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Nuclear Receptor Signaling Atlas
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CTBP1
Overview
Synonyms
50 kDa BFA-dependent ADP-ribosylation substrate ; 50-kDa BFA-induced ADP-ribosylated substrate ; 50-kDaBFA-inducedADP-ribosylatedsubstrate ; BARS ; BARS-50 ; Bars ; C-terminal-binding protein 1 ; C-terminal-binding protein 3 ; C-terminus binding protein 3/brefeldin A (BFA) adenosine diphosphate-ribosylated substrate ; CTBP1 ; CtBP1-L ; CtBP1-S ; CtBP3/BARS ; Ctbp1 ; D4S115h ; D5H4S115 ; D5H4S115E ; LOC612240 ; brefeldin A-ADP-riboslyated substrate ; brefeldin A-ribosylated substrate ; ctBP3 ; ctbp-1 ; fa96d06 ; wu:fa96d06 ; zgc:136929
NURSA Name
C-terminal binding protein 1
Official Symbol
CTBP1
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Description
CtBPs (C-terminal binding proteins) are highly conserved transcriptional co-repressors involved in various processes such as development, cell cycle regulation and transformation. The negative modulator CtBP was shown to interact with RIP140 through a sequence, PIDLSCK, in the amino-terminal third of the RIP140 protein. RIP140 is acetylated at this Lys residue by CBP/p300 and this modification abolishes the CtBP interaction, resulting in a loss of repression. Acetylation of transcriptional repressors may be a general mode of disrupting CtBP corepressor complexes.
Original References:
Schaeper U, Boyd JM, Verma S, Uhlmann E, Subramanian T and Chinnadurai G (1995) Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation. Proc. Natl. Acad. Sci. U.S.A. 92 10467-71 View Abstract | View PubMed
Vo N, Fjeld C and Goodman RH (2001) Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP. Mol. Cell. Biol. 21 6181-8 View Abstract | View PubMed
Castet A, Boulahtouf A, Versini G, Bonnet S, Augereau P, Vignon F, Khochbin S, Jalaguier S and Cavaillès V (2004) Multiple domains of the Receptor-Interacting Protein 140 contribute to transcription inhibition. Nucleic Acids Res. 32 1957-66 View Abstract | View PubMed
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