Any feedback?
Information on EC 2.7.11.23 - [RNA-polymerase]-subunit kinase
for references in articles please use BRENDA:EC2.7.11.23Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.11.23 [RNA-polymerase]-subunit kinaseIUBMB Comments
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.
Specify your search results
Word Map
- 2.7.11.23
- cyclin
- strand
- chromatin
- histone
-
non-homologous
-
cyclin-dependent
-
end-joining
-
radiosensitivity
-
transactivation
- helicase
-
checkpoint
-
radiation-induced
- pigmentosum
- xeroderma
- ataxia
- telangiectasia
- h2ax
-
dna-damaging
- tfiie
- wortmannin
-
preinitiation
- ataxia-telangiectasia
-
rejoin
- cak
-
cockayne
- brd4
-
pausing
-
snrnp
- tbp
- rad3-related
-
cdk-activating
-
bromodomains
- xrcc4
-
pikks
-
promoter-proximal
- rad51
-
paused
-
ir-induced
-
end-binding
- drb
- flavopiridol
-
artemis
-
unrepaired
-
gammah2ax
-
transcription-coupled
-
t-loop
-
atm-dependent
-
dsb-induced
- rpb1
-
atm-deficient
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
Synonyms
dna-pk, tfiih, p-tefb, dna-dependent protein kinase, positive transcription elongation factor b, kin28, ctd kinase, srb10, ctdk-i, tfiih kinase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bur1
C-terminal domain kinase
C-terminal repeat domain kinase
-
-
-
-
cdk7
CDK8
CDK9
Crk1
CTD kinase
CTD kinase I
Ctdk-1
CTDK-I
CTK-1
Ctk1
Ctk1 kinase
dCDK12
EC 2.7.1.141
-
-
formerly
-
Kin28
kinase, ribonucleate nucleotidyltransferase II C-terminal domain (phosphorylating)
-
-
-
-
kinase, ribonucleate nucleotidyltransferase isozyme II IIa subunit (phosphorylating)
-
-
-
-
Lsk1
Mcs6
mitotic catastrophe suppressor 6
P-TEFb
positive transcription elongation factor b
RNA pol II C-terminal domain kinase
RNA Pol II CTD kinase
RNA polymerase II carboxyl terminal domain kinase complex
RNA polymerase II CTD kinase
RNA polymerase II kinase
RNAPII CTD kinase complex
Srb10
TFIIH
additional information
CTD kinase
-
-
-
-
RNA polymerase II CTD kinase
-
-
-
-
additional information
-
the enzyme is organized in the CDKC-1/CYCLINT-1 kinase complex, see also EC 2.7.11.22
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [DNA-directed RNA polymerase] = ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:[DNA-directed RNA polymerase] phosphotransferase
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
122097-00-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + C-terminal domain of RNA polymerase II
ADP + phosphorylated C-terminal domain of RNA polymerase II
the recombinant GST-tagged CTD substrate is hyperphosphorylated by Kin28
-
-
?
ATP + chicken myosin regulatory light-chain
ADP + chicken myosin regulatory light-chain phosphate
-
-
-
-
?
ATP + CTD-containing fusion protein
ADP + phosphorylated CTD-containing fusion protein
-
-
-
-
?
ATP + GST-tagged yCTD fusion protein
?
hCDK13 purified from nuclear extracts displays CTD kinase activity in vitro with recombinant GST-tagged yeast CTD fusion proteins as substrate, hyperphosphorylation of the CTD by hCDK13 kinase
-
-
?
ATP + holo-RNA polymerase II
?
-
C-terminal domain phosphorylation by the serine 5-specific TFIIH complex, its kinase module TFIIK or by the C-terminal domain serine 2-specific kinase CTDK1
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal domain
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
ATP + RNA polymerase II C-terminal repeat domain
ADP + phosphoylated RNA polymerase II C-terminal repeat domain
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
ATP + RNA polymerase II carboxy terminal domain
ADP + phosphorylated RNA polymerase II carboxy terminal domain
ATP + Rps2
?
-
phosphorylates on Ser 238, phosphorylation of Rps2 is needed for translational accuracy
-
-
?
ATP + [carboxy terminal domain of RNA polymerase II]
ADP + phospho-[carboxy terminal domain of RNA polymerase II]
-
the enzyme GSK-3 phosphorylates the carboxy terminal domain of RNA polymerase II in vitro, but preferentially when the substrate is previously phosphorylated, consistently with the requirement of a priming phosphorylation reported for GSK-3 efficacy
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
ATP + [RNA polymerase II carboxyl terminal domain]
ADP + phospho-[RNA polymerase II carboxyl terminal domain]
dATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
dADP + ?
-
-
-
-
?
ATP + casein
ADP + phosphocasein
-
phosphorylated at about 30% the rate of RNA-polymerase II subunit
-
-
?
ATP + casein
ADP + phosphocasein
-
phosphorylated at about 30% the rate of RNA-polymerase II subunit
-
-
?
ATP + CTD-containing fusion proteins
ADP + ?
-
e.g. GAL4-CTD (formerly GC147) or HSP 90
-
-
?
ATP + histone H3
?
-
Ctk1 is essential for H3K36 methylation, also regulates H3K4 methylation
-
-
?
ATP + histone H3
?
-
Ctk1 is essential for H3K36 methylation, also regulates H3K4 methylation
-
-
?
