Affinage

TCERG1

Transcription elongation regulator 1 · UniProt O14776

Length
1098 aa
Mass
123.9 kDa
Annotated
2026-06-10
30 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TCERG1 (CA150) is a nuclear factor that couples RNA polymerase II (RNAPII) transcription elongation with pre-mRNA splicing through a modular architecture of tandem WW and FF domains (PMID:9315662, PMID:11604498, PMID:16782886). Its FF domains bind directly to the hyperphosphorylated CTD of elongating RNAPII, with high-affinity recognition by the FF4-FF5 docking surface requiring simultaneous Ser2, Ser5, and Ser7 phosphorylation within consecutive heptad repeats (PMID:10908677, PMID:23436654); tandem FF domains are organized by continuous interdomain helices into an elongated, conformationally adaptable arrangement suited to engaging the intrinsically disordered phosphoCTD (PMID:19660470, PMID:19715701). Through its WW domains TCERG1 contacts splicing-transcription factors including SF1 and Tat-SF1, physically bridging the elongation and splicing machineries (PMID:11604498, PMID:15485897). TCERG1 modulates RNAPII elongation rate and processivity—originally defined at the HIV-1 LTR, where it acts in a TATA-dependent, Tat-coupled manner and promotes CTD Ser2 phosphorylation to relieve pausing (PMID:9315662, PMID:10373521, PMID:24165037)—and this kinetic control governs co-transcriptional alternative splicing decisions, promoting the pro-apoptotic Bcl-x(S) isoform via the SB1 element and regulating Fas/CD95, thereby linking its activity to the mitochondrial apoptosis pathway (PMID:22158966, PMID:26462236). TCERG1 concentrates at the periphery of nuclear speckles through an FF4-FF5 targeting signal and assembles transcription and splicing components into higher-order complexes via transient rather than stable associations (PMID:16782886, PMID:22453921, PMID:26873599). Its elongation activity is negatively regulated by sumoylation at Lys-503 and Lys-608 by the Ubc9 pathway (PMID:20215116). Independent of its core transcription/splicing role, TCERG1 inhibits C/EBPα through its glutamine-alanine repeat-dependent relocalization (PMID:19911371, PMID:26264132) and modifies disease-associated proteins, rescuing mutant huntingtin-induced striatal death in a nuclear-restriction-dependent manner and enhancing TDP-43 production (PMID:16641246, PMID:30541625).

Mechanistic history

Synthesis pass · year-by-year structured walk · 20 steps
  1. 1997 High

    Establishing CA150 as a holoenzyme-associated factor needed for Tat-dependent HIV-1 transcription defined it as a bona fide transcriptional regulator rather than an incidental nuclear protein.

    Evidence Biochemical purification, immunodepletion from in vitro transcription, and Co-IP with the RNAPII holoenzyme and Tat

    PMID:9315662

    Open questions at the time
    • Did not define which domains mediate holoenzyme association
    • Endogenous cellular targets beyond the HIV-1 system unknown
  2. 1999 Medium

    Showing CA150 controls elongation in a TATA-dependent manner at the HIV-1 LTR localized its activity to the elongation step and tied it to defined cis-elements.

    Evidence In vivo reporter assays and transcription elongation analysis at the HIV-1 LTR

    PMID:10373521

    Open questions at the time
    • Molecular basis of elongation effect not resolved
    • Limited to the HIV-1 promoter context
  3. 2000 High

    Identifying FF domains as direct phosphoCTD-binding modules provided the molecular handle by which TCERG1 engages actively transcribing RNAPII.

    Evidence PhosphoCTD affinity purification and binding assays with recombinant FF domain fragments

    PMID:10908677

    Open questions at the time
    • Phospho-mark specificity not yet defined
    • Affinity and stoichiometry of CTD engagement unquantified
  4. 2001 High

    Defining the WW-SF1 and FF-phosphoCTD interactions as jointly required for repression revealed how a single protein bridges splicing and elongation machineries.

