◀ Back to ERCC2
CCNH — ERCC2
Pathways - manually collected, often from reviews:
-
Reactome Reaction:
ERCC2
→
CCNH
(reaction)
Tirode et al., Mol Cell 1999, Wood et al., Biochimie 1999, Fiedler et al., Bioessays 2000, Wang et al., Science 1992, Bunick et al., Cell 1982, Goodrich et al., Cell 1994, Parvin et al., Cell 1993, Orphanides et al., Genes Dev 1996, Holstege et al., EMBO J 1997, Yamada-Okabe et al., Nucleic Acids Res 1998, Tsukamoto et al., Biochem Biophys Res Commun 1998
-
Reactome Reaction:
ERCC2
→
CCNH
(indirect_complex)
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
CCNH
—
ERCC2
(colocalization, biochemical)
Havugimana et al., Cell 2012
-
IRef Biogrid Interaction:
CCNH
—
ERCC2
(physical association, affinity chromatography technology)
Drapkin et al., Proc Natl Acad Sci U S A 1996
-
MIPS CORUM TFIIH transcription factor complex:
TFIIH transcription factor complex complex (CCNH-CDK7-ERCC2-ERCC3-GTF2H1-GTF2H2-GTF2H3-GTF2H4-GTF2H5-MNAT1)
Giglia-Mari et al., Nat Genet 2004
-
MIPS CORUM TFIIH transcription factor complex:
TFIIH transcription factor complex complex (CCNH-CDK7-ERCC2-ERCC3-GTF2H1-GTF2H2-GTF2H3-GTF2H4-GTF2H5-MNAT1)
Drapkin et al., Proc Natl Acad Sci U S A 1996
-
MIPS CORUM CAK-ERCC2 complex:
CAK-ERCC2 complex complex (CCNH-CDK7-ERCC2-MNAT1)
Drapkin et al., Proc Natl Acad Sci U S A 1996
-
MIPS CORUM TFIIH transcription factor complex:
TFIIH transcription factor complex complex (CCNH-CDK7-ERCC2-ERCC3-GTF2H1-GTF2H2-GTF2H3-GTF2H4-MNAT1)
Marinoni et al., EMBO J 1997
-
MIPS CORUM TFIIH transcription factor complex:
TFIIH transcription factor complex complex (CCNH-CDK7-ERCC2-ERCC3-GTF2H1-GTF2H2-GTF2H3-GTF2H4-MNAT1)
Kershnar et al., J Biol Chem 1998
-
MIPS CORUM ERCC2/CAK complex:
ERCC2/CAK complex complex (CCNH-CDK7-ERCC2-MNAT1)
Reardon et al., Proc Natl Acad Sci U S A 1996
-
MIPS CORUM TFIIH transcription factor complex (ERCC2, ERCC3, GTF2H1, CDK7, CCNH, GTF2H2):
TFIIH transcription factor complex (ERCC2, ERCC3, GTF2H1, CDK7, CCNH, GTF2H2) complex (CCNH-CDK7-ERCC2-ERCC3-GTF2H1-GTF2H2)
Dubaele et al., Mol Cell 2003
-
IRef Corum Interaction:
Complex of 21 proteins
(association, cosedimentation through density gradient)
Reardon et al., Proc Natl Acad Sci U S A 1996
-
IRef Corum Interaction:
Complex of 19 proteins
(association, chromatography technology)
Marinoni et al., EMBO J 1997
-
IRef Corum Interaction:
Complex of 13 proteins
(association, coimmunoprecipitation)
Dubaele et al., Mol Cell 2003
-
IRef Corum Interaction:
Complex of 31 proteins
(association, chromatography technology)
Drapkin et al., Proc Natl Acad Sci U S A 1996
-
IRef Dip Interaction:
Complex of ERCC3-ERCC2-GTF2H1-GTF2H2-CCNH-GTF2H4
(anti bait coimmunoprecipitation)
Kainov et al., Nature structural & molecular biology 2008
-
IRef Hprd Interaction:
Complex of 37 proteins
(in vivo)
Reardon et al., Proc Natl Acad Sci U S A 1996, Drapkin et al., Proc Natl Acad Sci U S A 1996
-
IRef Hprd Interaction:
Complex of 17 proteins
(in vivo)
Drapkin et al., Proc Natl Acad Sci U S A 1996
-
IRef Hprd Interaction:
Complex of 82 proteins
(in vivo)
Drapkin et al., Proc Natl Acad Sci U S A 1996
-
IRef Hprd Interaction:
Complex of 101 proteins
(in vivo)
Giglia-Mari et al., Nat Genet 2004
-
IRef Intact Interaction:
Complex of 15 proteins
(association, tandem affinity purification)
Varjosalo et al., Cell reports 2013
-
IRef Ophid Interaction:
CCNH
—
ERCC2
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Chen et al., Mol Cell Biol 1999
:
Recent reports have shown that Tat can also interact with the multisubunit transcription factor
TFIIH complex and
increase the phosphorylation of
CTD by the Cdk activating kinase (CAK) complex associated with the core TFIIH
Vandel et al., EMBO J 1999
:
We demonstrate that
TFIIH is
responsible for the
E2F-1 phosphorylation observed in cell extracts and that endogenous E2F-1 interacts in vivo with p62, a component of TFIIH, during S phase ... These results suggest that
