| + |
CyclinK/CDK12 | up-regulates activity 
phosphorylation
|
POLR2A |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273104 |
Ser1616 |
TPQSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273097 |
Ser1623 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273092 |
Ser1644 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273090 |
Ser1651 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273091 |
Ser1665 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273096 |
Ser1672 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273095 |
Ser1693 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273094 |
Ser1714 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273098 |
Ser1721 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273093 |
Ser1735 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273108 |
Ser1763 |
TPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273107 |
Ser1784 |
TPTSPNYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273105 |
Ser1861 |
TPTSPKYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273087 |
Ser1868 |
SPTSPKYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273089 |
Ser1875 |
SPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273085 |
Ser1878 |
SPKYSPTsPTYSPTT |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273102 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273103 |
Ser1889 |
SPTTPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273101 |
Ser1896 |
SPTSPTYsPTSPVYT |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273106 |
Ser1910 |
TPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273100 |
Ser1917 |
SPTSPTYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273088 |
Ser1924 |
SPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273099 |
Ser1931 |
SPTSPTYsPTSPKGS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273084 |
Ser1941 |
SPKGSTYsPTSPGYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273086 |
Ser1948 |
SPTSPGYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Publications: |
25 |
Organism: |
Homo Sapiens |
| + |
RPAP2 | up-regulates activity
dephosphorylation
|
POLR2A |
0.727 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248734 |
Ser1616 |
TPQSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248735 |
Ser1619 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248747 |
Ser1623 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248736 |
Ser1626 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248748 |
Ser1644 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248737 |
Ser1647 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248749 |
Ser1651 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248738 |
Ser1654 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248750 |
Ser1665 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248739 |
Ser1668 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248751 |
Ser1672 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248740 |
Ser1675 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248752 |
Ser1693 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248741 |
Ser1696 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248753 |
Ser1714 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248742 |
Ser1717 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248754 |
Ser1721 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248743 |
Ser1724 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248755 |
Ser1735 |
SPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248744 |
Ser1738 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248756 |
Ser1763 |
TPTSPSYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248745 |
Ser1766 |
SPSYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248757 |
Ser1784 |
TPTSPNYsPTSPSYS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248746 |
Ser1787 |
SPNYSPTsPSYSPTS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 22137580 |
In addition, we show that RPAP2 is a CTD Ser5 phosphatase. Taken together, our results indicate that during transcription of snRNA genes, Ser7 phosphorylation facilitates recruitment of RPAP2, which in turn both recruits Integrator and dephosphorylates Ser5.|The Pol II CTD is first phosphorylated on Ser5 and then on Ser7 by CDK7. RPAP2 associates with the Pol II CTD after Ser7 phosphorylation and tethers a subcomplex of Integrator to snRNA genes. RPAP2 dephosphorylates Ser5P of the CTD, facilitating transcription and the subsequent recruitment of the Int11 catalytic subunit of Integrator |
|
| Publications: |
24 |
Organism: |
Homo Sapiens |
| + |
CyclinK/CDK13 | up-regulates activity
phosphorylation
|
POLR2A |
0.636 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273079 |
Ser1616 |
TPQSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273072 |
Ser1623 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273067 |
Ser1644 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273065 |
Ser1651 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273066 |
Ser1665 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273071 |
Ser1672 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273070 |
Ser1693 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273069 |
Ser1714 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273073 |
Ser1721 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273068 |
Ser1735 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273083 |
Ser1763 |
TPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273082 |
Ser1784 |
TPTSPNYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273080 |
Ser1861 |
TPTSPKYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273062 |
Ser1868 |
SPTSPKYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273064 |
Ser1875 |
SPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273060 |
Ser1878 |
SPKYSPTsPTYSPTT |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273077 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273078 |
Ser1889 |
SPTTPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273076 |
Ser1896 |
SPTSPTYsPTSPVYT |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273081 |
Ser1910 |
TPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273075 |
Ser1917 |
SPTSPTYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273063 |
Ser1924 |
SPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273074 |
Ser1931 |
SPTSPTYsPTSPKGS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273059 |
Ser1941 |
SPKGSTYsPTSPGYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273061 |
Ser1948 |
SPTSPGYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Publications: |
25 |
Organism: |
Homo Sapiens |
| + |
SSU72 | up-regulates activity
dephosphorylation
|
POLR2A |
0.849 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248803 |
Ser1616 |
TPQSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248804 |
Ser1619 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248816 |
Ser1623 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248805 |
Ser1626 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248817 |