    Evidence Domain mutagenesis, in vitro binding, Co-IP, and reporter repression assays

    PMID:11604498

    Open questions at the time
    • Mechanism by which SF1 engagement enforces repression unclear
    • Whether bridging is direct on a single polymerase untested
  5. 2001 Medium

    The interaction with huntingtin and partial colocalization with HD aggregates first linked TCERG1 to neurodegenerative disease pathology.

    Evidence Yeast two-hybrid screen, in vitro binding with lysates, and HD brain immunohistochemistry

    PMID:11172033

    Open questions at the time
    • Functional consequence of the htt interaction not established here
    • Direct vs. indirect binding not distinguished in cells
  6. 2004 High

    Quantifying FF-domain binding to Tat-SF1 and defining acidic consensus motifs explained how FF domains recognize multiple charged ligands including the CTD.

    Evidence Mass spectrometry partner identification, NMR titration, and peptide binding assays

    PMID:15485897

    Open questions at the time
    • Micromolar affinities leave physiological avidity mechanism open
    • How Ser2/Ser5 marks are read combinatorially not yet resolved
  7. 2006 High

    Mapping speckle localization to FF domains and showing both WW and FF regions are needed for complex assembly established TCERG1 as a scaffold organizing transcription/splicing components.

    Evidence Immunofluorescence, domain deletion mutants, and biochemical co-purification under transcription/CTD-phosphorylation perturbation

    PMID:16782886

    Open questions at the time
    • Composition of the higher-order complexes not defined
    • Functional output of speckle targeting untested at this stage
  8. 2006 Medium

    Demonstrating that CA150 overexpression rescues mutant huntingtin-induced striatal death implicated TCERG1 function in neuroprotection and tied it to nuclear localization.

    Evidence Lentiviral rat striatum and knock-in mouse cell models with QA-repeat mutant rescue and cell death assays

    PMID:16641246

    Open questions at the time
    • Endogenous TCERG1 role in HD not addressed
    • Transcriptional targets mediating rescue unidentified
  9. 2008 Medium

    Genome-scale knockdown showed TCERG1 broadly shapes alternative mRNA processing and 3'-UTR usage, generalizing it from a single-promoter factor to a global coupling regulator.

    Evidence siRNA knockdown with microarray, RT-PCR validation, and computational alternative-processing analysis

    PMID:18187414

    Open questions at the time
    • Direct vs. indirect targets not distinguished
    • Mechanism linking elongation to 3'-end choice unresolved
  10. 2009 High

    Crystal and NMR structures of tandem FF domains revealed continuous interdomain helices producing an elongated, flexible array optimized for engaging the disordered phosphoCTD.

    Evidence X-ray crystallography of FF1-3 and NMR solution structure plus relaxation of FF1+FF2

    PMID:19660470 PMID:19715701

    Open questions at the time
    • How flexibility translates to CTD recognition specificity not directly shown
    • Structures of the WW region and full-length protein absent
  11. 2010 High

    Identifying Lys-503/Lys-608 sumoylation by Ubc9 as a negative regulator of TCERG1 elongation activity revealed a post-translational switch separating its transcription from its splicing/localization functions.

    Evidence Sumoylation assays, acceptor-lysine mutagenesis, Ubc9 interaction, and reporter transcription/immunofluorescence

    PMID:20215116

    Open questions at the time
    • Upstream signals controlling TCERG1 sumoylation unknown
    • Endogenous extent and dynamics of modification not quantified
  12. 2010 Medium

    Defining TCERG1 as an inhibitor of C/EBPα via N-terminal-region-dependent relocalization extended its regulatory reach beyond general elongation to a specific anti-proliferative transcription factor.

    Evidence Reporter assays, confocal microscopy with localization mutants, and co-expression

    PMID:19911371 PMID:21503969

    Open questions at the time
    • Biochemical mechanism of C/EBPα inhibition not established
    • Physiological relevance in proliferating tissues untested
  13. 2011 High

    Showing TCERG1 promotes Bcl-x(S) by altering RNAPII elongation rate at the endogenous gene provided direct evidence for a kinetic coupling mechanism linking pausing to splice-site choice.