ATP + HIV Tat
ADP + phosphorylated HIV-Tat
-
Tat is an efficient substrate for DNA-PK only in the presence of DNA, three putative target sites of DNA-PK phosphorylation
-
-
?
ATP + RNA polymerase II
?
-
phosphorylation on C-terminal domain
-
-
?
ATP + RNA polymerase II
?
both cdk7 and cdk9 are responsible for phosphorylation at the C-terminal domain
-
-
?
ATP + RNA polymerase II
?
-
CDK9 phosphorylates the C-terminal domain on serine 5
-
-
?
ATP + RNA polymerase II
?
-
TFIIH and mediator phosphorylate at C-terminal domain at Ser 5, Ser5 phosphorylation by the yeast Cdk7 (Kin28) subunit of TFIIH is required for recruitment of capping enzyme to the promoter region, P-TEFb phosphorylates at Ser 2
-
-
?
ATP + RNA polymerase II
?
-
C-terminal domain phosphorylation is required for co-transcriptional splicing
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal domain
-
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal domain
the SRI domain of Set2 interacts with the phosphorylated CTD of elongating RNAPII leading to methylation of the chromatin during transcription
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
Ctk1 kinase activity regulates H3K4 methylation, the Ctk2 and Ctk3 components of CTDK-1 are necessary for Ctk1 kinase activity, overview
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
TFIIH, a 10-subunit complex with many resident enzymatic activities, is essential for transcription by RNA polymerase II involving the TFIIH-associated kinase, Cdk7, which phosphorylates the C-terminal domain, CTD, of Rpb1, the largest subunit of Pol II
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
Cdk7 phosphorylates the C-terminal domain, CTD, that consists of multiple YSPTSPS heptapeptide repeats, at Ser5
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
phosphorylation at Ser5, phosphorylation patterns, overview
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
Ctk1 kinase activity regulates H3K4 methylation, the Ctk2 and Ctk3 components of CTDK-1 are necessary for Ctk1 kinase activity, overview
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
phosphorylation at Ser5, phosphorylation patterns, overview
-
-
?
ATP + RNA polymerase II C-terminal repeat domain
ADP + phosphoylated RNA polymerase II C-terminal repeat domain
-
hyperphosphorylation, the Mediator complex associates with RNA polymerase II, RNAPII, at least partly via the RNAPII C-terminal repeat domain, CTD, whose phosphorylation is involved in triggering promoter clearance
-
-
?
ATP + RNA polymerase II C-terminal repeat domain
ADP + phosphoylated RNA polymerase II C-terminal repeat domain
-
i.e. RNAPII CTD, hyperphosphorylation, the target specificity of TFIIK and CTDK1 differm, TFIIK phosphorylates Ser5, while CTDK1 phosphorylates Ser2
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
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
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
phosphorylation of Ser2
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
i.e. RNAP II CTD, hypophosphorylated form of RNAP IIa is recruited to the preinitiation complex at the gene promoter by the general transcription factors. Initiation proceeds when the cdk7 complex phosphorylates the CTD at the serine 5 residues, resulting in a hyperphosphorylated RNAP II that recruits the RNA-capping enzymes, overview
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
the TFIIH mediator complex plays essential roles in transcription initiation and during the transition from initiation to elongation by transmitting signals from transcriptional activators to RNA polymerase II, phosphorylation of the C-terminal domain of RNA polymerase II plays central roles in the integrated events of eucaryotic gene expression, it is not only essential for transcription, but also as a platform for RNA processing and chromatin regulation, detailed overview
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
i.e. Pol II CTD, TFIIH and mediator phosphorylate Ser5 of the CTD heptapeptide repeat sequence
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
i.e. RNAP II CTD, phosphorylation at Ser5
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
the enzyme regulates transcription elongation at many genes and integrates mRNA synthesis with histone modification, pre-mRNA processing, and mRNA export. Recruitment of P-TEFb to target genes requires deubiquitination of H2Bub, phosphorylation of H3S10, and the bromodomain protein, Brd4, overview. P-TEFb accompanies the mature mRNA to the cytoplasm to promote translation elongation. Enzyme regulation system, detailed overview
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
phosphorylation at Ser2, Ser5, and Ser7, the extended C-terminal domain, CTD, of the Rbp1 subunit contains 52 heptad repeats with a consensus sequence YSPTSPS
-
-
?
ATP + RNA polymerase II carboxy terminal domain
ADP + phosphorylated RNA polymerase II carboxy terminal domain
-
the phosphorylated RNAPII CTD, interacts with BRCA1 for induction of DEF1-dependent cleavage and accumulation of a RNAPII fragment containing the P-CTD, overview
-
-
?
ATP + RNA polymerase II carboxy terminal domain
ADP + phosphorylated RNA polymerase II carboxy terminal domain
-
i.e. RNAPII CTD
-
-
?
ATP + Rps2
ADP + phosphorylated Rps2
-
a protein of the small ribosomal subunit, Ctk1 interacts with the transcription and mRNA export, TREX, complex, which couples transcription to mRNA export, and Ctk1 enhances efficient and accurate translation of the mRNA, Ctk1 is a prerequisite for correct decoding in vivo overview
-
-
?
ATP + Rps2
ADP + phosphorylated Rps2
-
a protein of the small ribosomal subunit, phosphorylation at Ser238
-
-
?
