain

FGB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1FZA, 1FZB, 1FZC, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 2A45, 2FFD, 2H43, 2HLO, 2HOD, 2HPC, 2OYH, 2OYI, 2Q9I, 2XNX, 2XNY, 2Z4E, 3BVH, 3E1I, 3GHG, 3H32, 3HUS
Identifiers
Aliases	FGB, HEL-S-78p, fibrinogen beta chain
External IDs	MGI: 99501 HomoloGene: 3772 GeneCards: FGB
Gene ontology Molecular function • protein binding, bridging • chaperone binding • structural molecule activity • protein binding • receptor binding • cell adhesion molecule binding Cellular component • cytoplasm • platelet alpha granule • extracellular vesicle • blood microparticle • plasma membrane • fibrinogen complex • extracellular region • cell surface • cell cortex • extracellular exosome • platelet alpha granule lumen • external side of plasma membrane • extracellular space Biological process • hemostasis • negative regulation of endothelial cell apoptotic process • positive regulation of peptide hormone secretion • protein polymerization • positive regulation of heterotypic cell-cell adhesion • adaptive immune response • fibrinolysis • immune system process • platelet degranulation • blood coagulation • cellular protein complex assembly • extracellular matrix organization • cellular response to leptin stimulus • response to calcium ion • positive regulation of substrate adhesion-dependent cell spreading • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors • positive regulation of vasoconstriction • cellular response to interleukin-1 • positive regulation of protein secretion • positive regulation of ERK1 and ERK2 cascade • positive regulation of exocytosis • blood coagulation, fibrin clot formation • plasminogen activation • innate immune response • cell-matrix adhesion • platelet aggregation • signal transduction • induction of bacterial agglutination • platelet activation • toll-like receptor signaling pathway Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2244	110135
Ensembl	ENSG00000171564	ENSMUSG00000033831
UniProt	P02675	Q8K0E8
RefSeq (mRNA)	NM_001184741 NM_005141	NM_181849
RefSeq (protein)	NP_001171670 NP_005132	NP_862897
Location (UCSC)	Chr 4: 154.56 – 154.57 Mb	Chr 3: 83.04 – 83.05 Mb
PubMed search	[1]	[2]
Wikidata
View/Edit Human View/Edit Mouse

Fibrinogen beta chain, also known as FGB, is a gene found in humans and most other vertebrates with a similar system of blood coagulation.

The protein encoded by this gene is the beta component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.^[3]

Interactions

Fibrinogen beta chain has been shown to interact with Lipoprotein(a).^[4]

See also

• Fibrin

References

Further reading

PDB gallery

1fza: CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D  1fzb: CRYSTAL STRUCTURE OF CROSSLINKED FRAGMENT D  1fzc: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH TWO DIFFERENT BOUND LIGANDS  1fze: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN  1fzf: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE  1fzg: CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE  1lt9: Crystal Structure of Recombinant Human Fibrinogen Fragment D  1ltj: Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands Gly-Pro-Arg-Pro-Amide and Gly-His-Arg-Pro-Amide  1n86: Crystal structure of human D-dimer from cross-linked fibrin complexed with GPR and GHRPLDK peptide ligands.  1n8e: Fragment Double-D from Human Fibrin  1re3: Crystal Structure of Fragment D of BbetaD398A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide  1re4: Crystal Structure of Fragment D of BbetaD398A Fibrinogen  1rf0: Crystal Structure of Fragment D of gammaE132A Fibrinogen  1rf1: Crystal Structure of Fragment D of gammaE132A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-amide  2a45: Crystal structure of the complex between thrombin and the central ""E"" region of fibrin  2ffd: Fibrinogen Fragment D with ""A"" knob peptide mimic GPRVVE  2h43: Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide  2hod: Crystal Structure of Fragment D from Human Fibrinogen Complexed with Gly-hydroxyPro-Arg-Pro-amide  2hpc: Crystal structure of fragment D from Human Fibrinogen Complexed with Gly-Pro-Arg-Pro-amide.  2oyh: Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide  2oyi: Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-Pro-Arg-Pro-Amide