    Evidence siRNA, RT-PCR splicing assays, RNA-association ChIP, transcription-rate analysis, and slow-polymerase rescue

    PMID:22158966

    Open questions at the time
    • Generality of kinetic mechanism across targets not shown here
    • Precise splice-site-selection step affected not pinpointed
  14. 2012 High

    Identifying FF4-FF5 as a portable speckle-periphery targeting signal that also contributes to splicing regulation linked subnuclear positioning to function.

    Evidence Domain fusion constructs, confocal immunofluorescence, NMR folding, and splicing reporter

    PMID:22453921

    Open questions at the time
    • How speckle-periphery positioning mechanistically aids splicing unclear
    • Endogenous targeting determinants in full-length protein not isolated
  15. 2013 High

    Defining the FF4/FF5 CTD-docking surface and a requirement for simultaneous Ser2/Ser5/Ser7 phosphorylation established a uniquely stringent code for TCERG1 recruitment to elongating RNAPII.

    Evidence NMR structure of FF4-FF6, phospho-peptide column binding, NMR titrations, and mutagenesis

    PMID:23436654

    Open questions at the time
    • Kinases generating the triple mark in vivo not identified
    • How this contrasts with CTD-independent recruitment seen in cells unreconciled
  16. 2013 Medium

    Showing TCERG1 depletion reduces HIV-1 transcription and increases CTD Ser2 phosphorylation at the endogenous locus connected its elongation function to pause-release via CTD modification.

    Evidence siRNA, RNAPII ChIP, nascent RNA quantification, and Ser2 phospho-CTD analysis at the HIV-1 LTR

    PMID:24165037

    Open questions at the time
    • Whether TCERG1 directly recruits a Ser2 kinase unknown
    • Effect at cellular genes beyond HIV-1 not measured here
  17. 2015 Medium

    Linking TCERG1-driven Bcl-x and Fas splicing to apoptotic execution established a functional output of its splicing activity in the mitochondrial death pathway.

    Evidence siRNA/overexpression, RT-PCR splicing, annexin-V/caspase/PARP assays, mitochondrial potential, and Bak activation

    PMID:26462236

    Open questions at the time
    • Causality between specific isoform shifts and death not fully isolated
    • Context-dependence across cell types not explored
  18. 2016 High

    Live-cell FRAP resolved the coupling model, showing TCERG1 engages paused elongation complexes and forms new complexes during co-transcriptional splicing through transient rather than stable interactions.

    Evidence FRAP with DRB, α-amanitin, spliceostatin A, and a co-transcriptional splicing reporter

    PMID:26873599

    Open questions at the time
    • CTD-independent recruitment mechanism in cells not molecularly defined
    • Identity of transient partners during splicing not captured
  19. 2016 Medium

    Mapping the QA repeat as required for C/EBPα complex formation and relocalization defined the structural determinant of TCERG1's anti-proliferative inhibition.

    Evidence QA-repeat deletion/truncation mutants, Co-IP, confocal microscopy, and growth-arrest assays

    PMID:26264132

    Open questions at the time
    • Direct QA-mediated contact surface on C/EBPα unknown
    • Whether QA repeat acts similarly at other partners untested
  20. 2018 Medium

    Identifying TCERG1 as a genetic modulator of TDP-43 production tied its mRNA-processing function to an ALS/FTD-relevant protein.

    Evidence Drosophila genetic screen with transcript analysis and mammalian overexpression with protein quantification