ATP + synthetic peptides
ADP + ?
-
e.g. Lys-(Tyr-Ser-Pro-Thr-Ser-Pro-Ser)4
-
-
?
ATP + synthetic peptides
ADP + ?
-
bovine serum albumin conjugated to heptapeptide
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies)
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies)
-
phosphorylates not Tyr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies)
-
phosphorylates to a lesser extent Thr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies)
-
phosphorylates predominantly Ser-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies)
-
the CTD is essential for viability, although mutants with deletions that remove approximately half of the repeats are still viable
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies) Kc
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies) Kc
-
phosphorylates not Tyr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies) Kc
-
phosphorylates to a lesser extent Thr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies) Kc
-
phosphorylates predominantly Ser-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
phosphorylates not Tyr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
kinase CTDK1: 33 mol phosphate per mol IIA-subunit
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
kinase CTDK1 almost exclusively phosphorylates Ser-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
phosphorylates Ser- and Thr-residues equally
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
kinase CTDK2 phosphorylates to a lesser extent Thr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
kinase CTDK2: 40-50 mol phosphate per mol IIA-subunit, i.e. 1 phosphate per heptapeptide repeat
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
phosphorylates predominantly Ser-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
presumably obligate part of transcription process
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
no substrates are dTTP and AMP-PNP
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
no substrates are the RNA polymerases II of Drosophila melanogaster and yeast
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
no substrates are CTP and UTP
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
presumably obligate part of transcription process
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
the CTD is essential for viability, although mutants with deletions that remove approximately half of the repeats are still viable
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
no substrate is phosvitin
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
phosphorylates not Tyr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
phosphorylates to a lesser extent Thr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
phosphorylates predominantly Ser-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
presumably obligate part of transcription process
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
CTD kinase 1 plays an important role in transcription elongation in vivo, the deletion of one ore more CTK genes is lethal but in combination with the deletion of PPR2 or ELP
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
deletion of the kinase subunit Ctk1 results in phosphorylation of serine in position 5 of the CTD repeat during logarithmic growth and eliminates the transient increase in CTD serine 2 phosphorylation during the diauxic shift
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
the CTD is essential for viability, although mutants with deletions that remove approximately half of the repeats are still viable
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
CTD kinase I affects pre-mRNA 3' cleavage/polyadenylation through the processing component Pti1p
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
phosphorylates to a lesser extent Thr-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
no substrates are bovine serum albumin and calf thymus histone
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
no substrate is GTP
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
phosphorylates predominantly Ser-residues
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
substrates are RNA-polymerase II subunits of wheat germ, soy bean, pea and human
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
distinct from other protein phosphokinases, transfers about 20 phosphates to the heptapeptide repeats Pro-Thr-Ser-Pro-Ser-Tyr-Ser in C-terminal domain of MW 220000 subunit of RNA-polymerase II
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
no substrates are CTP and UTP
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
presumably obligate part of transcription process
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
-
Cdk12 acts on the Ser2 residue in Pol II CTD heptad repeats
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
the cyclin-dependent kinase subunit Cdk7 of TFIIH phosphorylates Ser5 and Ser7
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
the cyclin-dependent kinase subunit Cdk8 of the Mediator phosphorylates CTD Ser5
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
Cdk9 phosphorylates Ser2. Phosphorylation of CTD-Tyr1
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
Plk3 phosphorylates Thr4 in human cells. Phosphorylation of CTD-Tyr1
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
the cyclin-dependent kinase subunit Cdk8 of the Mediator phosphorylates CTD Ser5. Phosphorylation of CTD-Tyr1
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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 Tyr1Ser2Pro3Thr4Ser5Pro6Ser7
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
kinases Bur1 and Ctk1 phosphorylate Ser2
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
subunit Srb10 of the Mediator phosphorylates CTD Ser5
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
the cyclin-dependent kinase subunit Kin28 of TFIIH phosphorylates Ser5 and Ser7
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
kinases Cdk9 and Lsk1 phosphorylate Ser2. Thr4 is also phosphorylated by a kinase
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
kinases Cdk9 and Lsk1 phosphorylate Ser2. Thr4 is also phosphorylated by a kinase
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
CTD phosphorylation and transcription cycle overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
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
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
Ser2 phosphorylation by dCDK12 in the C-terminal repeat domain, CTD
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit is required for transcription and 3' processing of snRNA, e.g. U1 and U2, recognition of the 3' box by the phosphorylated CTD, CTD kinase activity is not required for beta-actin expression, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the CTD of the RNA polymerase II is the target for numerous enzymes, including cell cycle-dependent kinases and phosphatases, thus phosphorylation of the CTD becomes a key event during mRNA metabolism and physiological regulation of transcription, and is affected by cell stress or embryonic development, CTD phosphorylation and transcription cycle overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the enzyme phosphorylates the C-terminal CTD domain of the RNA polymerase II large subunit, which has specific phosphorylation patterns for regulation of mRNA and snRNA processing
