| + |
TFIIH | up-regulates 
phosphorylation
|
ESR1 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269356 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 10949034 |
Activation of estrogen receptor alpha by s118 phosphorylation involves a ligand-dependent interaction with tfiih and participation of cdk7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFIIH | up-regulates activity
phosphorylation
|
POLR2A |
0.727 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269382 |
Ser1619 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269379 |
Ser1626 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269370 |
Ser1647 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269369 |
Ser1654 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269364 |
Ser1668 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269374 |
Ser1675 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269373 |
Ser1696 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269384 |
Ser1717 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269365 |
Ser1724 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269371 |
Ser1738 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269381 |
Ser1766 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269367 |
Ser1787 |
SPNYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269385 |
Ser1864 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269368 |
Ser1871 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269380 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269377 |
Ser1892 |
TPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269378 |
Ser1899 |
SPTYSPTsPVYTPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269376 |
Ser1913 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269366 |
Ser1920 |
SPTYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269375 |
Ser1927 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269386 |
Ser1934 |
SPTYSPTsPKGSTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269383 |
Ser1944 |
GSTYSPTsPGYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269372 |
Ser1951 |
SPGYSPTsPTYSLTS |
Homo sapiens |
|
| pmid |
sentence |
| 24746699 |
After PIC formation, Pol II initiates mRNA synthesis, but productive transcription requires Pol II to escape from the PIC and transit into transcription elongation. The transition between initiation and elongation is associated with phosphorylation at the serine 5 (Ser5) residues within the hepta-peptide repeats in the C-terminal domain (CTD) of the largest Pol II subunit. Ser5 phosphorylation is mediated primarily by Kin28, the kinase subunit of the general transcription factor TFIIH |
|
| Publications: |
23 |
Organism: |
Homo Sapiens |
| Pathways: | Transcription initiation |
| + |
TFIIH | down-regulates quantity by destabilization 
phosphorylation
|
POLR2A |
0.727 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269351 |
Ser1619 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269348 |
Ser1626 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269339 |
Ser1647 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269338 |
Ser1654 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269333 |
Ser1668 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269343 |
Ser1675 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269342 |
Ser1696 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269357 |
Ser1717 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269334 |
Ser1724 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269340 |
Ser1738 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269350 |
Ser1766 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269336 |
Ser1787 |
SPNYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269358 |
Ser1864 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269337 |
Ser1871 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269349 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269346 |
Ser1892 |
TPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269347 |
Ser1899 |
SPTYSPTsPVYTPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269345 |
Ser1913 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269335 |
Ser1920 |
SPTYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269344 |
Ser1927 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269359 |
Ser1934 |
SPTYSPTsPKGSTYS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269352 |
Ser1944 |
GSTYSPTsPGYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269341 |
Ser1951 |
SPGYSPTsPTYSLTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Publications: |
23 |
Organism: |
Homo Sapiens |
| Pathways: | Transcription initiation |
| + |
TFIIH | up-regulates
phosphorylation
|
NR5A1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269355 |
Ser203 |
EYPEPYAsPPQPGLP |
Homo sapiens |
|
| pmid |
sentence |
| 17901130 |
In conclusion, our results indicate that cdk7, as part of the cak complex and tfiih, phosphorylates sf1 at s203 followed by increased transcriptional activity of sf1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFIIH | down-regulates
phosphorylation
|
E2F1 |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269353 |
Ser403 |
PEEFISLsPPHEALD |
Homo sapiens |
|
| pmid |
sentence |
| 10428966 |
These results suggest that tfiih-mediated phosphorylation of e2f-1 plays a role in triggering e2f-1 degradation during s phase. here we show that the e2f-1 activation domain interacts with a kinase activity which phosphorylates two sites, ser403 and thr433, within the activation domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269354 |
Thr433 |
DCDFGDLtPLDF |