    PMID:30541625

    Open questions at the time
    • Step of TDP-43 mRNA processing affected not pinpointed
    • Endogenous loss-of-function effect on TDP-43 not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • How TCERG1 reconciles its in vitro requirement for triple-phosphorylated CTD with CTD-phosphorylation-independent recruitment in living cells, and what defines its transient co-transcriptional splicing partners, remains unresolved.
  • No defined recruitment pathway independent of CTD phosphorylation
  • Transient splicing-complex composition uncharacterized
  • Kinase(s) generating the FF-recognized CTD code not identified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 5 GO:0008092 cytoskeletal protein binding 3 GO:0045182 translation regulator activity 3 GO:0060090 molecular adaptor activity 3
Localization
GO:0005634 nucleus 3 GO:0005654 nucleoplasm 3
Pathway
R-HSA-74160 Gene expression (Transcription) 4 R-HSA-8953854 Metabolism of RNA 3 R-HSA-5357801 Programmed Cell Death 2
Partners
CEBPAHTTPOLR2ASF1TATSF1UBE2I
Complex memberships
RNA polymerase II holoenzyme

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 CA150 (TCERG1) is a nuclear protein associated with the RNA polymerase II holoenzyme; immunodepletion of CA150 abolished Tat trans-activation in vitro, and both CA150 and Tat were shown to co-immunoprecipitate with the RNAPII holoenzyme, establishing CA150 as a component required for Tat-dependent HIV-1 transcriptional activation. Biochemical purification, molecular cloning, immunodepletion from in vitro transcription assay, immunoprecipitation Molecular and cellular biology High 9315662
1999 CA150 regulates RNA polymerase II elongation in a TATA-box-dependent manner at the HIV-1 LTR promoter; functional assays showed CA150 affects transcription elongation complex processivity and requires the same cis-elements as Tat activation. In vivo reporter gene functional assays, transcription elongation analysis Molecular and cellular biology Medium 10373521
2000 The FF domains of CA150 (TCERG1) directly bind the hyperphosphorylated C-terminal repeat domain (phosphoCTD) of RNA polymerase II; the fifth FF domain alone was sufficient for phosphoCTD binding, identifying FF domains as protein-interaction modules that bind the phosphoCTD. Phospho-CTD affinity purification, binding assays with recombinant FF domain fragments Proceedings of the National Academy of Sciences of the United States of America High 10908677
2001 CA150 represses RNAPII transcription elongation; its FF repeat domains bind directly to the phosphorylated CTD of RNAPII (required for repression), while WW1 and WW2 domains interact directly with the splicing-transcription factor SF1 through a novel proline-rich motif in the C-terminal half of SF1, and these interactions are required for efficient CA150-mediated transcriptional repression. In vitro binding assays, domain deletion/mutation analysis, co-immunoprecipitation, reporter transcription assays Molecular and cellular biology High 11604498
2001 CA150 (TCERG1) interacts in vitro with full-length huntingtin (htt) from lymphoblastoid cells and co-localizes partially with ubiquitin-positive aggregates in HD brain tissue; a C. elegans WW-domain protein (ZK1127.9) was identified as an htt-interacting protein via yeast two-hybrid, with CA150 as its human homologue. Yeast two-hybrid screen, in vitro binding assay with cell lysates, immunohistochemistry Proceedings of the National Academy of Sciences of the United States of America Medium 11172033
2004 CA150/TCERG1 FF domains interact with multiple nuclear binding partners including Tat-SF1; individual FF domains bind Tat-SF1 peptide ligands noncooperatively with affinities of 150–500 µM through consensus acidic motifs (D/E)2/5-F/W/Y-(D/E)2/5; phosphorylation at both Ser2 and Ser5 of the RNAPII CTD generates the required negative charges for FF domain recognition. Mass spectrometry identification of binding partners, NMR titration, peptide binding assays Molecular and cellular biology High 15485897