TFIIH mediated phosphorylation of
E2F-1 plays a role in triggering E2F-1 degradation during S phase
Sakurai et al., Biochem Biophys Res Commun 1999
:
In the transcription process,
TFIIE regulates
TFIIH kinase activity that phosphorylates the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II
Kim et al., Mol Cell Biol 1999
:
We showed that hnRNP U can bind
TFIIH in vivo under certain conditions and
inhibit TFIIH mediated
CTD phosphorylation in vitro ... The abilities of hnRNP U to inhibit
TFIIH mediated
CTD phosphorylation and its Pol II association are necessary for hnRNP U to mediate the repression of Pol II elongation ... Based on these observations, we suggest that a subfraction of hnRNP U, as a component of the Pol II holoenzyme, may downregulate
TFIIH mediated
CTD phosphorylation in the basal transcription machinery and repress Pol II elongation
Spåhr et al., J Biol Chem 2000
:
This stimulation was species-specific, because S. pombe
Mediator could not
stimulate TFIIH purified from S. cerevisiae
Yokoi et al., J Biol Chem 2000
:
Interestingly, association of
TFIIH with DNA was observed in both wild-type and XP-A cell extracts but not in XP-C cell extracts, and
XPC-HR23B could
restore the association of TFIIH with DNA in XP-C cell extracts ... Interestingly, association of
TFIIH with DNA was observed in both wild-type and XP-A cell extracts but not in XP-C cell extracts, and
XPC-HR23B could
restore the association of TFIIH with DNA in XP-C cell extracts ... Moreover, we found that
XPC-HR23B was
necessary for efficient association of
TFIIH with damaged DNA in cell-free extracts ... Moreover, we found that
XPC-HR23B was
necessary for efficient association of
TFIIH with damaged DNA in cell-free extracts
Watanabe et al., Genes Cells 2000
:
In addition,
TFIIH phosphorylation of PolII was
stimulated by
TFIIE both in solution and during preinitiation complex formation, whereas Cdk7/Cyclin H and CAK phosphorylation of PolII was not
Wada et al., Mol Cell 2000
:
We find that the kinase activity of TFIIH is dispensable for this activity, demonstrating that
TFIIH mediated
CTD phosphorylation is not involved in the regulation of FACT and DSIF/NELF activities
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
Winkler et al., Biochemistry 2001
:
Furthermore, we reveal that
TFIIH inhibits the structure-specific endonuclease activities of both XPG and
ERCC1-XPF , responsible for the 3 ' and 5 ' incision in NER, respectively ... Furthermore, we reveal that
TFIIH inhibits the structure-specific endonuclease activities of both XPG and
ERCC1-XPF , responsible for the 3 ' and 5 ' incision in NER, respectively
Zhou et al., J Biol Chem 2001
:
TFIIH inhibits
CDK9 phosphorylation during human immunodeficiency virus type 1 transcription ... The presence of
TFIIH in the HIV-1 preinitiation complex
inhibits CDK9 phosphorylation
Braddock et al., Nature 2002
:
FBP bound to FUSE
acts through
TFIIH at the promoter
Brabazon et al., Biochim Biophys Acta 2002
:
Cyclin dependent kinase 8 (cdk8) regulates transcription by phosphorylating RNA polymerase II and
TFIIH
Sakurai et al., Genes Cells 2003
:
By using a chromatin immunoprecipitation technique, we found that
TFIIE is
necessary for stable binding of
TFIIH and RNAPII to the ADH1 promoter, whose activation requires TFIIE ... However, binding of
TFIIH and RNAPII to CUP1 upon its activation did not
require TFIIE
Chen et al., Nature 2003
:
Excess Xpd titrates CAK activity, resulting in decreased Cdk T-loop phosphorylation, mitotic defects and lethality, whereas a decrease in
Xpd results in increased
CAK activity and cell proliferation
Zurita et al., Trends Genet 2003
:
Interpretation of the phenotypes produced by mutations in TFIIH is complicated by the recent finding that
TFIIH plays a role in RNA polymerase I ( RNA
Pol I ) -mediated transcription
