Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
GPS 2 and TBL 1 , another component of the N CoR HDAC 3 complex , interact cooperatively with repression domain 1 of N CoR to form a heterotrimeric structure and are indirectly linked to HDAC 3 via an extended N CoR SANT domain that also activates latent HDAC 3 activity . ^^^ |
|
Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
Purification and functional characterization of the human N CoR complex : the roles of HDAC 3 , TBL 1 and TBLR 1 . ^^^ Corepressors N CoR and SMRT participate in diverse repression pathways and exist in large protein complexes including HDAC 3 , TBL 1 and TBLR 1 . ^^^ |
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Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
Here we show that endogenous N CoR , TBL 1 , and histone deacetylase 3 ( HDAC 3 ) , but not HDAC 1 , 2 , or 4 , are recruited to a stably integrated reporter gene repressed by unliganded TR as well as the orphan receptor RevErb . ^^^ |
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Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
Here , we report that transcriptional activation mediated by liganded nuclear receptors unexpectedly requires the actions of two highly related F box / WD 40 containing factors , TBL 1 and TBLR 1 , initially identified as components of an N CoR corepressor complex . ^^^ |
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Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
Although the N terminal RD binds transducin beta like protein 1 ( TBL 1 ) , TBLR 1 , and mSin 3 , deletion of this region did not affect the ability of N CoR to mediate repression by TR . ^^^ |
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Interacting proteins: O60907 and O75376 |
Pubmed |
SVM Score :0.0 |
Since Sif2p appears to be the yeast homolog of human TBL 1 and TBLR 1 , which function in the N CoR / SMRT complexes , its structural and oligomeric properties are likely to be very similar . . ^^^ |
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