| Interacting proteins: O43463 and Q13547 |
Pubmed |
SVM Score :0.94093133 |
| Coimmunoprecipitation experiments indicated that Suv39H1 can physically interact with HDAC 1 , 2 and 3 , therefore suggesting that transcriptional repression by Suv39H1 could be the consequence of histone deacetylases recruitment . 0.94093133^^^ |
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| Interacting proteins: O43463 and Q13547 |
Pubmed |
SVM Score :0.0 |
| By immunoprecipitation and GST pull down , we show that DNMT3B interacts with HDAC 1 , HDAC 2 , HP 1 proteins , Suv39h1 , and the ATP dependent chromatin remodeling enzyme hSNF2H . ^^^ |
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| Interacting proteins: O43463 and Q13547 |
Pubmed |
SVM Score :0.0 |
| Chromatin immunoprecipitation assay demonstrated that cyclin D 1 enhanced recruitment of HDAC 1 and HDAC 3 and histone methyltransferase SUV39H1 to the PPAR response element of the lipoprotein lipase promoter and decreased acetylation of total histone H 3 and histone H 3 lysine 9 . ^^^ |
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| Interacting proteins: O43463 and Q13547 |
Pubmed |
SVM Score :0.0 |
| Here we show that p 130 is the predominant Rb family member associated with E2F in neurons , that its major partner for repression of pro apoptotic genes is E2F4 , and that the p 130 E2F4 complex recruits the chromatin modifiers HDAC 1 and Suv39H1 to promote gene silencing and neuron survival . ^^^ |
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| Interacting proteins: O43463 and Q13547 |
Pubmed |
SVM Score :0.0 |
| Mutation analysis of HDAC 1 , HDAC 2 , SUV39H1 , and SUV39H2 revealed only two out of 181 cancer samples ( both cell lines ) with significant coding sequence alterations . ^^^ |
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| Interacting proteins: O43463 and Q13547 |
Pubmed |
SVM Score :0.0 |
| The pRb protein represses gene transcription , required for transition from G 1 to S phase , by directly binding to the transactivation domain of E2F and by binding to the promoter of these genes as a complex with E2F . pRb represses transcription also by remodeling chromatin structure through interaction with proteins such as hBRM , BRG 1 , HDAC 1 and SUV39H1 , which are involved in nucleosome remodeling , histone acetylation / deacetylation and methylation , respectively . ^^^ |
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