| Interacting proteins: Q01094 and Q92793 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q01094 and Q92793 |
Pubmed |
SVM Score :0.0 |
| E2F1 and E1A ( 12S ) have a homologous activation domain regulated by RB and CBP . ^^^ The sequence homology reflects , at least partly , the conservation of common binding sites for the RB and CBP / p300 proteins , which are preserved in the same relative order along E2F1 and E1A . ^^^ |
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| Interacting proteins: Q01094 and Q92793 |
Pubmed |
SVM Score :0.0 |
| The CBP co activator stimulates E2F1 / DP1 activity . ^^^ The E2F1 activation domain has sequence similarity to the N terminal activation domain of E1A ( 12S ) , which contains binding sites for CBP as well as RB . ^^^ Here , we present evidence that the CBP protein directly contacts E2F1 / DP1 and stimulates its activation capacity . ^^^ We show that CBP interacts with the activation domain of E2F1 both in vitro and in vivo . ^^^ Deletion of four residues from the E2F1 activation domain reduces CBP binding as well as transcriptional activation , but still allows the binding of RB and MDM 2 . ^^^ |
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| Interacting proteins: Q01094 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Indeed , recent studies have demonstrated that multiple transcription factors bind to CBP , including c jun , c myb , MyoD , E2F1 , YY 1 , and members of the steroid hormone receptor superfamily , although it is not yet clear which of these transcription factors depend upon CBP for function . ^^^ |
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| Interacting proteins: Q01094 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Functional analysis of the E2F1 core domain demonstrated that replacement of phenylalanine residues 413 , 425 , and 429 with alanine reduces both transcriptional activation of the dhfr promoter and protein protein interactions with CBP , transcription factor ( TF ) IIH , and TATA binding protein ( TBP ) . ^^^ |
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| Interacting proteins: Q01094 and Q92793 |
Pubmed |
SVM Score :0.0 |
| TSA enhanced the protein expression of p 21 ( WAF 1 ) , CREB binding protein , cyclinE , cyclin A , Bak and Bax , while it reduced the expression of E2F 1 , E2F 4 , HDAC 1 , p 53 and hyperphosphorylated form of Rb . ^^^ |
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| Interacting proteins: Q01094 and Q92793 |
Pubmed |
SVM Score :0.0 |
| In view of this dichotomy in its functions and its critical role in cell cycle control , this study examined the following four aspects of E2F 1 in a panel of 87 non small cell lung carcinomas ( NSCLCs ) , previously analysed for defects in the pRb p 53 MDM2 network : firstly , the status of E2F 1 at the protein , mRNA and DNA levels ; secondly , its relationship with the kinetic parameters and genomic instability of the tumours ; thirdly , its association with the status of its transcriptional co activator CBP , downstream target PCNA and main cell cycle regulatory and E2F 1 interacting molecules pRb , p 53 and MDM 2 ; and fourthly , its impact on clinical outcome . ^^^ The protein levels of E2F 1 and its co activator CBP were significantly higher in the tumour area than in the corresponding normal epithelium ( p < 0 . 001 ) . ^^^ |
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