FGB

Gene Information
 
Gene Symbol
FGB
 
Aliases
HEL-S-78p
 
Entrez Gene ID
 
Gene Name
Fibrinogen beta chain
 
Chromosomal Location
4q31.3
 
HGNC ID
 
Summary
The protein encoded by this gene is the beta component of fibrinogen, a blood-borne glycoprotein comprised 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. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2014]
 
RefSeq DNA
 
RefSeq mRNA
  e!Ensembl
Gene
Transcript  
Protein

Gene Ontology (GO)

GO ID Ontology Function Evidence Reference
GO:0007160 Biological process Cell-matrix adhesion IDA 10903502
GO:0031639 Biological process Plasminogen activation IDA 16846481
GO:0034116 Biological process Positive regulation of heterotypic cell-cell adhesion IDA 8100742
GO:0034622 Biological process Cellular protein-containing complex assembly IDA 8910396
GO:0042730 Biological process Fibrinolysis IDA 16846481
Protein Information
 
Protein Name
Fibrinogen beta chain, beta-fibrinogen, epididymis secretory sperm binding protein Li 78p, fibrinogen, B beta polypeptide
 
Function
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.
 
Refseq Proteins
 
UniProt
 
PDB
 
Pfam
Pfam Accession Pfam ID
PF08702 Fib_alpha
PF00147 Fibrinogen_C
Pathways
 
KEGG
 
Reactome
 

Complement and coagulation cascades
Platelet activation

 

Platelet degranulation
Common Pathway of Fibrin Clot Formation
Integrin cell surface interactions
Integrin signaling
GRB2:SOS provides linkage to MAPK signaling for Integrins
p130Cas linkage to MAPK signaling for integrins
MAP2K and MAPK activation
Regulation of TLR by endogenous ligand
Signaling by moderate kinase activity BRAF mutants
Signaling by high-kinase activity BRAF mutants
Signaling by BRAF and RAF fusions
Paradoxical activation of RAF signaling by kinase inactive BRAF
Signaling downstream of RAS mutants

Interactions
 
STRING MINT IntAct
ENSP00000368880 Q12778 Q12778
    View interactions
     

Associated Diseases

Disease groupDisease NameReferences
Blood Disorders
Dysfibrinogenemia
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Fibrinogen Deficiency
Dysfibrinogenemia
Endocrine System Diseases
PCOS
Musculoskeletal Diseases
Osteoporosis
References
 

Overlap of proteomics biomarkers between women with pre-eclampsia and PCOS: a systematic review and biomarker database integration.

Khan Gulafshana Hafeez, Galazis Nicolas, Docheva Nikolina, Layfield Robert, Atiomo William
Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK gulafshanahafeez@hotmail.com.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK.| School of Life Sciences, University of Nottingham, Nottingham, UK.| Division of Human Development, School of Clinical Sciences, University of Nottingham, Queen's Medical Centre, D Floor, East Block, Nottingham, UK.
Hum Reprod. 2015 Jan;30(1):133-48. doi: 10.1093/humrep/deu268. Epub 2014 Oct 28.

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