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Protein Page:
FGB (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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; Secreted, signal peptide; Secreted; Cell surface
Cellular Component: extracellular space; cell surface; fibrinogen complex; extracellular region; plasma membrane; cell cortex; external side of plasma membrane
Molecular Function: protein binding, bridging; protein binding; chaperone binding; receptor binding
Biological Process: protein polymerization; platelet activation; extracellular matrix organization and biogenesis; platelet degranulation; response to calcium ion; blood coagulation; signal transduction
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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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 R53 HRPLDKKREEAPsLR
0 1 S58-p KKREEAPsLRPAPPP
0 4 Y71-p PPISGGGyRARPAKA
1 1 Y182-p ELEKHQLyIDETVNS
0 1 K247 ECEEIIRKGGETSEM
0 1 K264 IQPDSSVKPyRVYCD
0 4 Y266-p PDSSVKPyRVYCDMN
0 1 N273 yRVYCDMNTENGGWT
0 4 K313-a VATNTDGkNYCGLPG
0 1 K313 VATNTDGKNYCGLPG
0 2 T338-p QLTRMGPtELLIEME
0 2 K348-a LIEMEDWkGDKVKAH
0 1 K353 DWkGDKVKAHyGGFT
0 2 Y356-p GDKVKAHyGGFTVQN
0 2 Y368-p VQNEANKyQISVNKY
0 1 K374 KyQISVNKYRGTAGN
0 1 Y408-p NGMFFSTyDRDNDGW
0 1 K426 DPRKQCSKEDGGGWW
0 5 K471-a GVVWMNWkGSWYSMR
  mouse

 
K43-u HRPVDRRkEEPPSLR
S48 RRkEEPPSLRPAPPP
Y61 PPISGGGYRARPAKA
Y172 ILEDQRLYIDETVND
K237-u ECEEIIRkGGETSEM
K254-u IQPDTSIkPYRVYCD
Y256 PDTSIkPYRVYCDMk
K263-u YRVYCDMkTENGGWT
K303-a IATNEDAkKYCGLPG
K303-u IATNEDAkKYCGLPG
T328 QLTRMGPTELLIEME
K338 LIEMEDWKGDKVkAH
K343-u DWKGDKVkAHYGGFT
Y346 GDKVkAHYGGFTVQN
Y358 VQNEASKYQVSVNkY
K364-u KYQVSVNkYKGTAGN
Y398 NGMFFSTYDRDNDGW
K416-u DPRKQCSkEDGGGWW
K461 GVVWMNWKGSWYSMR
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