Homo sapiens |
|
| pmid |
sentence |
| 10428966 |
These results suggest that tfiih-mediated phosphorylation of e2f-1 plays a role in triggering e2f-1 degradation during s phase. here we show that the e2f-1 activation domain interacts with a kinase activity which phosphorylates two sites, ser403 and thr433, within the activation domain. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TFIIH | down-regulates
phosphorylation
|
AR |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269331 |
Ser516 |
VSRVPYPsPTCVKSE |
Homo sapiens |
|
| pmid |
sentence |
| 21157430 |
Here, we show that the transcription factor tfiih, via its cdk7 kinase, phosphorylates the androgen receptor (ar) at position ar/s515. Strikingly, this phosphorylation is a key step for an accurate transactivation that includes the cyclic recruitment of the transcription machinery, the mdm2 e3 ligase, the subsequent ubiquitination of ar at the promoter of target genes and its degradation by the proteasome machinery |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFIIH |
phosphorylation
|
RARA |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269332 |
Ser77 |
EIVPSPPsPPPLPRI |
Homo sapiens |
|
| pmid |
sentence |
| 11955452 |
Thus, we demonstrate that the cdk7 kinase of tfiih phosphorylates the nuclear receptor, then allowing ligand-dependent control of the activation of the hormone-responsive genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GTF2H2C | form complex 
binding
|
TFIIH |
0.716 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269317 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAD23B | up-regulates activity
binding
|
TFIIH |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275696 |
|
|
|
|
| pmid |
sentence |
| 24086043 |
GG-NER is initiated by the GG-NER specific factor XPC-RAD23B, in some cases with the help of UV-DDB (UV-damaged DNA-binding protein). TC-NER is initiated by RNA polymerase stalled at a lesion with the help of TC-NER specific factors CSA, CSB, and XAB2. Both pathways require the core NER factors to complete the excision process|The core NER dual incision reaction has been reconstituted in vitro with purified factors using XPC-RAD23B, TFIIH, XPA, RPA, XPG, and ERCC1-XPF (Aboussekhra et al. 1995; Mu et al. 1995; Araujo et al. 2000).|The core NER dual incision reaction has been reconstituted in vitro with purified factors using XPC-RAD23B, TFIIH, XPA, RPA, XPG, and ERCC1-XPF (Aboussekhra et al. 1995; Mu et al. 1995; Araujo et al. 2000). Functional studies revealed that XPC-RAD23B is the initial damage recognition factor in this system, as the presence of XPC-RAD23B is required for assembly of the other core NER factors and progression through the NER pathway both in vitro and in vivo |
|
| Publications: |
1 |
| + |
TFIIE | up-regulates activity
relocalization
|
TFIIH |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269363 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31064989 |
The heterodimer TFIIE (composed of the TFIIEα and TFIIEβ subunits) seems to play a pivotal role in transcription by directly influencing the transition from initiation to elongation3,4. TFIIE interacts with different factors within the PIC, including Pol II5,6 as well as with DNA immediately upstream of the transcription bubble region7,8. Furthermore, TFIIE seems to influence TFIIH activity9, although it is not clear how this molecular process can occur. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269362 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31064989 |
The heterodimer TFIIE (composed of the TFIIEα and TFIIEβ subunits) seems to play a pivotal role in transcription by directly influencing the transition from initiation to elongation3,4. TFIIE interacts with different factors within the PIC, including Pol II5,6 as well as with DNA immediately upstream of the transcription bubble region7,8. Furthermore, TFIIE seems to influence TFIIH activity9, although it is not clear how this molecular process can occur. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Transcription initiation |
| + |
GTF2H5 | form complex
binding
|
TFIIH |
0.875 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269310 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERCC3 | form complex
binding
|
TFIIH |
0.89 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GTF2H3 | form complex
binding
|
TFIIH |
0.905 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269314 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERCC2 | form complex
binding
|
TFIIH |
0.869 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269312 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GTF2H1 | form complex
binding
|
TFIIH |
0.905 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269316 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFIIH | up-regulates 
|
Nucleotide-excision_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269322 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFIIH | up-regulates
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269323 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GTF2H2 | form complex
binding
|
TFIIH |
0.867 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269311 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAK complex | form complex
binding
|
TFIIH |
0.847 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269318 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GTF2H4 | form complex
binding
|
TFIIH |
0.911 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269315 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
TFIIH
CPX-2395