2006 CA150/TCERG1 localizes to nuclear speckles enriched in splicing factors; this localization requires FF domains (not WW domains) and is not affected by inhibition of transcription or RNAPII CTD phosphorylation; both the N-terminal WW-domain region and a C-terminal FF-domain region are required to assemble transcription and splicing components into higher-order complexes. Immunofluorescence/confocal microscopy, domain deletion mutant analysis, biochemical co-purification assays Molecular and cellular biology High 16782886
2006 CA150 expression rescues striatal cell death induced by mutant huntingtin in both lentiviral overexpression (rat) and knock-in (mouse cell) models; rescue requires the (Gln-Ala)38 repeat, which is necessary for nuclear restriction of exogenous CA150 but dispensable for CA150 transcriptional repression activity, suggesting nuclear localization is critical for neuroprotection. Lentiviral overexpression in rat striatum, knock-in mouse cell system, cell death assays, confocal microscopy, mutant rescue experiments The Journal of neuroscience Medium 16641246
2008 Knockdown of TCERG1 by siRNA leads to widespread alterations in alternative mRNA processing and affects 3'-UTR processing; TCERG1 cellular targets are enriched in microRNA-binding sites, supporting a role for TCERG1 in coupling transcription and mRNA processing. siRNA knockdown, microarray gene expression analysis, RT-PCR validation, computational alternative processing analysis The Journal of biological chemistry Medium 18187414
2009 Crystal structure of the first three tandem FF domains of CA150/TCERG1 at 2.7 Å resolution reveals that consecutive FF domains are connected by a continuous alpha-helix (the last helix of one FF domain merges into the first helix of the next), creating an elongated arrangement that exposes charged residues for intermolecular interactions. X-ray crystallography (2.7 Å resolution), peptide binding studies Journal of molecular biology High 19660470
2009 NMR solution structure and relaxation analysis of the CA150 FF1+FF2 tandem shows that the interdomain linker forms a helical extension of helix α3 of FF1, maintaining distance between the two FF domains without fixing their relative orientation; the domains adopt a dumbbell-like arrangement allowing individual FF domains to maneuver for recognition of flexible partners such as the intrinsically-disordered phosphoCTD. NMR spectroscopy (solution structure + relaxation experiments) Journal of molecular biology High 19715701
2010 TCERG1 is sumoylated at Lys-503 and Lys-608 by SUMO family proteins; TCERG1 binds the E2 SUMO-conjugating enzyme Ubc9; mutation of the SUMO acceptor lysines enhanced TCERG1 transcriptional activity (but did not affect nuclear speckle localization or alternative splicing function), establishing that sumoylation negatively regulates TCERG1 transcriptional elongation activity. Sumoylation assays, site-directed mutagenesis of SUMO acceptor lysines, interaction assays with Ubc9, reporter transcription assays, immunofluorescence The Journal of biological chemistry High 20215116
2010 TCERG1 inhibits the transcriptional and anti-proliferative activities of C/EBPα; the inhibitory activity maps to the amino-terminal region of TCERG1; co-expression with C/EBPα causes redistribution of TCERG1 from nuclear speckles to pericentromeric sites where C/EBPα resides, and this nuclear relocalization is required for the inhibitory activity. Reporter gene assays, confocal microscopy with nuclear localization mutants, co-expression experiments Journal of cellular biochemistry Medium 19911371
2011 TCERG1 regulates alternative splicing of the apoptosis gene Bcl-x in a promoter-dependent manner: it promotes the short pro-apoptotic Bcl-x(S) isoform through the SB1 regulatory element in exon 2; TCERG1 associates with the Bcl-x pre-mRNA; it modifies the elongation rate of RNAPII on endogenous Bcl-x and affects pre-mRNA levels at distal regions, indicating a kinetic coupling mechanism linking RNAPII pausing to splice-site selection. siRNA knockdown, RT-PCR splicing assays, chromatin immunoprecipitation (RNA association), RNAPII transcription rate analysis, slow polymerase mutant rescue experiments Molecular and cellular biology High 22158966
2011 TCERG1 redistribution from nuclear speckles to pericentromeric regions upon C/EBPα co-expression does not require C/EBPα to be transcriptionally active or to be localized to pericentromeric heterochromatin itself; TCERG1 can inhibit C/EBPα activity regardless of its nuclear location, indicating the inhibitory mechanism is not simply sequestration at heterochromatin. Confocal microscopy with C/EBPα mutants (V296A and others), reporter assays Journal of cellular biochemistry Medium 21503969
