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Literature summary extracted from

  • Heidemann, M.; Hintermair, C.; Voß, K.; Eick, D.
    Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription (2013), Biochim. Biophys. Acta, 1829, 55-62.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.11.23 chromatin
-
 Saccharomyces cerevisiae 785
-
2.7.11.23 chromatin
-
 Drosophila melanogaster 785
-
2.7.11.23 chromatin
-
 Schizosaccharomyces pombe 785
-
2.7.11.23 nucleus
-
 Saccharomyces cerevisiae 5634
-
2.7.11.23 nucleus
-
 Drosophila melanogaster 5634
-
2.7.11.23 nucleus
-
 Schizosaccharomyces pombe 5634
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.23 Mg2+ required Homo sapiens
2.7.11.23 Mg2+ required Saccharomyces cerevisiae
2.7.11.23 Mg2+ required Drosophila melanogaster
2.7.11.23 Mg2+ required Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Homo sapiens only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Also phosphorylation of threonine 4 and tyrosine 1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Drosophila melanogaster only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser-Pro3-Thr4-Ser5-Pro6-Ser7 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Saccharomyces cerevisiae only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Schizosaccharomyces pombe only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Drosophila melanogaster only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Saccharomyces cerevisiae only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1–Ser2–Pro3–Thr4–Ser5–Pro6–Ser7 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Schizosaccharomyces pombe ATCC 24843 only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 additional information Drosophila melanogaster dynamic changes in the CTD phosphorylation pattern due to a complex interplay of various kinases and phosphatases subsequently orchestrate the binding of CTD interacting proteins, cf. CTD code ?
-
 ?
2.7.11.23 additional information Schizosaccharomyces pombe dynamic changes in the CTD phosphorylation pattern due to a complex interplay of various kinases and phosphatases subsequently orchestrate the binding of CTD interacting proteins, cf. CTD code ?
-
 ?
2.7.11.23 additional information Saccharomyces cerevisiae the CTD differs in length dependent on the complexity of the organism. While Saccharomyces cerevisiae has 26 repeats, which nearly all obey the consensus sequence, mammalian CTD comprises 52. Dynamic changes in the CTD phosphorylation pattern due to a complex interplay of various kinases and phosphatases subsequently orchestrate the binding of CTD interacting proteins, cf. CTD code ?
-
 ?
2.7.11.23 additional information Schizosaccharomyces pombe ATCC 24843 dynamic changes in the CTD phosphorylation pattern due to a complex interplay of various kinases and phosphatases subsequently orchestrate the binding of CTD interacting proteins, cf. CTD code ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.23 Drosophila melanogaster Q24216
-
-
2.7.11.23 Drosophila melanogaster Q9VT57
-
-
2.7.11.23 Homo sapiens P49336 Cdk8
-
2.7.11.23 Homo sapiens P50613 cdk7
-
2.7.11.23 Homo sapiens P50750 cdk9
-
2.7.11.23 Homo sapiens Q9H4B4 Plk3
-
2.7.11.23 Saccharomyces cerevisiae P06242 Kin28
-
2.7.11.23 Saccharomyces cerevisiae P23293 Bur1
-
2.7.11.23 Saccharomyces cerevisiae P39073 Srb10
-
2.7.11.23 Saccharomyces cerevisiae Q03957 Ctk1
-
2.7.11.23 Schizosaccharomyces pombe O14098 Lsk1
-
2.7.11.23 Schizosaccharomyces pombe Q12126 Crk1/Mcs6
-
2.7.11.23 Schizosaccharomyces pombe Q96WV9 cdk9
-
2.7.11.23 Schizosaccharomyces pombe ATCC 24843 O14098 Lsk1
-
2.7.11.23 Schizosaccharomyces pombe ATCC 24843 Q12126 Crk1/Mcs6
-
2.7.11.23 Schizosaccharomyces pombe ATCC 24843 Q96WV9 cdk9
