| Interacting proteins: P61758 and P40337 |
Pubmed |
SVM Score :0.54483008 |
| It was also established that epitope tagged pVHL strongly forms complexes with VBP 1 in vivo using immunoprecipitation Western blotting analysis . 0.54483008^^^ These results indicate that VBP 1 can form a complex with VHL protein in vivo and hence VHL affects the intracellular localization of VBP 1 protein . . 0.52589692^^^ |
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| Interacting proteins: P61758 and P40337 |
Pubmed |
SVM Score :0.0 |
| Recently , a protein ( VBP 1 ) was isolated that was found to bind to the VHL protein in vivo . ^^^ Moreover , expression of the human VBP 1 gene was investigated in cerebellum and in various tumours of VHL patients encompassinghaemangioblastomas , renal cell carcinomas and pheochromocytomas . ^^^ |
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| Interacting proteins: P61758 and P40337 |
Pubmed |
SVM Score :0.0 |
| A further VHL binding protein of unknown function , VBP 1 , fails to bind to truncated forms of VHL . ^^^ We have investigated the possible roles of CUL 2 and VBP 1 in renal tumorigenesis by analyzing sporadic RCC of known VHL mutation or hypermethylation status , including CC RCC without VHL inactivation ( n = 40 ) ; CC RCC with VHL inactivation ( n = 35 ) ; and non CC RCC ( n = 14 ) . ^^^ |
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| Interacting proteins: P61758 and P40337 |
Pubmed |
SVM Score :0.0 |
| The VHL gene product is reported to form complexes with various proteins including elongin B , elongin C , VBP 1 , fibronectin , Spl , CUL 2 , and HIF 1 . ^^^ Although most of the regions in pVHL that had been implicated in binding specific proteins demonstrated evolutionary conservation , the carboxy terminal putative VBP 1 binding site was less well conserved , suggesting that VBP 1 binding may have less functional significance . ^^^ |
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| Interacting proteins: P61758 and P40337 |
Pubmed |
SVM Score :0.0 |
| VBP 1 has been isolated as a novel protein binding to the von Hippel Lindau ( VHL ) tumor suppressor gene product . ^^^ |
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| Interacting proteins: P61758 and P40337 |
Pubmed |
SVM Score :0.0 |
| As a step forward to the understanding of the molecular mechanisms underlying the roles of these two mammalian MutS homologues , here we have identified von Hippel Lindau ( VHL ) tumor suppressor binding protein 1 ( VBP 1 ) as an interacting protein partner for human MSH 4 ( hMSH 4 ) . ^^^ |
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| Interacting proteins: P61758 and P40337 |
Pubmed |
SVM Score :0.0 |
| Furthermore , during the interaction of Mnk 2 with von Hippel Lindau ( VHL ) tumor suppressor binding protein 1 ( VBP 1 ) , it appears that Mnk 2 also joins to modulate cell shape as VBP 1 plays an important role in the process of the maturation of the cytoskeleton and in the process of morphogenesis . . ^^^ |
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