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TCERG1 encodes a nuclear protein that regulates transcriptional elongation and pre-mRNA splicing. Additionally we are shipping and many more products for this protein.
Showing 10 out of 59 products:
Human Polyclonal TCERG1 Primary Antibody for IHC (p), IHC - ABIN152555
McFie, Wang, Timchenko, Wilson, Hu, Roesler: Identification of a co-repressor that inhibits the transcriptional and growth-arrest activities of CCAAT/enhancer-binding protein alpha. in The Journal of biological chemistry 2006
Show all 4 Pubmed References
Human Monoclonal TCERG1 Primary Antibody for IF, WB - ABIN968310
Suñé, Hayashi, Liu, Lane, Young, Garcia-Blanco: CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription. in Molecular and cellular biology 1997
The QA repeat domain of TCERG1 is required for relocalization of CEBPalpha.
TCERG1 binds independently to elongation and splicing complexes, thus performing their coupling by transient interactions rather than by stable association with one or the other complexes.
TCERG1 sensitizes a cell to apoptotic agents, thus promoting apoptosis by regulating the alternative splicing of both the Bcl-x (show BCL2L1 Antibodies) and Fas/CD95 (show FAS Antibodies) genes.
This study reveals that TCERG1 regulates HIV-1 transcriptional elongation by increasing the elongation rate of RNAPII and phosphorylation of Ser 2 within the carboxyl-terminal domain.
Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2 (show JAG2 Antibodies), Ser5, and Ser7 within the carboxyl-terminal domain repeat.
The FF4 and FF5 domains of transcription elongation regulator 1 (TCERG1) target proteins to the periphery of speckles.
We propose that TCERG1 modulates the elongation rate of RNAPII to relieve pausing, thereby activating the proapoptotic Bcl-x (show BCL2L1 Antibodies)(S) 5' splice site.
TCERG1 can inhibit C/EBPalpha (show CEBPA Antibodies) activity regardless of the latter's location in the nucleus
mutation of the SUMO acceptor lysine residues enhanced TCERG1 transcriptional activity, indicating that SUMO modification negatively regulates TCERG1 transcriptional activity
Specific alleles in GluR6 (show GRIK2 Antibodies) and CA150 locus were only observed in HD patients.
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 (show DRP2 Antibodies).
CA150 FF domains recognize multiple sites within the Tat-SF1 (show HTATSF1 Antibodies) protein conforming to the consensus motif (D/E)(2/5)-F/W/Y-(D/E)(2/5).
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.
transcription factor CA150
, transcription elongation regulator 1
, TATA box binding protein (TBP)-associated factor, RNA polymerase II, S, 150kD
, TATA box-binding protein-associated factor 2S
, co-activator of 150 kDa
, transcription elongation regulator 1 (CA150)
, FBP 28
, coactivator of 150 kD
, formin-binding protein 28
, transcription factor CA150b