Relation Results

Summary

Name FGA
Full Name Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]
Synonyms FIBA_HUMAN
Primary ID P02671
Links - -
Type protein
Relations 14
Function Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insolu ...
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Type: Score: Layout: SPV 
0.20.20.20.20.7680.70.5770.382MMP13FGAMMP8MMP12MMP14FibrinogenPlatelet_aggregationAIIB/b3 integrinITGAX

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ MMP13down-regulates quantity by destabilization img/direct_inhibition.png cleavage FGA 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263612 Ala20 VVGTAWTaDSGEGDF in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-13 27YVATRDN g-chain| 20ADSGEGD a-chain| 124RNSVDXLNXN b-chain| 442LRTGKEKV a-chain
Identifier Residue Sequence Organism Cell Line
SIGNOR-263613 Leu442 TSKGDKElRTGKEKV in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-13 27YVATRDN g-chain| 20ADSGEGD a-chain| 124RNSVDXLNXN b-chain| 442LRTGKEKV a-chain
Publications: 2 Organism: In Vitro
+ MMP8down-regulates quantity by destabilization img/direct_inhibition.png cleavage FGA 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263625 Ala20 VVGTAWTaDSGEGDF in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-8 20ADSGEGD a-chain | 442LRTGKEKV a-chain
Identifier Residue Sequence Organism Cell Line
SIGNOR-263626 Leu442 TSKGDKElRTGKEKV in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-8 20ADSGEGD a-chain | 442LRTGKEKV a-chain
Publications: 2 Organism: In Vitro
+ MMP12down-regulates quantity by destabilization img/direct_inhibition.png cleavage FGA 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263622 Ala20 VVGTAWTaDSGEGDF in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-12 20ADSGEGD a-chain| 540FVSETESRG a-chain|433LVTSKGDK a-chain
Identifier Residue Sequence Organism Cell Line
SIGNOR-263624 Leu433 REYHTEKlVTSKGDK in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-12 20ADSGEGD a-chain| 540FVSETESRG a-chain|433LVTSKGDK a-chain
Identifier Residue Sequence Organism Cell Line
SIGNOR-263623 Phe540 FSPMLGEfVSETESR in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system. |Fibrinogen was subjected to MMP-cleavage, and the resulting fragments were isolated. The amino acid sequences were determined by automated Edman degradation.|MMP-12 20ADSGEGD a-chain| 540FVSETESRG a-chain|433LVTSKGDK a-chain
Publications: 3 Organism: In Vitro
+ MMP14down-regulates quantity by destabilization img/direct_inhibition.png cleavage FGA 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263619 Leu105 NNKDSHSlTTNIMEI in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain
Identifier Residue Sequence Organism Cell Line
SIGNOR-263620 Leu433 REYHTEKlVTSKGDK in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain
Identifier Residue Sequence Organism Cell Line
SIGNOR-263621 Phe117 MEILRGDfSSANNRD in vitro
pmid sentence
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-14 27YVATRDN g-chain| 105XDAATLKSR g-chain | 92LTYNPDES g-chain |105LTTNIXEXL a-chain|433LVTSKGDKE a-chain| 117FXSANNRD a-chain
Publications: 3 Organism: In Vitro
+ FGAform complex img/form-complex.png binding Fibrinogen 0.768
Identifier Residue Sequence Organism Cell Line
SIGNOR-263392 in vitro
pmid sentence
Fibrinogen is a plasma glycoprotein mainly synthesised by hepatocytes and circulating as a 340-kDa hexamer consisting of two sets of three different polypeptide chains (Aalpha, Bbeta, and gamma, encoded by the FGA, FGB, and FGG gene, respectively).
Publications: 1 Organism: In Vitro
+ FGAup-regulates img/indirect-activation.png Platelet_aggregation 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-253372
pmid sentence
In response to agonist stimulation, the αIIbβ3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation.
Publications: 1
+ AIIB/b3 integrinup-regulates activity img/direct-activation.png binding FGA 0.577
Identifier Residue Sequence Organism Cell Line
SIGNOR-253359 Homo sapiens Blood Platelet
pmid sentence
In response to agonist stimulation, the αIIbβ3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation.
Publications: 1 Organism: Homo Sapiens
+ FGAup-regulates img/direct-activation.png binding ITGAX 0.382
Identifier Residue Sequence Organism Cell Line
SIGNOR-31320 Homo sapiens
pmid sentence
To map the binding sites for four distinct ligands for mac-l: ic3b, fibrinogen, icam-1. __the i domain on the ot chain of mac-1 is an important recognition site for all four ligands.
Publications: 1 Organism: Homo Sapiens
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