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	OMIM: 134830; MGI: 99501; HomoloGene: 3772; GeneCards: FGB; OMA: FGB - orthologs
Gene location ( Human)
Chr.	Chromosome 4 (human)
End	154,571,086 bp
Gene location ( Mouse)
Chr.	Chromosome 3 (mouse)
End	82,957,170 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; beta cell; ; gonad; ; human kidney; ; kidney tubule; ; testicle; ; metanephric glomerulus; ; epithelium of colon; ; decidua; ; body of stomach;
	Top expressed in
	left lobe of liver; ; human fetus; ; yolk sac; ; fetal liver hematopoietic progenitor cell; ; gallbladder; ; abdominal wall; ; sexually immature organism; ; primitive streak; ; embryo; ; semi-lunar valve;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	protein-macromolecule adaptor activity; chaperone binding; structural molecule activity; protein binding; signaling receptor binding; cell adhesion molecule binding; extracellular matrix structural constituent;
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; endoplasmic reticulum; synapse; collagen-containing extracellular matrix;
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; 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
Orthologs
	2244
	110135
	ENSG00000171564
	ENSMUSG00000033831
	P02675
	Q8K0E8
	NM_001184741; NM_005141
	NM_181849
NP_001171670; NP_005132; NP_001369688; NP_001369689; NP_001369690;
	NP_001369691; NP_001369692; NP_001369693; NP_001369694
	NP_862897
	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.^[5]

Interactions

Fibrinogen beta chain has been shown to interact with Lipoprotein(a).^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000171564 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000033831 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: FGB fibrinogen beta chain".
^ Klose R, Fresser F, Kochl S, Parson W, Kapetanopoulos A, Fruchart-Najib J, Baier G, Utermann G (December 2000). "Mapping of a minimal apolipoprotein(a) interaction motif conserved in fibrin(ogen) beta - and gamma -chains". J. Biol. Chem. 275 (49). UNITED STATES: 38206–12. doi: 10.1074/jbc.M003640200. ISSN 0021-9258. PMID 10980194.

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Vasse M, Paysant J, Soria J, et al. (1997). "Regulation of fibrinogen biosynthesis by cytokines, consequences on the vascular risk". Haemostasis. 26 Suppl 4 (4): 331–9. doi: 10.1159/000217313. PMID 8979138.
Herrick S, Blanc-Brude O, Gray A, Laurent G (1999). "Fibrinogen". Int. J. Biochem. Cell Biol. 31 (7): 741–6. doi: 10.1016/S1357-2725(99)00032-1. PMID 10467729.
Redman CM, Xia H (2001). "Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion". Ann. N. Y. Acad. Sci. 936 (1): 480–95. Bibcode: 2001NYASA.936..480R. doi: 10.1111/j.1749-6632.2001.tb03535.x. PMID 11460506. S2CID 31741202.
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Tarakhovskiĭ IuS, Galushchenko IV, Boroviagin VL, et al. (1979). "[Temperature-dependent changes in the profile of the sarcoplasmic reticulum membrane hydrophobic zones]". Biokhimiia. 44 (5): 897–902. PMID 156564.
Watt KW, Takagi T, Doolittle RF (1979). "Amino acid sequence of the beta chain of human fibrinogen". Biochemistry. 18 (1): 68–76. doi: 10.1021/bi00568a011. PMID 420779.
Gårdlund B, Hessel B, Marguerie G, et al. (1977). "Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments". Eur. J. Biochem. 77 (3): 595–610. doi: 10.1111/j.1432-1033.1977.tb11704.x. PMID 891553.
Blombäck B, Hessel B, Hogg D (1976). "Disulfide bridges in nh2 -terminal part of human fibrinogen". Thromb. Res. 8 (5): 639–58. doi: 10.1016/0049-3848(76)90245-0. PMID 936108.
Koopman J, Haverkate F, Grimbergen J, et al. (1992). "Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes". Proc. Natl. Acad. Sci. U.S.A. 89 (8): 3478–82. Bibcode: 1992PNAS...89.3478K. doi: 10.1073/pnas.89.8.3478. PMC 48891. PMID 1565641.
Koopman J, Haverkate F, Lord ST, et al. (1992). "Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala----Thr". J. Clin. Invest. 90 (1): 238–44. doi: 10.1172/JCI115841. PMC 443086. PMID 1634610.
Wu C, Chung AE (1991). "Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen A alpha and B beta chains". J. Biol. Chem. 266 (28): 18802–7. doi: 10.1016/S0021-9258(18)55134-6. PMID 1680863.
Yoshida N, Wada H, Morita K, et al. (1991). "A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine". Blood. 77 (9): 1958–63. doi: 10.1182/blood.V77.9.1958.1958. PMID 2018836.
Chung DW, Harris JE, Davie EW (1991). "Nucleotide Sequences of the Three Genes Coding for Human Fibrinogen". Fibrinogen, Thrombosis, Coagulation, and Fibrinolysis. Advances in Experimental Medicine and Biology. Vol. 281. pp. 39–48. doi: 10.1007/978-1-4615-3806-6_3. ISBN 978-1-4613-6697-3. PMID 2102623.
Danishefsky K, Hartwig R, Banerjee D, Redman C (1990). "Intracellular fate of fibrinogen B beta chain expressed in COS cells". Biochim. Biophys. Acta. 1048 (2–3): 202–8. doi: 10.1016/0167-4781(90)90057-9. PMID 2322576.
Berg K, Kierulf P (1989). "DNA polymorphisms at fibrinogen loci and plasma fibrinogen concentration". Clin. Genet. 36 (4): 229–35. doi: 10.1111/j.1399-0004.1989.tb03195.x. PMID 2572363. S2CID 35604138.