Ser1644 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248806 |
Ser1647 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248818 |
Ser1651 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248807 |
Ser1654 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248819 |
Ser1665 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248808 |
Ser1668 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248820 |
Ser1672 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248809 |
Ser1675 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248821 |
Ser1693 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248810 |
Ser1696 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248822 |
Ser1714 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248811 |
Ser1717 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248823 |
Ser1721 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248812 |
Ser1724 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248824 |
Ser1735 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248813 |
Ser1738 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248825 |
Ser1763 |
TPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248814 |
Ser1766 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248826 |
Ser1784 |
TPTSPNYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248815 |
Ser1787 |
SPNYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 15125841 |
Phosphorylation of serine-2 (S2) and serine-5 (S5) of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates the transcription cycle and coordinates recruitment of RNA processing factors. The Fcp1 CTD phosphatase catalyzes dephosphorylation of S2-P.| Depletion of Ssu72 impairs transcription in vitro |
|
| Publications: |
24 |
Organism: |
In Vitro |
| + |
BRD4 | up-regulates
phosphorylation
|
POLR2A |
0.461 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197012 |
Ser1616 |
TPQSPSYsPTSPSYS |
Homo sapiens |
Breast Cancer Cell, Leukemia Cell, Lymphoma Cell |
| pmid |
sentence |
| 22509028 |
We report that brd4 is an atypical kinase that binds to the carboxyl-terminal domain (ctd) of rna polymerase ii and directly phosphorylates its serine 2 (ser2) sites both in vitro and in vivo under conditions where other ctd kinases are inactive. our findings may provide a mechanistic basis for several functional studies that showed that loss of brd4 causes transcription termination and embryonic lethality |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTDSP1 | up-regulates activity
dephosphorylation
|
POLR2A |
0.441 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248767 |
Ser1616 |
TPQSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 17157258 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248768 |
Ser1619 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248780 |
Ser1623 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248769 |
Ser1626 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248781 |
Ser1644 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248770 |
Ser1647 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248782 |
Ser1651 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248771 |
Ser1654 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248783 |
Ser1665 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248772 |
Ser1668 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248784 |
Ser1672 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248773 |
Ser1675 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248785 |
Ser1693 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248774 |
Ser1696 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248786 |
Ser1714 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248775 |
Ser1717 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248787 |
Ser1721 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248776 |
Ser1724 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248788 |
Ser1735 |
SPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248777 |
Ser1738 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248789 |
Ser1763 |
TPTSPSYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248778 |
Ser1766 |
SPSYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248790 |
Ser1784 |
TPTSPNYsPTSPSYS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248779 |
Ser1787 |
SPNYSPTsPSYSPTS |
in vitro |
|
| pmid |
sentence |
| 22137580 |
Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. | This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. |
|
| Publications: |
24 |
Organism: |
In Vitro |
| + |
CDK13 | up-regulates activity
phosphorylation
|
POLR2A |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273054 |
Ser1616 |
TPQSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273047 |
Ser1623 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273042 |
Ser1644 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273040 |
Ser1651 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273041 |
Ser1665 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273046 |
Ser1672 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273045 |
Ser1693 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273044 |
Ser1714 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273048 |
Ser1721 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273043 |
Ser1735 |
SPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273058 |
Ser1763 |
TPTSPSYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273057 |
Ser1784 |
TPTSPNYsPTSPSYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273055 |
Ser1861 |
TPTSPKYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273037 |
Ser1868 |
SPTSPKYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273039 |
Ser1875 |
SPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273035 |
Ser1878 |
SPKYSPTsPTYSPTT |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273052 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273053 |
Ser1889 |
SPTTPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273051 |
Ser1896 |
SPTSPTYsPTSPVYT |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273056 |
Ser1910 |
TPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273050 |
Ser1917 |
SPTSPTYsPTSPKYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273038 |
Ser1924 |
SPTSPKYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273049 |
Ser1931 |
SPTSPTYsPTSPKGS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273034 |
Ser1941 |
SPKGSTYsPTSPGYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273036 |
Ser1948 |
SPTSPGYsPTSPTYS |
Homo sapiens |
MV-4-11 Cell |
| pmid |
sentence |
| 32917631 |
Together, these studies demonstrate the important, yet largely redundant, role for CDK12 and CDK13 for the regulation of POLII CTD phosphorylation at multiple residues, as well as the global role for both of these kinases in regulating POLII occupancy across the genome.|CDK12 and CDK13 are thus evolutionarily related and structurally similar kinases, and biochemical assays have demonstrated that both have POLII C-terminal domain (CTD) kinase activity and the ability to phosphorylate the Ser2 residue of the repetitive CTD heptad sequence |
