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Protein Page:
FGG (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
FGG Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Defects in FGG 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. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted
Cellular Component: extracellular space; cell surface; fibrinogen complex; extracellular region; plasma membrane; cell cortex; external side of plasma membrane
Molecular Function: protein binding, bridging; metal ion binding; cell adhesion molecule binding; structural molecule activity; receptor binding
Biological Process: protein polymerization; platelet activation; extracellular matrix organization and biogenesis; positive regulation of heterotypic cell-cell adhesion; cell-matrix adhesion; signal transduction; cellular protein complex assembly; platelet degranulation; positive regulation of protein secretion; positive regulation of vasoconstriction; response to calcium ion; blood coagulation; positive regulation of exocytosis
Reference #:  P02679 (UniProtKB)
Alt. Names/Synonyms: FGG; FIBG; Fibrinogen gamma chain; fibrinogen, gamma chain; fibrinogen, gamma polypeptide
Gene Symbols: FGG
Molecular weight: 51,512 Da
Basal Isoelectric point: 5.37  Predict pI for various phosphorylation states
Select Structure to View Below

FGG

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 K84 ENKTSEVKQLIKAIQ
0 1 K101 YNPDESSKPNMIDAA
0 17 Y140-p IRYLQEIyNSNNQKI
0 1 K146 IyNSNNQKIVNLKEK
0 1 K185 DCQDIANKGAKQSGL
0 8 K231-a LDGSVDFkKNWIQYK
0 1 K232 DGSVDFkKNWIQYKE
0 3 Y288-p GRTSTADyAMFKVGP
0 12 Y300-p VGPEADKyRLTYAYF
0 14 Y374-p AGHLNGVyyQGGtyS
0 3 Y375-p GHLNGVyyQGGtySK
0 2 T379-p GVyyQGGtySKASTP
0 4 Y380-p VyyQGGtySKASTPN
  mouse

 
K83-u ENRTTEAkELIKAIQ
K100-u YNPDQPPkPGMIDSA
Y139 IRYLQEIYNSNNQkI
K145-u IYNSNNQkITNLKQK
K184-u DCQEIANkGAKESGL
K230 IDGSLDFKkNWIQYK
K231-u DGSLDFKkNWIQYKE
Y287 GRTSTADYAMFRVGP
Y299 VGPESDKYRLTYAYF
Y373 AGHLNGVYHQGGTYS
H374 GHLNGVYHQGGTYSK
T378 GVYHQGGTYSKSSTT
Y379 VYHQGGTYSKSSTTN
  rat

 
K84 ENRTTEAKELIKAIQ
K101 YNPDQPPKPGMIEGA
Y140 IRYLQDIYTSNKQKI
K146 IYTSNKQKITNLKQK
K185 DCQDIANKGAKESGL
K231 LDGSVDFKKNWIQYK
K232 DGSVDFKKNWIQYKE
Y288 GRTSTADYAMFRVGP
Y300 VGPESDKYRLTYAYF
Y374 AGHLNGVYYQGGTYS
Y375 GHLNGVYYQGGTYSK
T379 GVYYQGGTYSKSSTP
Y380 VYYQGGTYSKSSTPN
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