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.23 ATP + [DNA-directed RNA polymerase II] only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Also phosphorylation of threonine 4 and tyrosine 1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 Homo sapiens ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser-Pro3-Thr4-Ser5-Pro6-Ser7 Drosophila melanogaster ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 Saccharomyces cerevisiae ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 Schizosaccharomyces pombe ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 Drosophila melanogaster ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1–Ser2–Pro3–Thr4–Ser5–Pro6–Ser7 Saccharomyces cerevisiae ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Cdk9 phosphorylates Ser2. Phosphorylation of CTD-Tyr1 Homo sapiens ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] kinases Bur1 and Ctk1 phosphorylate Ser2 Saccharomyces cerevisiae ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] kinases Cdk9 and Lsk1 phosphorylate Ser2. Thr4 is also phosphorylated by a kinase Schizosaccharomyces pombe ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] Plk3 phosphorylates Thr4 in human cells. Phosphorylation of CTD-Tyr1 Homo sapiens ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] subunit Srb10 of the Mediator phosphorylates CTD Ser5 Saccharomyces cerevisiae ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] the cyclin-dependent kinase subunit Cdk7 of TFIIH phosphorylates Ser5 and Ser7 Drosophila melanogaster ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] the cyclin-dependent kinase subunit Cdk7 of TFIIH phosphorylates Ser5 and Ser7. Subunit Cdk8 of the Mediator also phosphorylates CTD Ser5. Phosphorylation of CTD-Tyr1 Homo sapiens ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] the cyclin-dependent kinase subunit Cdk8 of the Mediator phosphorylates CTD Ser5 Drosophila melanogaster ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] the cyclin-dependent kinase subunit Cdk8 of the Mediator phosphorylates CTD Ser5. Phosphorylation of CTD-Tyr1 Homo sapiens ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] the cyclin-dependent kinase subunit Kin28 of TFIIH phosphorylates Ser5 and Ser7 Saccharomyces cerevisiae ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] the cyclin-dependent kinase subunit Mcs6 of TFIIH phosphorylates Ser5 and Ser7 of the CTD early in the transcription cycle in a Mediator-dependent manner, which leads to the dissociation of Mediator. Thr4 is also phosphorylated by a kinase Schizosaccharomyces pombe ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] only Rpb1, the largest subunit of RNAPII evolved a unique, highly repetitive carboxy-terminal domain, termed CTD. Dynamic phosphorylation patterns of serine residues in the CTD during gene transcription. Phosphorylation of Ser2, Ser5, Thr4, and Tyr1 in the CTD. CTD is composed of multiple tandem heptapeptides with the evolutionary conserved consensus motif Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 Schizosaccharomyces pombe ATCC 24843 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] kinases Cdk9 and Lsk1 phosphorylate Ser2. Thr4 is also phosphorylated by a kinase Schizosaccharomyces pombe ATCC 24843 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 ATP + [DNA-directed RNA polymerase II] the cyclin-dependent kinase subunit Mcs6 of TFIIH phosphorylates Ser5 and Ser7 of the CTD early in the transcription cycle in a Mediator-dependent manner, which leads to the dissociation of Mediator. Thr4 is also phosphorylated by a kinase Schizosaccharomyces pombe ATCC 24843 ADP + phospho-[DNA-directed RNA polymerase II]
-
 ?
2.7.11.23 additional information dynamic changes in the CTD phosphorylation pattern due to a complex interplay of various kinases and phosphatases subsequently orchestrate the binding of CTD interacting proteins, cf. CTD code Drosophila melanogaster ?
-
 ?
2.7.11.23 additional information dynamic changes in the CTD phosphorylation pattern due to a complex interplay of various kinases and phosphatases subsequently orchestrate the binding of CTD interacting proteins, cf. CTD code Schizosaccharomyces pombe ?
-
 ?
2.7.11.23 additional information the CTD differs in length dependent on the complexity of the organism. While Saccharomyces cerevisiae has 26 repeats, which nearly all obey the consensus sequence, mammalian CTD comprises 52. Dynamic changes in the CTD phosphorylation pattern due to a complex interplay of various kinases and phosphatases subsequently orchestrate the binding of CTD interacting proteins, cf. CTD code Saccharomyces cerevisiae ?
-
 ?