|
| Publications: |
25 |
Organism: |
Homo Sapiens |
| + |
CDK9 | up-regulates
phosphorylation
|
POLR2A |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203508 |
Ser1616 |
TPQSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203512 |
Ser1623 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203516 |
Ser1644 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203520 |
Ser1651 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203524 |
Ser1665 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203528 |
Ser1672 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203532 |
Ser1693 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203536 |
Ser1714 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203540 |
Ser1721 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203544 |
Ser1735 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203552 |
Ser1763 |
TPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203556 |
Ser1784 |
TPTSPNYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203560 |
Ser1861 |
TPTSPKYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203564 |
Ser1868 |
SPTSPKYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203568 |
Ser1875 |
SPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203576 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203580 |
Ser1889 |
SPTTPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203584 |
Ser1896 |
SPTSPTYsPTSPVYT |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203588 |
Ser1910 |
TPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203592 |
Ser1917 |
SPTSPTYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203596 |
Ser1924 |
SPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203600 |
Ser1931 |
SPTSPTYsPTSPKGS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203604 |
Ser1941 |
SPKGSTYsPTSPGYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203608 |
Ser1948 |
SPTSPGYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Publications: |
24 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates 
phosphorylation
|
POLR2A |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120084 |
Ser1619 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120088 |
Ser1626 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120092 |
Ser1647 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-119366 |
Ser1654 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120096 |
Ser1668 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120100 |
Ser1675 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120104 |
Ser1696 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120108 |
Ser1717 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120112 |
Ser1724 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120116 |
Ser1738 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120120 |
Ser1766 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120124 |
Ser1787 |
SPNYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120128 |
Ser1864 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120132 |
Ser1871 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120136 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120140 |
Ser1892 |
TPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120144 |
Ser1899 |
SPTYSPTsPVYTPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120148 |
Ser1913 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120152 |
Ser1920 |
SPTYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120156 |
Ser1927 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120160 |
Ser1934 |
SPTYSPTsPKGSTYS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120164 |
Ser1944 |
GSTYSPTsPGYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120168 |
Ser1951 |
SPGYSPTsPTYSLTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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 |
| + |
TFIIH | up-regulates activity
phosphorylation
|
POLR2A |
0.718 |
| 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 |
0.718 |
| 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 |
| + |
CDK7 | down-regulates
phosphorylation
|
POLR2A |
0.781 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119992 |
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-119996 |
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-120000 |
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-120004 |
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-120008 |
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-120012 |
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-120016 |
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-120020 |
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-120024 |
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-120028 |
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-120032 |
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-120036 |
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-120040 |
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-120044 |
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-120048 |
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-120052 |
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-120056 |
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-120060 |
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-120064 |
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-120068 |
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-120072 |
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-120076 |
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-120080 |
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 |
| + |
MAPK3 | down-regulates
phosphorylation
|
POLR2A |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120172 |
Ser1619 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120176 |
Ser1626 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120180 |
Ser1647 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120184 |
Ser1654 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120188 |
Ser1668 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120192 |
Ser1675 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120196 |
Ser1696 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120200 |
Ser1717 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120204 |
Ser1724 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120208 |
Ser1738 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120212 |
Ser1766 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120216 |
Ser1787 |
SPNYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120220 |
Ser1864 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120224 |
Ser1871 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120228 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120232 |
Ser1892 |
TPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120236 |
Ser1899 |
SPTYSPTsPVYTPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120240 |
Ser1913 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120244 |