2012 The FF4 and FF5 domains of TCERG1 constitute a speckle-periphery targeting signal; this FF4-FF5 pair folds as a functional unit in solution and is both necessary and sufficient (when fused to heterologous proteins) to direct proteins to the periphery of nuclear speckles; this targeting signal also contributes to alternative splicing regulation of a reporter pre-mRNA. Domain deletion/fusion constructs, confocal immunofluorescence, NMR folding assay, in vivo splicing reporter assay The Journal of biological chemistry High 22453921
2013 Structural characterization (NMR + biochemistry) of the tandem FF4-FF5-FF6 domains of TCERG1 shows a rigid integral domain structure; binding to the phosphoCTD of RNAPII requires simultaneous phosphorylation at Ser2, Ser5, AND Ser7 within two consecutive heptad repeats, and is mediated by CTD-docking sites on FF4 and FF5 (but not FF6) — the first example of a nuclear factor requiring all three phospho-Ser marks for high-affinity CTD binding. NMR structure determination, peptide column binding assays, NMR titrations, site-specific phospho-CTD peptides The Journal of biological chemistry High 23436654
2013 TCERG1 depletion reduces basal and Tat-activated transcription from the HIV-1 LTR; TCERG1 directly affects RNAPII elongation rate in vivo at the HIV-1 locus and increases phosphorylation of Ser2 within the RNAPII CTD, suggesting a mechanism by which TCERG1 relieves transcriptional pausing by promoting CTD Ser2 phosphorylation. siRNA knockdown, ChIP for RNAPII distribution, nascent RNA quantification at distal regions, Ser2 phospho-CTD analysis Retrovirology Medium 24165037
2015 TCERG1 modulates alternative splicing of both Bcl-x and Fas/CD95 genes; changes in Bcl-x splicing by TCERG1 correlate with induction of apoptosis (assessed by annexin-V binding, caspase-3 cleavage, PARP-1 cleavage, mitochondrial membrane permeabilization); depletion of TCERG1 reduces activated Bak levels, linking TCERG1-mediated splicing to the mitochondrial apoptosis pathway. siRNA knockdown and overexpression, RT-PCR splicing assays, cell death assays (annexin-V, caspase cleavage, PARP cleavage), mitochondrial membrane potential assay, Bak activation assay PloS one Medium 26462236
2016 Live-cell FRAP experiments show TCERG1 is highly mobile in the nucleoplasm; DRB (transcription elongation inhibitor) but not α-amanitin (RNAPII degrader) reduces TCERG1 mobility, indicating interaction with paused elongation complexes; TCERG1 is recruited to active transcription sites independently of RNAPII CTD phosphorylation; mobility is further reduced when splicing occurs co-transcriptionally, indicating formation of new macromolecular complexes during co-transcriptional splicing, consistent with TCERG1 coupling elongation and splicing via transient rather than stable interactions. Live-cell FRAP (fluorescence recovery after photobleaching), DRB and α-amanitin treatment, spliceostatin A treatment, cotranscriptional splicing reporter RNA High 26873599
2016 The glutamine-alanine (QA) repeat domain of TCERG1 is required for inhibition of C/EBPα growth arrest activity; deletion of the QA repeat abrogates TCERG1–C/EBPα complex formation, prevents relocalization from nuclear speckles to pericentromeric regions, and enlarges nuclear speckles; a minimal number of QA repeats is required for inhibitory activity. QA-repeat deletion and truncation mutants, co-immunoprecipitation, confocal microscopy, growth arrest functional assays Journal of cellular biochemistry Medium 26264132
2018 TCERG1 (human homolog of Drosophila CG42724) was identified as a genetic modulator of TDP-43 production; CG42724 overexpression in a Drosophila model promotes production of TDP-43 mRNA transcripts efficiently released into the cytoplasm; overexpression of human TCERG1 in mammalian cells increases TDP-43 protein steady-state levels. Drosophila genetic screen, mRNA transcript analysis, mammalian cell overexpression with protein level quantification Acta neuropathologica communications Medium 30541625