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit, e.g. at Ser2 and Ser5, by cyclin-dependent kinase 7 and 9, i.e. Cdk7 and Cdk9
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the enzyme phosphorylates the C-terminal CTD domain of the RNA polymerase II large subunit
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
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, e.g. at Ser2 and Ser5, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
DYRK1A phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5. The mammalian RNAPII C-terminal domain consists of 52 hepta-residue repeats (YSPTSPS), and its phosphorylation governs the paused or elongating phases of the transcription cycle
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
enzyme DNA-PK phosphorylates all three serine residues, Ser2, Ser5, and Ser7, of C-terminal domain, CTD
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
DYRK1A phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
enzyme DNA-PK phosphorylates all three serine residues, Ser2, Ser5, and Ser7, of C-terminal domain, CTD. Serine residues at positions 2 and 7 are preferred to serine 5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
Ser phosphorylation in the C-terminal repeat domain, CTD
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
CDKC1 phosphorylates the C-terminal YSPTSPS hexapeptide repeat domain CTD of the largest subunit of RNA polymerase II at Ser5, no activity with RNA polymerase II mutant S5A
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
phosphorylation at Ser2 by BRD4 kinase. BRD4 phosphorylates the Pol II CTD in in vitro transcription reactions
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
BRD4 phosphorylates CTD proteins containing the consensus sequence and Ala substitutions at Ser5 and Ser7, but it does not phosphorylate Ser2 substitutions either alone or combined with Ser5. BRD4 phosphorylates all consensus CTD heptad repeats. Assay substrate is recombinant full-length human GST-tagged CTD
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
CTD phosphorylation facilitates pre-mRNA processing, CTD phosphorylation and transcription cycle overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit by Ctk1 is essentially required for methylation of histone H3 Lys36 in transcription elongation in volving association of Set2 to the hyperphosphorylated RNA polymerase II, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal repeat domain CTD of the RNA polymerase II large subunit is required for elongation of mRNA, the enzyme is involved in functional organization of transcription and nuclear metabolism
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
phosphorylation of Ser2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing by recruiting factors for polyadenylation and 3' end processing, phosphorylation of Ser5 during initiation recruits the capping enzyme
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the CTD kinases Ctk1, Bur1, Kin28, and Srb10 are involved in preinitiation of transcription and elongation
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the enzyme is involved, together with several factors, in regulation of RNA elongation, transition at the 3' end, and polyadenylation, the enzyme is responsible for crosslinking of polyadenylation factors, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the enzyme preferentially phosphorylates RNA poylmerase II bound in a native ternary complex in opposite to the Fcp1 phosphatase preferably dephosphorylating free RNA poylmerase II, after complex disruption, at Ser5, not Ser2, of the CTD, the TFIIH TD kinase is involved in RNA poylmerase II activity regulation, mechanism, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
CTD kinase 1 hyperphosphorylates the C-terminal repeat domain CTD of the RNA polymerase II large subunit, phosphorylation of CTD leads to interaction/binding of several proteins with nuclear functions in vitro, i.e. phosphoCTD-associating proteins, purification and analysis of PCAPs, e.g. Ess1, Hrr25, Prp40, Ssd1, SSd1, and Set2, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
Ctk1 kinase phosphorylates Ser2 and Ser5 of the C-terminal CTD domain of the RNA polymerase II large subunit
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
Ctk1 kinase phosphorylates the C-terminal CTD domain of the RNA polymerase II large subunit, primarily at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
phosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
recombinant GST-tagged protein substrate or synthetic GST-tagged peptide substrate derived from RNA polymerase II, CTD kinase 1 hyperphosphorylates the C-terminal repeat domain CTD of the RNA polymerase II large subunit at Ser2 and/or Ser5, determination of phosphorylation sites, already phosphorylated substrates are more efficient substrates for CTD kinase I
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the enzyme phosphorylates the C-terminal CTD domain of the RNA polymerase II large subunit
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
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, e.g. at Ser5, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
Ctk1 is the major serine 2 kinase in vivo
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
CTK1 phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
KIN28 phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
SRB10 phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
in vitro, Ctk1 complex can phosphorylate the CTD at all three serines, although with different efficiencies. Ctk1 phosphorylates Ser2 in vitro
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
phosphorylation of Ser2, Ser5, and Ser7 in CTD
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
phosphorylation of Ser5 and Ser7 in CTD, Bur1 phosphorylates Ser2 in vitro
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit by Ctk1 is essentially required for methylation of histone H3 Lys36 in transcription elongation in volving association of Set2 to the hyperphosphorylated RNA polymerase II, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
CTD phosphorylation facilitates pre-mRNA processing, CTD phosphorylation and transcription cycle overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
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
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
enzyme phosphorylates residues in the C-terminal domain, CTD, of the largest RNA polymerase II (RNA Pol II) subunit, RPB1
-
-
?
ATP + [RNA polymerase II carboxyl terminal domain]
ADP + phospho-[RNA polymerase II carboxyl terminal domain]
-
phosphorylation at Ser-2
-
-
?
ATP + [RNA polymerase II carboxyl terminal domain]
ADP + phospho-[RNA polymerase II carboxyl terminal domain]
Neurospora crassa 87-3
-
phosphorylation at Ser-2
-
-
?
ATP + [RNA polymerase II]
ADP + phospho-[RNA polymerase II]
the CDK9 subunit of positive transcription elongation factor b phosphorylates RNA polymerase II at its Ser-2 carboxy-terminal domain repeat
-
-
?
