Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.59049407
Shc , Grb 2 , Sos 1 , and a 150 kilodalton tyrosine phosphorylated protein form complexes with Fms in hematopoietic cells . 0.59049407^^^
Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
Kinetic analysis reveals that the tyrosine phosphorylation of Cbl is coincident with its plasma membrane translocation and association with the activated tyrosine phosphorylated CSF 1 R , p 85 , Grb 2 , and tyrosine phosphorylated p58Shc and that these events precede the simultaneous multiubiquitination of Cbl and the CSF 1 R . ^^^ In the membrane fraction of cells stimulated at 4 degrees C , the association of p58Shc and Grb 2 with Cbl is stable , whereas its association with Sos and p 85 is transient and their dissociation occurs at the time CSF 1 R and Cbl multiubiquitination commence . ^^^ Complexes formed by Sos and Cbl are largely independent and membrane complexes of Cbl with other tyrosine phosphorylated proteins , p 85 and Grb 2 also contain CSF 1 R . ^^^ The membrane translocation and the pattern of association of Sos with the CSF 1R , p 85 , Grb 2 , and p58Shc resemble those of Cbl but Sos is not tyrosine phosphorylated , nor multiubiquitinated and the coprecipitation of these proteins , other than Grb 2 , with Sos is much less . ^^^
Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
A small pool of CSF 1R formed a multimeric complex with phosphatidylinositol 3 kinase ( PI 3 kinase ) , SHP 1 , Grb 2 , Shc , c Src , Cbl , and a significant number of tyrosine phosphorylated proteins in CSF 1 stimulated cells . ^^^ The major pool of activated CSF 1R formed transient multimeric complexes with distinctly different tyrosine phosphorylated proteins , which included STAT 3 but also PI 3 kinase , Shc , SHP 1 , and Grb 2 . ^^^
Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
Complexes are formed between Fms and other signal transduction proteins such as Grb 2 , Shc , Sos 1 , and p 85 . ^^^
Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
The 100 kDa protein did not appear to bind directly to Fms , Ship , Cbl , Shc , or Grb 2 , although all of these proteins were coimmunoprecipitated with p 85 after M CSF stimulation . ^^^
Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
Identification of a second Grb 2 binding site in the 5 Fms tyrosine kinase . ^^^ As reported previously , Y696KNI in the kinase insert domain of 5 Fms binds to the growth factor receptor bound protein 2 ( Grb 2 ) , a stimulator of the Ras / Raf1 pathway . ^^^ A yeast two hybrid system which allowed the formation of a functional Fms tyrosine kinase was employed to quantify binding of Grb 2 . ^^^ Fms protein containing either one of the two phosphorylation sites bound Grb 2 equally well , binding was increased for proteins carrying both sites . ^^^
Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
Accordingly , Mona interacts with activated Fms on phosphorylated Tyr 697 , which is also the Grb 2 binding site . ^^^
Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
After macrophage colony stimulating factor ( M CSF ) stimulation of FDC P 1 ( Fms ) myeloid cells , both 145 and 135 kD SHIP forms were tyrosine phosphorylated and could be coimmunoprecipitated with antibodies to Shc and Grb 2 . ^^^
Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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Interacting proteins: P07333 and P62993 Pubmed SVM Score :0.0
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