Source papers

Stage 0 corpus · 30 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis. Proceedings of the National Academy of Sciences of the United States of America 134 11172033
2001 The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1. Molecular and cellular biology 105 11604498
1997 CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription. Molecular and cellular biology 87 9315662
2000 Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II. Proceedings of the National Academy of Sciences of the United States of America 79 10908677
2004 FF domains of CA150 bind transcription and splicing factors through multiple weak interactions. Molecular and cellular biology 55 15485897
1999 Transcriptional cofactor CA150 regulates RNA polymerase II elongation in a TATA-box-dependent manner. Molecular and cellular biology 52 10373521
2006 Human transcription elongation factor CA150 localizes to splicing factor-rich nuclear speckles and assembles transcription and splicing components into complexes through its amino and carboxyl regions. Molecular and cellular biology 49 16782886
2006 CA150 expression delays striatal cell death in overexpression and knock-in conditions for mutant huntingtin neurotoxicity. The Journal of neuroscience : the official journal of the Society for Neuroscience 47 16641246
2011 TCERG1 regulates alternative splicing of the Bcl-x gene by modulating the rate of RNA polymerase II transcription. Molecular and cellular biology 46 22158966
2008 Identification of the cellular targets of the transcription factor TCERG1 reveals a prevalent role in mRNA processing. The Journal of biological chemistry 36 18187414
2006 Gender biased differential alternative splicing patterns of the transcriptional cofactor CA150 gene in Schistosoma mansoni. Molecular and biochemical parasitology 30 16904200
2010 Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1). The Journal of biological chemistry 23 20215116
2014 A new optimized formulation of cationic solid lipid nanoparticles intended for gene delivery: development, characterization and DNA binding efficiency of TCERG1 expression plasmid. International journal of pharmaceutics 21 24999055
2013 Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat. The Journal of biological chemistry 21 23436654
2008 Solution structure of the yeast URN1 splicing factor FF domain: comparative analysis of charge distributions in FF domain structures-FFs and SURPs, two domains with a similar fold. Proteins 20 18536009
2015 Functional Consequences for Apoptosis by Transcription Elongation Regulator 1 (TCERG1)-Mediated Bcl-x and Fas/CD95 Alternative Splicing. PloS one 15 26462236
2022 Huntington's disease age at motor onset is modified by the tandem hexamer repeat in TCERG1. NPJ genomic medicine 14 36064847
2016 The in vivo dynamics of TCERG1, a factor that couples transcriptional elongation with splicing. RNA (New York, N.Y.) 14 26873599
2012 The FF4 and FF5 domains of transcription elongation regulator 1 (TCERG1) target proteins to the periphery of speckles. The Journal of biological chemistry 12 22453921
2018 Identification of TCERG1 as a new genetic modulator of TDP-43 production in Drosophila. Acta neuropathologica communications 11 30541625
2013 Transcription elongation regulator 1 (TCERG1) regulates competent RNA polymerase II-mediated elongation of HIV-1 transcription and facilitates efficient viral replication. Retrovirology 11 24165037
2009 Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays. Journal of molecular biology 10 19715701
2004 Conspicuous accumulation of transcription elongation repressor hrp130/CA150 on the intron-rich Balbiani ring 3 gene. Chromosoma 10 15480727
2013 Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain. International journal of molecular sciences 9 23999589
2009 Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150. Journal of molecular biology 9 19660470
2006 Expression and purification of active WW domains of FBP11/HYPA and FBP28/CA150. Protein and peptide letters 6 16472085
2010 Nuclear redistribution of TCERG1 is required for its ability to inhibit the transcriptional and anti-proliferative activities of C/EBPalpha. Journal of cellular biochemistry 5 19911371
2011 TCERG1 inhibits C/EBPα through a mechanism that does not involve sequestration of C/EBPα at pericentromeric heterochromatin. Journal of cellular biochemistry 4 21503969
2016 The Glutamine-Alanine Repeat Domain of TCERG1 is Required for the Inhibition of the Growth Arrest Activity of C/EBPα. Journal of cellular biochemistry 3 26264132
2024 Spliceosome component TCERG1 regulates the aggressiveness of somatotroph adenoma. Journal of endocrinological investigation 0 39361240

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