2.7.11.23 additional information dynamic changes in the CTD phosphorylation pattern due to a complex interplay of various kinases and phosphatases subsequently orchestrate the binding of CTD interacting proteins, cf. CTD code Schizosaccharomyces pombe ATCC 24843 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.23 Bur1
-
 Saccharomyces cerevisiae
2.7.11.23 cdk7
-
 Homo sapiens
2.7.11.23 cdk7
-
 Drosophila melanogaster
2.7.11.23 CDK8
-
 Homo sapiens
2.7.11.23 CDK8
-
 Drosophila melanogaster
2.7.11.23 CDK9
-
 Homo sapiens
2.7.11.23 CDK9
-
 Schizosaccharomyces pombe
2.7.11.23 Crk1
-
 Schizosaccharomyces pombe
2.7.11.23 Ctk1
-
 Saccharomyces cerevisiae
2.7.11.23 Kin28
-
 Saccharomyces cerevisiae
2.7.11.23 Lsk1
-
 Schizosaccharomyces pombe
2.7.11.23 Mcs6
-
 Schizosaccharomyces pombe
2.7.11.23 mitotic catastrophe suppressor 6 UniProt Schizosaccharomyces pombe
2.7.11.23 Plk3
-
 Homo sapiens
2.7.11.23 Srb10
-
 Saccharomyces cerevisiae
2.7.11.23 TFIIH kinase
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.23 ATP
-
 Homo sapiens
2.7.11.23 ATP
-
 Saccharomyces cerevisiae
2.7.11.23 ATP
-
 Drosophila melanogaster
2.7.11.23 ATP
-
 Schizosaccharomyces pombe

General Information

EC Number General Information Comment Organism
2.7.11.23 malfunction mutation of Cdk7 phosphorylation site Ser7 in substrate RNAPII CTD is lethal to human cells Homo sapiens
2.7.11.23 malfunction mutation of Thr4 in substrate RNAPII CTD is lethal to human cells. Replacement of Thr4 to alanine leads to a global defect in RNA elongation while few genes become activated and show an enrichment of RNAPII within the gene body. Hypoxia leads to activation of Plk3 and concomitant increase of Thr4-P levels, while knockdown of Plk3 by RNA interference decreases Thr4-P levels in mammalian cells Homo sapiens
2.7.11.23 malfunction mutation of Thr4 in substrate RNAPII CTD is not lethal to fission yeast cells Schizosaccharomyces pombe
2.7.11.23 malfunction the lethality caused by the substitution of Ser5 to alanine in CTD can be circumvented by covalent tethering of mRNA capping enzymes to the CTD in fission yeast Saccharomyces cerevisiae
2.7.11.23 malfunction the lethality caused by the substitution of Ser5 to alanine in CTD can be circumvented by covalent tethering of mRNA capping enzymes to the CTD in fission yeast. Mutation of Kin28 phosphorylation site Ser7 in substrate RNAPII CTD is not lethal to yeast cells. The substitution of tyrosine 1 by phenylalanine is lethal in Saccharomyces cerevisiae, indicating an important functional role of this CTD residue Saccharomyces cerevisiae
2.7.11.23 malfunction the lethality caused by the substitution of Ser5 to alanine in CTD can be circumvented by covalent tethering of mRNA capping enzymes to the CTD in fission yeast. Mutation of Thr4 in substrate RNAPII CTD is not lethal to fission yeast cells Schizosaccharomyces pombe
2.7.11.23 physiological function CTD Ser2 phosphorylation (Ser2-P) rises downstream of the transcription start site (TSS) and concurs with the entry of RNAPII in the productive elongation phase of transcription. The recruitment of kinases during this step is Ser5-P dependent, either in a direct or indirect way Homo sapiens
2.7.11.23 physiological function CTD Ser2 phosphorylation (Ser2-P) rises downstream of the transcription start site (TSS) and concurs with the entry of RNAPII in the productive elongation phase of transcription. The recruitment of kinases during this step is Ser5-P dependent, either in a direct or indirect way. Two enzymes share the job to phosphorylate Ser2: Bur1, which is recruited directly to RNAPII by Ser5-P, and Ctk1 Saccharomyces cerevisiae
2.7.11.23 physiological function the cyclin-dependent kinase subunit Cdk7 of TFIIH phosphorylates Ser5 and Ser7 of the CTD early in the transcription cycle in a Mediator-dependent manner, which leads to the dissociation of Mediator. Subunit Cdk8 of the Mediator also phosphorylates CTD Ser5. The histone methyltransferase Set1, which trimethylates histone H3 lysine 4, a specific tag for epigenetic transcriptional activation, interacts with RNAP II dependent on CTD-Ser5-P and recruitment of Rpd3C(S), a histone H3 and H4 deacetylase, is also stimulated by Ser5-P. CTD Ser2 phosphorylation (Ser2-P) rises downstream of the transcription start site (TSS) and concurs with the entry of RNAPII in the productive elongation phase of transcription. The recruitment of kinases during this step is Ser5-P dependent, either in a direct or indirect way Drosophila melanogaster
