The enzyme appears to be distinct from other protein kinases. It brings about multiple phosphorylations of the unique C-terminal repeat domain of the largest subunit of eukaryotic DNA-directed RNA polymerase (EC 2.7.7.6). The enzyme does not phosphorylate casein, phosvitin or histone.
The taxonomic range for the selected organisms is: Drosophila melanogaster The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The enzyme appears to be distinct from other protein kinases. It brings about multiple phosphorylations of the unique C-terminal repeat domain of the largest subunit of eukaryotic DNA-directed RNA polymerase (EC 2.7.7.6). The enzyme does not phosphorylate casein, phosvitin or histone.
Positive transcription elongation factor b is the major metazoan RNA polymerase II carboxyl-terminal domain Ser2 kinase, P-TEFb is critical for the maturation of RNA PolII into productive elongation in vivo, overview
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
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
the enzyme phosphorylates the C-terminal CTD domain of the RNA polymerase II large subunit, the CTD phosphorylation pattern is precisely modified as RNA polymerase II progresses along the genes and is involved in sequential recruitment of RNA processing factors, multiple phosphorylation sites and epitopes, overview
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
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
Positive transcription elongation factor b is the major metazoan RNA polymerase II carboxyl-terminal domain Ser2 kinase, P-TEFb is critical for the maturation of RNA PolII into productive elongation in vivo, overview
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
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
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
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
distribution of dCDK12 and hyperphosphorylated RNAPII (Pol II0) on Dm polytene chromosomes by fluorescence microscopy. The dCDK12 kinase appears to be closely associated with Pol II0, not only at loci expressed normally during development, but also at heat-shock loci
dCDK12 is present on the transcribed regions of active genes. dCDK12 amounts are lower at the 5' end and higher in the middle and at the 3 end of genes (both normalized to RNAPII)
cells lacking CDK12 function are viable and able to proliferate. Antioxidant gene expression is compromised in flies with reduced Cdk12 function, which makes them oxidative stress sensitive, Cdk12 knockdown increases sensitivity to oxidative stress
the majority of Ser2 phosphorylation on productively elongating RNAPII in Saccharomyces cerevisiae appears to be catalyzed by CTDK-I, a three-subunit enzyme consisting of Ctk1 (a CDK homologue), Ctk2 (a cyclin homologue), and Ctk3
Cdk12 is a gene-selective RNA polymerase II kinase that regulates a subset of the transcriptome, including Nrf2 target genes. The enzyme engages a global shift in gene expression to switch cells from a metabolically active state to stress-defence mode when challenged by external stress. Cdk12 is not essential for bulk mRNA transcription. Cdk12 may be specifically required for stress activated gene expression. Cdk12 suppresses genes that support metabolic functions in stressed conditions. Cdk12 is a positive regulator of CncC target gene activity. Cdk12 is required for Nrf2 reporter activity in vivo, Cdk12 is critical for the expression of endogenous Nrf2 target genes. Cdk12 promotes stress resistance and overall survival in oxidative stress conditions
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
RNAi knockdown of dCDK12 in S2 cells. Chimeric yeast/human versions of Ctk1 containing the kinase homology domains of hCDK12/13 (or hCDK9) are functional in yeast cells (and also in vitro)