| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :1.1939368 |
| We show that RPD 3 associates with RbAp 48 through N and C terminal contacts and that RbAp 48 also interacts with SIN 3 . 1.1939368^^^ |
|
| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :0.0 |
| In addition to RPD 3 , repression by pRB in yeast requires MSI 1 , an ortholog of RbAp 48 , but not SIN 3 or SAP 30 . ^^^ |
|
| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :0.0 |
| Furthermore , the same HDAC 1 domain is also necessary for in vitro binding of HDAC 2 and HDAC 3 , association with RbAp 48 and for catalytic activity of the enzyme . ^^^ |
|
| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :0.0 |
| The histone deacetylase HDAC 3 targets RbAp 48 to the retinoblastoma protein . ^^^ HDAC 3 was thought not to interact with RbAp 48 . ^^^ Rather , we found , surprisingly , that HDAC 3 could physically interact with RbAp 48 both in vitro and in living cells . ^^^ |
|
| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :0.0 |
| Here , we use a purified Mi 2 complex containing six components , Mi 2 , Mta 1 like , p 66 , RbAp 48 , RPD 3 , and MBD 3 , to investigate the capacity of this complex to destabilize histone DNA interactions and deacetylate core histones . ^^^ |
|
| Interacting proteins: O15379 and Q09028 |
Pubmed |
SVM Score :0.0 |
| One complex contains Sin 3 , Rpd 3 , and RbAp 48 ; the second complex contains a Sin 3 independent histone deacetylase ; and the third complex lacks histone deacetylase activity . ^^^ |
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