The process of introducing a phosphate group on to an amino acid residue in the C-terminal domain of RNA polymerase II. Typically, this occurs during the transcription cycle and results in production of an RNA polymerase II enzyme where the carboxy-terminal domain (CTD) of the largest subunit is extensively phosphorylated, often referred to as hyperphosphorylated or the II(0) form. Specific types of phosphorylation within the CTD are usually associated with specific regions of genes, though there are exceptions. The phosphorylation state regulates the association of specific complexes such as the capping enzyme or 3'-RNA processing machinery to the elongating RNA polymerase complex.

Any phosphorylation of RNA polymerase II C-terminal domain serine 5 residues that is involved in positive regulation of transcription elongation from RNA polymerase II promoter.

The synthesis of RNA from a DNA template by RNA polymerase I (RNAP I), originating at an RNAP I promoter.

The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs).

The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs).

Addition of the 7-methylguanosine cap to the 5' end of a nascent messenger RNA transcript.

The process of introducing a phosphate group on to a protein.

Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.

The process of introducing a phosphate group on to an amino acid residue in the C-terminal domain of RNA polymerase II. Typically, this occurs during the transcription cycle and results in production of an RNA polymerase II enzyme where the carboxy-terminal domain (CTD) of the largest subunit is extensively phosphorylated, often referred to as hyperphosphorylated or the II(0) form. Specific types of phosphorylation within the CTD are usually associated with specific regions of genes, though there are exceptions. The phosphorylation state regulates the association of specific complexes such as the capping enzyme or 3'-RNA processing machinery to the elongating RNA polymerase complex.

Any phosphorylation of RNA polymerase II C-terminal domain serine 5 residues that is involved in recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex.

Any phosphorylation of RNA polymerase II C-terminal domain that is involved in recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex.

Any phosphorylation of RNA polymerase II C-terminal domain that is involved in recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex.

Any process that activates or increases the frequency, rate or extent of Atg1/ULK1 kinase complex assembly.

Any process that stops, prevents or reduces the frequency, rate or extent of filamentous growth of a population of unicellular organisms.

Any process in which the P-TEFb-cap methyltransferase complex is transported to, or maintained in, a specific location.

The process of introducing a phosphate group onto a serine residue at position 5 within the heptapeptide repeat (YSPTSPS) of the C-terminal domain of RNA polymerase II. Typically, phosphorylation of serine 5 (Ser5) occurs near the 5' ends of genes. It is generally still observed in the middle of genes, overlapping with phosphorylation of serine 2, but is generally not present at the 3' ends of genes. In vivo, Ser5 phosphorylation occurs primarily through the action of TFIIH (KIN28 in S. cerevisiae, CKD7 in metazoans).

Any phosphorylation of RNA polymerase II C-terminal domain serine 2 residues that is involved in positive regulation of transcription elongation from RNA polymerase II promoter.

A transcription factor complex that forms part of the holo TFIIH complex. In Saccharomyces/human, TFIIK contains Ccl1p/Cyclin H, Tfb3p/MAT1 and Kin28p/CDK7.

A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

A complex that is capable of kinase activity directed towards the C-terminal Domain (CTD) of the largest subunit of RNA polymerase II and is essential for initiation at RNA polymerase II promoters in vitro. It is composed of the core TFIIH complex and the TFIIK complex.

The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome in the nucleus.

A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

A cyclin-dependent kinase activating kinase complex capable of activating cyclin-dependent kinases by threonine phosphorylation, thus regulating cell cycle progression. consists of a kinase, cyclin and optional assembly factors, in human CDK7, CCNH and MNAT1. CAK activity is itself regulated throughout the cell cycle by T-loop phosphorylation of its kinase component (CDK7 in human). Phosphorylation of serine residues during mitosis inactivates the enzyme. Also capable of CAK phosphorylating the carboxyl-terminal domain (CTD) of RNA polymerase II and other transcription activating proteins, as part of the general transcription factor TFIIH.