◀ Back to POLR2E
ERCC3 — POLR2E
Pathways - manually collected, often from reviews:
-
Reactome Reaction:
POLR2E
→
ERCC3
(reaction)
Tirode et al., Mol Cell 1999, Fiedler et al., Bioessays 2000, Fiedler et al., Nucleic Acids Res 2001, Pal et al., Mol Cell Biol 2001, Pal et al., Mol Cell Biol 2002, Yuan et al., EMBO Rep 2002, Wang et al., Science 1992, Jacob et al., J Biol Chem 1991, Bunick et al., Cell 1982, Zawel et al., Genes Dev 1995, Goodrich et al., Cell 1994, Parvin et al., Cell 1993, Orphanides et al., Genes Dev 1996, Dvir et al., Proc Natl Acad Sci U S A 1997, Dvir et al., J Biol Chem 1997, Holstege et al., EMBO J 1997, Yamada-Okabe et al., Nucleic Acids Res 1998, Tsukamoto et al., Biochem Biophys Res Commun 1998
-
Reactome Reaction:
POLR2E
→
ERCC3
(indirect_complex)
Fiedler et al., Nucleic Acids Res 2001, Pal et al., Mol Cell Biol 2001, Kugel et al., Mol Cell Biol 2002, Yuan et al., EMBO Rep 2002, Conaway et al., J Biol Chem 1988, Zawel et al., Genes Dev 1995, Orphanides et al., Genes Dev 1996, Dvir et al., J Biol Chem 1997, Holstege et al., EMBO J 1997
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Yamamoto et al., Mol Cell Biol 2001
:
Here we demonstrate for the first time that
TFIIH mediated phosphorylation of
RNA polymerase II (Pol II) is essential for the transition to elongation
Giglia-Mari et al., PLoS Biol 2006
:
Transcription/repair factor IIH (TFIIH) is
essential for
RNA polymerase II transcription and nucleotide excision repair ( NER )
Dvir et al., J Biol Chem 1996
:
A
role for ATP and
TFIIH in activation of the
RNA polymerase II preinitiation complex prior to transcription initiation
Dvir et al., Proc Natl Acad Sci U S A 1997
:
In this report, we present direct evidence that
TFIIH also
controls RNA polymerase II activity at a postinitiation stage of transcription, by preventing premature arrest by very early elongation complexes just prior to their transition to stably elongating complexes