Mason et al., Mol Cell Biol 2003
:
In Saccharomyces cerevisiae cells,
FACT specifically associates with active Pol II genes in a
TFIIH dependent manner and travels across the gene with elongating Pol II
Guidi et al., J Biol Chem 2004
:
Mediator does not stimulate the activity of several other CTD kinases, suggesting that the specific enhancement of
TFIIH kinase activity
results in
Kin28 being the primary CTD kinase at initiation
Fukuda et al., Mol Cell Biol 2004
:
Furthermore, PC4 displayed physical interactions with both
TFIIH and GAL4-VP16 through its coactivator domain, and these interactions were
regulated distinctly by
PC4 phosphorylation
Drané et al., Mol Cell 2004
:
Selective
regulation of
vitamin D receptor-responsive genes by
TFIIH
Brondani et al., Biochem Biophys Res Commun 2005
:
The transcription factor
TFIIH mediates phosphorylation of the
retinoic acid receptor alpha (RARalpha) at position Ser77
Giglia-Mari et al., PLoS Biol 2006
:
Transcription/repair factor IIH (TFIIH) is
essential for
RNA polymerase II transcription and nucleotide excision repair ( NER )
Kim et al., EMBO J 2006
:
Upon
stimulation of the cells by
TNF-alpha , NF-kappaB and
TFIIH are rapidly recruited to the promoter together with additional Mediator and RNAP II, but CDK8 is lost
Okuda et al., EMBO J 2008
:
Among the GTFs,
TFIIE recruits TFIIH to complete the PIC formation and
regulates enzymatic activities of
TFIIH
Bruck et al., EMBO J 2009
:
We demonstrate that
MSK1 phosphorylates RARalpha at S369 located in the ligand binding domain,
allowing the binding of
TFIIH and thereby phosphorylation of the N-terminal domain at S77 by cdk7/cyclin H ... We demonstrate that MSK1 phosphorylates
RARalpha at S369 located in the ligand binding domain,
allowing the binding of
TFIIH and thereby phosphorylation of the N-terminal domain at S77 by cdk7/cyclin H ... Finally, the phosphorylation cascade initiated by MSK1 controls the recruitment of
RARalpha/TFIIH complexes to response elements and subsequently
RARalpha target gene
activation
Ohkuma et al., Mol Cell Biol 1995
:
The general transcription factor TFIIE recruits TFIIH at a late stage of transcription initiation complex formation and markedly stimulates
TFIIH dependent phosphorylation of the
carboxy-terminal domain (CTD) of RNA polymerase II ... To study this function of TFIIE in more detail, systematic deletion mutations were introduced into the large subunit of TFIIE ( TFIIE-alpha ) and were analyzed with regard to their effects on
TFIIH dependent
CTD phosphorylation, TFIIE dependent basal and enhancer dependent transcription, and interactions of TFIIE-alpha with both TFIIE-beta and TFIIH
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
Drapkin et al., Proc Natl Acad Sci U S A 1996
:
We present evidence proposing a critical
role for
ERCC2 in mediating the association of
CAK with core TFIIH subunits ... We present evidence proposing a critical
role for
ERCC2 in mediating the association of CAK with core
TFIIH subunits
Parada et al., Nature 1996
:
Here we show that Tat enhanced
HIV-1 transcription in vitro
requires both
TFIIH and the CTD of Pol II ... Under conditions that jointly restrict transcriptional elongation and
TFIIH mediated
CTD phosphorylation, Tat stimulates both these activities ... Thus, stimulation of Pol II elongation by Tat may involve direct effects on
TFIIH mediated
CTD phosphorylation
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
Yokomori et al., Proc Natl Acad Sci U S A 1998
:
These studies suggest an alternative PIC assembly pathway in which
TFIIE affects both TBP and
TFIIH functions during initiation of RNA synthesis
Okamoto et al., J Biol Chem 1998
:
In addition, we analyzed the effects of the TFIIEbeta deletion mutations on
TFIIH dependent phosphorylation of the C-terminal domain of RNA polymerase II and on wild type
TFIIEbeta-driven basal transcription