| + |
TFIIH | up-regulates 
phosphorylation
|
ESR1 |
0.308 |
| 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 | down-regulates quantity by destabilization 
phosphorylation
|
POLR2A |
0.73 |
| 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 activity
phosphorylation
|
POLR2A |
0.73 |
| 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 | 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 |
0.313 |
| 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 |
0.313 |
| 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 |
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#0 /home/prisca/signor/relation_result.php(2084): implode()
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4.0
TFIIH
CPX-2395