2.7.11.23 physiological function the cyclin-dependent kinase subunit Cdk7 of TFIIH phosphorylates Ser5 and Ser7 of the CTD early in the transcription cycle in a Mediator-dependent manner, which leads to the dissociation of Mediator. Subunit Cdk8 of the Mediator also phosphorylates CTD Ser5. The histone methyltransferase Set1, which trimethylates histone H3 lysine 4, a specific tag for epigenetic transcriptional activation, interacts with RNAP II dependent on CTD-Ser5-P and recruitment of Rpd3C(S), a histone H3 and H4 deacetylase, is also stimulated by Ser5-P. CTD Ser2 phosphorylation (Ser2-P) rises downstream of the transcription start site (TSS) and concurs with the entry of RNAPII in the productive elongation phase of transcription. The recruitment of kinases during this step is Ser5-P dependent, either in a direct or indirect way. In protein-coding genes the Ser7-P is placed early in transcription, similar to Ser5-P, but its levels remain stable until the polyadenylation site Homo sapiens
2.7.11.23 physiological function the cyclin-dependent kinase subunit Cdk7 of TFIIH phosphorylates Ser5 and Ser7 of the CTD early in the transcription cycle in a Mediator-dependent manner, which leads to the dissociation of Mediator. Subunit Cdk8 of the Mediator also phosphorylates CTD Ser5. The histone methyltransferase Set1, which trimethylates histone H3 lysine 4, a specific tag for epigenetic transcriptional activation, interacts with RNAP II dependent on CTD-Ser5-P and recruitment of Rpd3C(S), a histone H3 and H4 deacetylase, is also stimulated by Ser5-P. The recruitment of kinases during entry of RNAPII in the productive elongation phase of transcription is Ser5-P dependent, either in a direct or indirect way. In protein-coding genes the Ser7-P is placed early in transcription, similar to Ser5-P, but its levels remain stable until the polyadenylation site. Cdk7, the CTD-Ser5-kinase, is also the primary kinase for Ser7 phosphorylation in human cells Homo sapiens
2.7.11.23 physiological function the placement of the 7-methyl-guanosine cap on the 5' end of newly synthesized transcripts is phospho-CTD-dependent. Recruitment of the capping machinery is a main function of Ser5-P. Other protein interactions require the Ser5-P as well Schizosaccharomyces pombe
2.7.11.23 physiological function the placement of the 7-methyl-guanosine cap on the 5' end of newly synthesized transcripts is phospho-CTD-dependent. Recruitment of the capping machinery is a main function of Ser5-P. Other protein interactions require the Ser5-P as well. Nrd1, a factor involved in the 3' end formation and early termination of non-polyadenylated transcripts, interacts with CTD in a Ser5-P dependent manner in Saccharomyces cerevisiae. The cyclin-dependent kinase subunit Cdk7 of TFIIH phosphorylates Ser5 and Ser7 of the CTD early in the transcription cycle in a Mediator-dependent manner, which leads to the dissociation of Mediator. Subunit Srb10 of the Mediator also phosphorylates CTD Ser5. The histone methyltransferase Set1, which trimethylates histone H3 lysine 4, a specific tag for epigenetic transcriptional activation, interacts with RNAP II dependent on CTD-Ser5-P and recruitment of Rpd3C(S), a histone H3 and H4 deacetylase, is also stimulated by Ser5-P Saccharomyces cerevisiae
2.7.11.23 physiological function the placement of the 7-methyl-guanosine cap on the 5' end of newly synthesized transcripts is phospho-CTD-dependent. Recruitment of the capping machinery is a main function of Ser5-P. Other protein interactions require the Ser5-P as well. Nrd1, a factor involved in the 3' end formation and early termination of non-polyadenylated transcripts, interacts with CTD in a Ser5-P dependent manner in Saccharomyces cerevisiae. The cyclin-dependent kinase subunit Cdk7 of TFIIH phosphorylates Ser5 and Ser7 of the CTD early in the transcription cycle in a Mediator-dependent manner, which leads to the dissociation of Mediator. Subunit Srb10 of the Mediator also phosphorylates CTD Ser5. The histone methyltransferase Set1, which trimethylates histone H3 lysine 4, a specific tag for epigenetic transcriptional activation, interacts with RNAP II dependent on CTD-Ser5-P and recruitment of Rpd3C(S), a histone H3 and H4 deacetylase, is also stimulated by Ser5-P. Kin28, the CTD-Ser5-kinase, is also the primary kinase for Ser7 phosphorylation in yeast cells. Phosphorylation of Tyr1 in CTD occurs at all active genes in the yeast genome Saccharomyces cerevisiae
2.7.11.23 physiological function two enzymes share the job to phosphorylate Ser2: Bur1 orthologue Cdk9, which is directed to the transcription machinery by the Ser5-P dependent capping enzyme, and Lsk1, which is responsible for the majority of Ser2-P Schizosaccharomyces pombe
2.7.11.23 physiological function two enzymes share the job to phosphorylate Ser2: Bur1 orthologue Cdk9, which is directed to the transcription machinery by the Ser5-P dependent capping enzyme, and Lsk1,which is responsible for the majority of Ser2-P Schizosaccharomyces pombe