ATP + [RNA polymerase II]
ADP + phospho-[RNA polymerase II]
cyclin-dependent kinase 9 (CDK9) is a subunit of the positive transcription elongation factor b (P-TEFb) complex that regulates gene transcription elongation by phosphorylating the C-terminal domain (CTD) of RNA polymerase II
-
-
?
GTP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
GDP + ?
-
poor substrate
-
-
?
GTP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
GDP + ?
-
kinase CTDK1, not kinase CTDK2
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
Drosophila CDK12 manifests CTD kinase activity in vitro
-
-
?
additional information
?
-
-
human enzyme consists of 2 components: component A bears the active site and is capable of DNA-independent autophosphorylation, component B stimulates component A and is phosphorylated only in the presence of DNA
-
-
?
additional information
?
-
-
phosphorylation of CTD is required to disrupt the interactions between unphosphorylated CTD and the mediator complex to form a holoenzyme of RNA polymerase II or with transcription factors to form a preinitiation complex of transcription, disruption of the interactions at elongation of transcription are required to assist the recruitment of pre-mRNA modification enzymes
-
-
?
additional information
?
-
-
the cyclin-dependent kinase 7 and 9 are involved in processing of cytomegalovirus RNA in infected cells, enzyme inhibition results in changes in differential splicing and polyadenylation of viral immediate early and UL37 transcripts, overview, viral infection alters localization of RNA polymerase II
-
-
?
additional information
?
-
-
the RNA polymerase II recruits factors including the enzyme that hyperphosphorylate its C-terminal domain, i.e. CTD, and the CTD in turn recruits proteins needed for mRNA splicing and polyadenylation, snRNA promoters probably recruit a CTD kinase, whose snRNA-specific phosphorylation patterns recruits factors required for promoter-coupled 3'-end formation, overview
-
-
?
additional information
?
-
-
cyclin-dependent kinase 7 and 9, i.e. Cdk7 and Cdk9, perform also the cyclin-dependent phosphorylation of other proteins, EC 2.7.11.22
-
-
?
additional information
?
-
-
cyclin-dependent kinase Cdk1, Cdk7, and Cdk9, EC 2.7.11.22, and by MAPK, EC 2.7.11.24, phosphorylating specific serine residues
-
-
?
additional information
?
-
-
cdk7 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
cdk7 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
cdk7 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
-
cdk9 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
cdk9 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
cdk9 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
-
DYRK1A targets contain a TCTCGCGAGA motif, which drives DYRK1A-dependent activation. DYRK1A interacts with RNAPII independently of its kinase activity
-
-
?
additional information
?
-
during transcription after repair, UV irradiation induces a specific Ser-2 phosphorylation of the RNA polymerase II and this phosphorylation is Cockayne syndrome group B protein-dependent. The CDK9 subunit of positive transcription elongation factor b is not responsible for this phosphorylation but instead might play a nonenzymatic role in transcription restart after DNA repair
-
-
-
additional information
?
-
-
the CDKC-1/CYCLINT-1 kinase complex is a positive regulator of transcription in Medicago sativa, the level and activity of the enzyme is not cell cycle dependent
-
-
?
additional information
?
-
-
the enzyme also performs the reaction of EC 2.7.11.22
-
-
?
additional information
?
-
BRD4 autophosphorylation in an in vitro kinase reaction. Phoshorylation site determination with RNA Pol II CTD using a series of GST-CTD fusions with 25- or 16-heptad repeats bearing alanine substitutions in every heptad at Ser2, Ser5, Ser7, or Thr4 as substrates
-
-
?
additional information
?
-
-
CTD kinase function is opposed by Ess1, an essential prolyl isomerase binding to the C-terminal domain of the RNA polymerase, Ess1 interacts with CTD kinases, especially with Ctk1 and Srb10, the kinase and Ess1 compete for Ser5 of RNA polymerase II
-
-
?
additional information
?
-
-
the reaction is also in vitro performed by cyclin-dependent kinase Ctk1, and Bur1, EC 2.7.11.22, phosphorylating specific serine residues
-
-
?
additional information
?
-
-
CTK1 kinase is required for BRCA1-induced lethality in yeast, overview
-
-
?
additional information
?
-
-
P-TEFb co-operates with c-Myc during transactivation and cell transformation, and also requires SKIP, c-Ski-interacting protein, an mRNA elongationand splicing factor. Some functions of the P-TEFb/Ser2P CTD are executed by the Spt6 transcription elongation factor, which binds directly to the phosphorylated CTD and recruits the Iws1 protein, overview. Because P-TEFb counteracts NELF- and DSIF-induced pausing in cell-free transcription reactions, at least part of its activity does not depend upon chromatin
-
-
?
additional information
?
-
Set2-catalyzed H3K36me2 does not require either Ctk1-dependent phosphorylation of RNA polymerase II or the presence of the phospho-C-terminal domain, CTD, interaction (SRI) domain of Set2 for methylation of histone H3 at lysine 36 promoting deacetylation of transcribed chromatin and repressing cryptic promoters within genes. By contrast, H3K36me3 requires Spt6, proline 38 on histone H3, the CTD of RNAPII, Ctk1, and the C-terminal SRI domain of Set2, overview
-
-
?
additional information
?
-
-
enzyme-Mediator complex dissociation assay, overview
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
Ctdk-1 interacts with RNA polymerase I forming a complex
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
Ctk3 shows no binding to CTD peptides
-
-
?
additional information
?
