| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.59503087 |
| These results suggest that GAP can transiently interact with the insulin receptor after insulin treatment , and this interaction is arrested after PAO pretreatment . . 0.59503087^^^ However , after insulin treatment in the presence of the phosphotyrosine phosphatase inhibitor phenylarsine oxide ( PAO ) , 5 10 % of GAP was found to be associated with the insulin receptor , and , in addition , a fraction of total GAP was phosphorylated on tyrosine . 0.50877596^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.83413449 |
| Insulin receptor phosphorylated IRS5 / DOK4 associates with RasGAP , Crk , Src , and Fyn , but not phosphatidylinositol 3 kinase p 85 , Grb 2 , SHP 2 , Nck , or phospholipase Cgamma Src homology 2 domains , and activates MAPK in cells . 0.83413449^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Sam 68 is a docking protein linking GAP and PI3K in insulin receptor signaling . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Grb 2 and Ras GAP appeared in the immunoprecipitates by anti insulin receptor and anti IRS 1 from insulin treated cells . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| The Tyr ( P ) forms of the insulin receptor and its 160 kDa substrate protein ( pp 160 ) associated with fusion proteins containing either or both the SH 2 domains of PI3K , but not with fusion proteins containing the two SH 2 domains of GAP or phospholipase C gamma . ^^^ These results demonstrate a specificity for the association of the Tyr ( P ) form of the insulin receptor and pp 160 with SH 2 domains that parallels the reported effects of insulin on PI3K , GAP , and phospholipase C gamma in vivo . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| These studies indicate that insulin stimulates the tyrosine phosphorylation of at least two distinct 60 kDa proteins , one that becomes associated with GAP and appears to be a direct substrate of the insulin receptor kinase and another that associates with the phosphatidylinositol 3 kinase . . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Localization of the insulin receptor binding sites for the SH 2 domain proteins p 85 , Syp , and GAP . ^^^ The insulin receptor is known to interact with the SH 2 domain proteins p 85 ( the regulatory subunit of phosphatidylinositol 3 kinase ) , Syp ( a tyrosine phosphatase ) , and GAP ( GTPase activating protein ) . ^^^ The NPXY internalization domain peptide inhibited insulin receptor precipitation by GAP GST . ^^^ The insulin receptor C terminal mutants , delta CT and Y / F2 , were not precipitated by p 85 or Syp GST and the NPXY mutant insulin receptors , delta Ex 16 and HI delta NPEY , were not precipitated by GAP GST . ^^^ Therefore , we conclude that p 85 and Syp bind to the insulin receptor C terminus at tyrosine 1322 and GAP binds to the insulin receptor NPXY domain at tyrosine 960 . . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Previously , we reported that after insulin treatment of rat HTC cells expressing human insulin receptors , a unique insulin receptor signaling complex was formed that contained the insulin receptor , the p 85 subunit of PI3K , GTPase activating protein ( GAP ) , and p 62 GAP associated protein . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Direct interaction of effector proteins such as the p 85 regulatory subunit of phosphatidylinositol 3 kinase ( PI 3 kinase ) , SYP ( SH 2 domain containing tyrosine phosphatase ) and GAP ( Ras GTPase activating protein ) with the insulin receptor ( IR ) and insulin like growth factor 1 ( IGF 1 ) type 1 receptor ( IGF 1R ) has been reported in some studies . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| In rat HTC hepatoma cells overexpressing normal human insulin receptors ( HTC IR ) , p 85 regulatory subunit of phosphatidylinositol 3 kinase ( PI3K ) forms signaling complexes containing the insulin receptor , insulin receptor substrate 1 ( IRS 1 ) , guanosine triphosphatase activating protein ( GAP ) and 60 70 kDa phosphotyrosine proteins ( p 60 70 ) . ^^^ These data suggest that 1 ) GAP associated protein , but not Sam 68 , is a part of insulin signaling complexes ; and 2 ) p85alpha and p85beta form similar , but distinct , insulin receptor signaling complexes . . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| In response to insulin , the following proteins were rapidly phosphorylated on tyrosine residues : 1 ) insulin receptor substrates 1 ( IRS 1 ) , 2 , and 4 ; 2 ) phospholipase C isoenzyme gamma ; 3 ) the Ras GTPase activating protein ( GAP ) associated with Rho GAP and p 62 ( Src ) ; 4 ) the insulin receptor beta subunit ; 5 ) the p 85 subunits of phosphatidylinositol 3 kinase ( PI 3 kinase ) ; 6 ) the Src homology 2 alpha collagen protein ; 7 ) protein kinase B ; 8 ) mitogen activated protein ( MAP ) kinase 1 and 2 ; and 9 ) growth receptor bound protein 2 . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Sam 68 associates with the SH 3 domains of Grb 2 recruiting GAP to the Grb 2 SOS complex in insulin receptor signaling . ^^^ We have recently found that Sam 68 is a substrate of the insulin receptor ( IR ) that translocates from the nucleus to the cytoplasm and that Tyr phosphorylated Sam 68 associates with the SH 2 domains of p 85 PI3K and GAP , in vivo and in vitro . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Insulin signal transduction involves the multisite docking protein insulin receptor substrate 1 ( IRS 1 ) and a number of Src homology 2 ( SH 2 ) domain factors , including p85 / p110 phosphatidylinositol 3 kinase , p 110 GTPase activating protein , and the phosphotyrosine specific phosphatase PTP1D . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| By this method we have found multiple proteins ( including the p 85 subunit of phosphatidylinositol 3 ' kinase and the ras GTPase activating protein ) that specifically associate with the activated ( phosphorylated ) insulin receptor ( insulin receptor complex proteins ) but are released from the complex after they are phosphorylated on tyrosine residues . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Lowest affinity ( 80 to 300 fold lower ) was observed with phosphopeptides corresponding to phosphorylated tyrosines of GTPase activating protein , insulin receptor substrate 1 , and SH 2 domain containing protein tyrosine phosphatase 1 . . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Role of p 85 subunit of phosphatidylinositol 3 kinase as an adaptor molecule linking the insulin receptor , p 62 , and GTPase activating protein . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| The injection of peroxovanadate also enhanced the tyrosine phosphorylation of many of the proteins known to function downstream of these receptors , including SHC , signal transducer and activator of transcription ( Stat ) 1alpha , beta , Stat 3 , Stat 5 , phospholipase C gamma , insulin receptor substrate 1 , GTPase activating protein , beta catenin , gamma catenin , p120cas , SHP 1 , and SHP 2 . ^^^ |
|
| Interacting proteins: P20936 and P06213 |
Pubmed |
SVM Score :0.0 |
| Insulin receptor mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase activating protein and Nck and is essential for inhibiting insulin stimulated activation of Ras and Akt . ^^^ |
|