Ser1920 |
SPTYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120248 |
Ser1927 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120252 |
Ser1934 |
SPTYSPTsPKGSTYS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120256 |
Ser1944 |
GSTYSPTsPGYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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-120260 |
Ser1951 |
SPGYSPTsPTYSLTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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 |
| + |
CDK12 | up-regulates
phosphorylation
|
POLR2A |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176793 |
Ser1861 |
TPTSPKYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176797 |
Ser1868 |
SPTSPKYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176801 |
Ser1875 |
SPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176809 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176813 |
Ser1889 |
SPTTPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176817 |
Ser1896 |
SPTSPTYsPTSPVYT |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176821 |
Ser1910 |
TPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176825 |
Ser1917 |
SPTSPTYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176829 |
Ser1924 |
SPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176833 |
Ser1931 |
SPTSPTYsPTSPKGS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176837 |
Ser1941 |
SPKGSTYsPTSPGYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176841 |
Ser1948 |
SPTSPGYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Publications: |
12 |
Organism: |
Homo Sapiens |
| + |
CDK9 | up-regulates activity
phosphorylation
|
POLR2A |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203572 |
Ser1878 |
SPKYSPTsPTYSPTT |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK12 | up-regulates activity
phosphorylation
|
POLR2A |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176805 |
Ser1878 |
SPKYSPTsPTYSPTT |
Homo sapiens |
|
| pmid |
sentence |
| 22012619 |
Cyck/cdk12 can activate transcription and phosphorylate ser2 in the ctd of rnapii / phosphorylation of serine at position 2 (ser2) is thought to be responsible for productive transcriptional elongation and synthesis of full-length mature mrna |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INTS4 | up-regulates activity
binding
|
POLR2A |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261185 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16239144 |
The Integrator Complex Can Directly Associate with the C-Terminal Domain of RNA Polymerase II Largest Subunit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POLR2A | form complex 
binding
|
RNA Polymerase II |
0.864 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266160 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9852112 |
Pol II is composed of 10–12 polypeptides ranging in size from 220 to 7 kDa, depending on the source of purification (11, 12, 13). The subunits of human pol II (or RNA polymerase B) have been defined as RPB1 (220 kDa), RPB2 (140 kDa), RPB3 (33 kDa), RPB4 (18 kDa), RPB5 (28 kDa), RPB6 (19 kDa), RPB7 (27 kDa), RPB8 (17 kDa), RPB9 (14.5 kDa), RPB10alpha (or RPB12, 7.0 kDa), RPB10beta (or RPB10, 7.6 kDa), and RPB11 (14 kDa) (3,11, 12, 13). RPB5, RPB6, RPB8, RPB10alpha, and RPB10beta are shared by all three eukaryotic RNA polymerases, whereas the rest of the RPB components are unique to pol II |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Transcription initiation |
| + |
ERK1/2 | down-regulates
phosphorylation
|
POLR2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270156 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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: |
1 |
Organism: |
Homo Sapiens |
| + |
TFIID | up-regulates activity
binding
|
POLR2A |
0.524 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263934 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27096372 |
Our structures suggest that a primary function of TFIID during PIC assembly is the proper positioning of TBP on the upstream promoter, which ultimately determines the placement of Pol II relative to the TSS. The structures presented here offer a structural framework for understanding the complex mechanism underlying TFIID function, shedding new light into the overlapping roles of TFIID as both a coactivator and a general platform for PIC assembly in the coordination of transcription initiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Transcription initiation |
| + |
PHF3 | down-regulates activity
binding
|
POLR2A |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266965 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 34667177 |
PHF3 interacts with RNA polymerase II through the SPOC domain. PHF3 negatively regulates mRNA levels. Here, we identify PHD-finger protein 3 (PHF3) as a regulator of transcription and mRNA stability that docks onto Pol II CTD through its SPOC domain. Our data suggest that PHF3 acts as a prominent effector of neuronal gene regulation by bridging transcription with mRNA decay. PHF3 SPOC preferentially binds RNA Pol II CTD phosphorylated on Serine-2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WWP2 | down-regulates quantity
ubiquitination
|
POLR2A |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268851 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 31048545 |
WWP2 ubiquitylates RNA polymerase II for DNA-PK-dependent transcription arrest and repair at DNA breaks|In response to DSBs, WWP2 targets the RNAPII subunit RPB1 for K48-linked ubiquitylation, thereby driving DNA-PK- and proteasome-dependent eviction of RNAPII. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
P-TEFb | up-regulates activity
phosphorylation
|
POLR2A |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261039 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32048991 |
Phosphorylation of Pol II CTD by positive transcription elongation factor b (P-TEFb) is a necessary precursor event that enables productive transcription elongation. To perform this task, Pol II needs to be activated by a complex of proteins called P-TEFb; however, P-TEFb is usually found in an inactive form held by another group of proteins. Yet, it is unclear how P-TEFb is released and allowed to activate Pol II. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POLR2A | up-regulates activity
relocalization
|
Integrator complex |
0.65 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261476 |
|
|
in vitro |
|
| pmid |
sentence |
| 20457598 |
The pol II CTD specifically mediates recruitment of Integrator to the promoter of snRNA genes to activate transcription and direct 3' end processing of the transcripts. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
Gbeta | down-regulates
phosphorylation
|
POLR2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270039 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Erk1/2 are major ser-5 kinases after h2o2 treatment. 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: |
1 |
Organism: |
Homo Sapiens |
3.0
POLR2A
- 
- 