-
-
Ctk3 shows no binding to CTD peptides
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal domain
the SRI domain of Set2 interacts with the phosphorylated CTD of elongating RNAPII leading to methylation of the chromatin during transcription
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
ATP + RNA polymerase II C-terminal repeat domain
ADP + phosphoylated RNA polymerase II C-terminal repeat domain
-
hyperphosphorylation, the Mediator complex associates with RNA polymerase II, RNAPII, at least partly via the RNAPII C-terminal repeat domain, CTD, whose phosphorylation is involved in triggering promoter clearance
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
ATP + RNA polymerase II carboxy terminal domain
ADP + phosphorylated RNA polymerase II carboxy terminal domain
-
the phosphorylated RNAPII CTD, interacts with BRCA1 for induction of DEF1-dependent cleavage and accumulation of a RNAPII fragment containing the P-CTD, overview
-
-
?
ATP + Rps2
ADP + phosphorylated Rps2
-
a protein of the small ribosomal subunit, Ctk1 interacts with the transcription and mRNA export, TREX, complex, which couples transcription to mRNA export, and Ctk1 enhances efficient and accurate translation of the mRNA, Ctk1 is a prerequisite for correct decoding in vivo overview
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
ATP + [RNA polymerase II carboxyl terminal domain]
ADP + phospho-[RNA polymerase II carboxyl terminal domain]
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
Ctk1 kinase activity regulates H3K4 methylation, the Ctk2 and Ctk3 components of CTDK-1 are necessary for Ctk1 kinase activity, overview
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
TFIIH, a 10-subunit complex with many resident enzymatic activities, is essential for transcription by RNA polymerase II involving the TFIIH-associated kinase, Cdk7, which phosphorylates the C-terminal domain, CTD, of Rpb1, the largest subunit of Pol II
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
Ctk1 kinase activity regulates H3K4 methylation, the Ctk2 and Ctk3 components of CTDK-1 are necessary for Ctk1 kinase activity, overview
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
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
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
i.e. RNAP II CTD, hypophosphorylated form of RNAP IIa is recruited to the preinitiation complex at the gene promoter by the general transcription factors. Initiation proceeds when the cdk7 complex phosphorylates the CTD at the serine 5 residues, resulting in a hyperphosphorylated RNAP II that recruits the RNA-capping enzymes, overview
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
the TFIIH mediator complex plays essential roles in transcription initiation and during the transition from initiation to elongation by transmitting signals from transcriptional activators to RNA polymerase II, phosphorylation of the C-terminal domain of RNA polymerase II plays central roles in the integrated events of eucaryotic gene expression, it is not only essential for transcription, but also as a platform for RNA processing and chromatin regulation, detailed overview
-
-
?
ATP + RNA polymerase II C-terminal subunit
ADP + phosphoylated RNA polymerase II C-terminal subunit
-
the enzyme regulates transcription elongation at many genes and integrates mRNA synthesis with histone modification, pre-mRNA processing, and mRNA export. Recruitment of P-TEFb to target genes requires deubiquitination of H2Bub, phosphorylation of H3S10, and the bromodomain protein, Brd4, overview. P-TEFb accompanies the mature mRNA to the cytoplasm to promote translation elongation. Enzyme regulation system, detailed overview
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies)
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies)
-
the CTD is essential for viability, although mutants with deletions that remove approximately half of the repeats are still viable
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
Drosophila sp. (in: flies) Kc
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
presumably obligate part of transcription process
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
presumably obligate part of transcription process
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
the CTD is essential for viability, although mutants with deletions that remove approximately half of the repeats are still viable
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
presumably obligate part of transcription process
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
CTD kinase 1 plays an important role in transcription elongation in vivo, the deletion of one ore more CTK genes is lethal but in combination with the deletion of PPR2 or ELP
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
deletion of the kinase subunit Ctk1 results in phosphorylation of serine in position 5 of the CTD repeat during logarithmic growth and eliminates the transient increase in CTD serine 2 phosphorylation during the diauxic shift
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
the CTD is essential for viability, although mutants with deletions that remove approximately half of the repeats are still viable
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
CTD kinase I affects pre-mRNA 3' cleavage/polyadenylation through the processing component Pti1p
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
-
-
-
?
ATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa]
ADP + phospho-[DNA-directed RNA polymerase II subunit IIa]
-
presumably obligate part of transcription process
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[DNA-directed RNA polymerase II]
-
Cdk12 acts on the Ser2 residue in Pol II CTD heptad repeats
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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 Tyr1Ser2Pro3Thr4Ser5Pro6Ser7
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase II]
ADP + phospho-[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
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
CTD phosphorylation and transcription cycle overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
Ser2 phosphorylation by dCDK12 in the C-terminal repeat domain, CTD
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit is required for transcription and 3' processing of snRNA, e.g. U1 and U2, recognition of the 3' box by the phosphorylated CTD, CTD kinase activity is not required for beta-actin expression, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the CTD of the RNA polymerase II is the target for numerous enzymes, including cell cycle-dependent kinases and phosphatases, thus phosphorylation of the CTD becomes a key event during mRNA metabolism and physiological regulation of transcription, and is affected by cell stress or embryonic development, CTD phosphorylation and transcription cycle overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the enzyme phosphorylates the C-terminal CTD domain of the RNA polymerase II large subunit, which has specific phosphorylation patterns for regulation of mRNA and snRNA processing
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
DYRK1A phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5. The mammalian RNAPII C-terminal domain consists of 52 hepta-residue repeats (YSPTSPS), and its phosphorylation governs the paused or elongating phases of the transcription cycle
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
enzyme DNA-PK phosphorylates all three serine residues, Ser2, Ser5, and Ser7, of C-terminal domain, CTD
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
phosphorylation at Ser2 by BRD4 kinase. BRD4 phosphorylates the Pol II CTD in in vitro transcription reactions
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
CTD phosphorylation facilitates pre-mRNA processing, CTD phosphorylation and transcription cycle overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit by Ctk1 is essentially required for methylation of histone H3 Lys36 in transcription elongation in volving association of Set2 to the hyperphosphorylated RNA polymerase II, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal repeat domain CTD of the RNA polymerase II large subunit is required for elongation of mRNA, the enzyme is involved in functional organization of transcription and nuclear metabolism
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
phosphorylation of Ser2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing by recruiting factors for polyadenylation and 3' end processing, phosphorylation of Ser5 during initiation recruits the capping enzyme
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the CTD kinases Ctk1, Bur1, Kin28, and Srb10 are involved in preinitiation of transcription and elongation
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the enzyme is involved, together with several factors, in regulation of RNA elongation, transition at the 3' end, and polyadenylation, the enzyme is responsible for crosslinking of polyadenylation factors, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
the enzyme preferentially phosphorylates RNA poylmerase II bound in a native ternary complex in opposite to the Fcp1 phosphatase preferably dephosphorylating free RNA poylmerase II, after complex disruption, at Ser5, not Ser2, of the CTD, the TFIIH TD kinase is involved in RNA poylmerase II activity regulation, mechanism, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
Ctk1 is the major serine 2 kinase in vivo
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
CTK1 phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
KIN28 phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
SRB10 phosphorylates the C-terminal domain of RNA polymerase II at Ser2 and Ser5
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
hyperphosphorylation of the C-terminal domain CTD of the RNA polymerase II large subunit by Ctk1 is essentially required for methylation of histone H3 Lys36 in transcription elongation in volving association of Set2 to the hyperphosphorylated RNA polymerase II, overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
CTD phosphorylation facilitates pre-mRNA processing, CTD phosphorylation and transcription cycle overview
-
-
?
ATP + [DNA-directed RNA polymerase]
ADP + phospho-[DNA-directed RNA polymerase]
-
enzyme phosphorylates residues in the C-terminal domain, CTD, of the largest RNA polymerase II (RNA Pol II) subunit, RPB1
-
-
?
ATP + [RNA polymerase II carboxyl terminal domain]
ADP + phospho-[RNA polymerase II carboxyl terminal domain]
-
phosphorylation at Ser-2
-
-
?
ATP + [RNA polymerase II carboxyl terminal domain]
ADP + phospho-[RNA polymerase II carboxyl terminal domain]
Neurospora crassa 87-3
-
phosphorylation at Ser-2
-
-
?
ATP + [RNA polymerase II]
ADP + phospho-[RNA polymerase II]
the CDK9 subunit of positive transcription elongation factor b phosphorylates RNA polymerase II at its Ser-2 carboxy-terminal domain repeat
-
-
?
ATP + [RNA polymerase II]
ADP + phospho-[RNA polymerase II]
cyclin-dependent kinase 9 (CDK9) is a subunit of the positive transcription elongation factor b (P-TEFb) complex that regulates gene transcription elongation by phosphorylating the C-terminal domain (CTD) of RNA polymerase II
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
phosphorylation of CTD is required to disrupt the interactions between unphosphorylated CTD and the mediator complex to form a holoenzyme of RNA polymerase II or with transcription factors to form a preinitiation complex of transcription, disruption of the interactions at elongation of transcription are required to assist the recruitment of pre-mRNA modification enzymes
-
-
?
additional information
?
-
-
the cyclin-dependent kinase 7 and 9 are involved in processing of cytomegalovirus RNA in infected cells, enzyme inhibition results in changes in differential splicing and polyadenylation of viral immediate early and UL37 transcripts, overview, viral infection alters localization of RNA polymerase II
-
-
?
additional information
?
-
-
the RNA polymerase II recruits factors including the enzyme that hyperphosphorylate its C-terminal domain, i.e. CTD, and the CTD in turn recruits proteins needed for mRNA splicing and polyadenylation, snRNA promoters probably recruit a CTD kinase, whose snRNA-specific phosphorylation patterns recruits factors required for promoter-coupled 3'-end formation, overview
-
-
?
additional information
?
-
-
cdk7 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
cdk7 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
cdk7 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
-
cdk9 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
cdk9 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
cdk9 of the host transcription machinery is recruited to human cytomegalovirus immediate-early transcription sites, inhibition of the cyclin-dependent kinases at the beginning of human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinase cdk7 at the viral transcriptosome, overview
-
-
?
additional information
?
-
-
DYRK1A targets contain a TCTCGCGAGA motif, which drives DYRK1A-dependent activation. DYRK1A interacts with RNAPII independently of its kinase activity
-
-
?
additional information
?
-
-
the CDKC-1/CYCLINT-1 kinase complex is a positive regulator of transcription in Medicago sativa, the level and activity of the enzyme is not cell cycle dependent
-
-
?
additional information
?
