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Transcription elongation regulator 1

CA150, FBP28, TCERG1
This gene encodes a nuclear protein that regulates transcriptional elongation and pre-mRNA splicing. The encoded protein interacts with the hyperphosphorylated C-terminal domain of RNA polymerase II via multiple FF domains, and with the pre-mRNA splicing factor SF1 via a WW domain. Alternative splicing results in multiple transcripts variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on CA150
The FF4 and FF5 domains of transcription elongation regulator 1 (TCERG1) target proteins to the periphery of speckles.
Suñé et al., Armilla, Spain. In J Biol Chem, 2012
The FF4 and FF5 domains of transcription elongation regulator 1 (TCERG1) target proteins to the periphery of speckles.
TCERG1 regulates alternative splicing of the Bcl-x gene by modulating the rate of RNA polymerase II transcription.
Suñé et al., Granada, Spain. In Mol Cell Biol, 2012
We propose that TCERG1 modulates the elongation rate of RNAPII to relieve pausing, thereby activating the proapoptotic Bcl-x(S) 5' splice site.
TCERG1 inhibits C/EBPα through a mechanism that does not involve sequestration of C/EBPα at pericentromeric heterochromatin.
Roesler et al., Saskatoon, Canada. In J Cell Biochem, 2011
TCERG1 can inhibit C/EBPalpha activity regardless of the latter's location in the nucleus
The ensemble folding kinetics of the FBP28 WW domain revealed by an all-atom Monte Carlo simulation in a knowledge-based potential.
Shakhnovich et al., Cambridge, United States. In Proteins, 2011
The study examines the order of formation of two beta-hairpins, the folding mechanism of each individual beta-hairpin, and transition state ensemble of formin-binding protein 28, FBP28 WW domain.
Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1).
Suñé et al., Granada, Spain. In J Biol Chem, 2010
mutation of the SUMO acceptor lysine residues enhanced TCERG1 transcriptional activity, indicating that SUMO modification negatively regulates TCERG1 transcriptional activity
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