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CAV1 — F2R

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: Complex of CAV1-CSK → F2R (increases, CAV1/CSK Activity) Lu et al., Cell Signal 2006*
  Evidence: These results indicated that phosphocaveolin-1 was associated with the SH2 domain of Csk in response to PAR1 activation.

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: F2R — CAV1 (colocalization, biochemical) Banfi et al., Journal of thrombosis and haemostasis : JTH 2007*
• IRef Biogrid Interaction: F2R — CAV1 (physical association, affinity chromatography technology) Banfi et al., Journal of thrombosis and haemostasis : JTH 2007*
• IRef Biogrid Interaction: F2R — CAV1 (physical association, affinity chromatography technology) Bae et al., J Biol Chem 2010*
• IRef Intact Interaction: CAV1 — F2R (association, anti bait coimmunoprecipitation) Bae et al., J Biol Chem 2010*
• IRef Intact Interaction: Complex of F2R-CAV1-PROCR-CAV1-F2R-PROCR-PROCR-CAV1-F2R (association, anti bait coimmunoprecipitation) Bae et al., J Biol Chem 2010*

Text-mined interactions from Literome

Lu et al., Cell Signal 2006 : Of interest, activation of PAR1 resulted in the phosphorylation of caveolin-1 , a principal component of caveolae, on tyrosine 14 by a Gi-linked Src kinase pathway and p38 mitogen activated protein kinase
Banfi et al., Journal of thrombosis and haemostasis : JTH 2007 : In addition, siRNA directed against caveolin-1 inhibited TF activation by PAR1 ( P < 0.01 and P < 0.01, respectively )