-
-
CTD kinase function is opposed by Ess1, an essential prolyl isomerase binding to the C-terminal domain of the RNA polymerase, Ess1 interacts with CTD kinases, especially with Ctk1 and Srb10, the kinase and Ess1 compete for Ser5 of RNA polymerase II
-
-
?
additional information
?
-
-
CTK1 kinase is required for BRCA1-induced lethality in yeast, overview
-
-
?
additional information
?
-
-
P-TEFb co-operates with c-Myc during transactivation and cell transformation, and also requires SKIP, c-Ski-interacting protein, an mRNA elongationand splicing factor. Some functions of the P-TEFb/Ser2P CTD are executed by the Spt6 transcription elongation factor, which binds directly to the phosphorylated CTD and recruits the Iws1 protein, overview. Because P-TEFb counteracts NELF- and DSIF-induced pausing in cell-free transcription reactions, at least part of its activity does not depend upon chromatin
-
-
?
additional information
?
-
Set2-catalyzed H3K36me2 does not require either Ctk1-dependent phosphorylation of RNA polymerase II or the presence of the phospho-C-terminal domain, CTD, interaction (SRI) domain of Set2 for methylation of histone H3 at lysine 36 promoting deacetylation of transcribed chromatin and repressing cryptic promoters within genes. By contrast, H3K36me3 requires Spt6, proline 38 on histone H3, the CTD of RNAPII, Ctk1, and the C-terminal SRI domain of Set2, overview
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
-
661111, 661590, 661630, 661828, 661832, 662227, 662435, 662864, 680010, 680768, 681926, 686270, 689712, 689778
additional information
cyclin K is associated with purified dCDK12, implicating it as the cyclin subunit of this CTD kinase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-2-(4-(4-chlorophenyl)-2,3,9-trimethyl-6H-thieno[3,2-f][1,2,4]triazolo[4,3-a][1,4]diazepin-6-yl)acetamide
i.e. CPI203, phosphorylation of the CTD Ser2 is inhibited in vivo by a BRD4 inhibitor that blocks its binding to chromatin
(S)-tert-butyl 2-(4-(4-chlorophenyl)-2,3,9-trimethyl-6H-thieno[3,2-f][1,2,4]triazolo[4,3-a][1,4]diazepin-6-yl)acetate
i.e. JQ1
1-NA-PP1
-
potent inhibitor of Kin28as allele kinase activity, Kin28as inhibition reduces transcript capping, overview, but inhibition of Kin28 does not inhibit transcription
6-[(2-[[4-(2,4-dichlorophenyl)-5-(4-methyl-1H-imidazol-2-yl)pyrimidin-2-yl]amino]ethyl)amino]pyridine-3-carbonitrile
-
-
8-(methylthio)-4,5-dihydrothieno[3',4':5,6]benzoisoxazole-6-carboamide
-
KM05283, CTD kinase inhibitor
Bovine serum albumin conjugated to heptapeptide
-
with RNA-polymerase II subunit as substrate
-
flavopiridol
-
causes a reduction in Ser2 phosphorylation and a defect in the transcription elongation of heat shock genes
GST-CTD
-
overexpression of this fragment inhibits tyrosine phosphorylation of RNAP II in vivo
-
Synthetic peptide
-
multimers of consensus heptapeptide repeat Pro-Thr-Ser-Pro-Ser-Tyr-Ser, with RNA-polymerase II subunit as substrate
-
1-(5-isoquinolinesulfonyl)-2-methylpiperazine
-
i.e. H7, CTD kinase inhibitor, blocks mRNA elongation in vivo, but does not affect U2 snRNA transcription
5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole
-
CTD kinase inhibitor, blocks mRNA elongation in vivo, but does not affect U2 snRNA transcription
5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole
-
CDK9 inhibitor, inhibits transcriptional activation by EBNA 2, potential anti-Epstein-Barr virus agent
roscovitine
impairment in the localization of proteins to the immediate-early transcription sites during roscovitine treatment is specific to cdk9 and cdk7, decreases levels of cdk9 and cdk7 RNA, a corresponding reduction in cdk9 protein but only a modest decrease in cdk7 protein, a delay in the addition of roscovitine until 8 h p.i. does not inhibit cdk9 and cdk7 protein expression in human cytomegalovirus-infected cells, overexpression of cdk9 does not compensate for the effects of roscovitine on its localization in human cytomegalovirus-infected cells; inhibition of cdk7 expression during roscovitine treatment occurs at the RNA level; inhibition of cdk9 expression during roscovitine treatment occurs at the RNA level, overexpression of cdk9 does not compensate for the effects of roscovitine on its localization in HCMV-infected cells
additional information
-
enzyme inhibition affects the binding of Hsp70 to RNA polymerase II, overview
-
additional information
-
no inhibition by cycloheximide, inhibition of the CTD kinase in vivo affects the 3' processing of snRNA, but only slightly the initiation and elongation of transcription of U2 genes, overview
-
additional information
-
the level and activity of the enzyme is not cell cycle dependent
-
additional information
BRD4 phosphorylation of the CTD is not affected by either flavopiridol or roscovitine. Inhibitors of DNA-PK and MAP (Erk1/2) CTD kinases as well as common broad spectrum kinase inhibitors have no effect on BRD4
-
additional information
-
transcription through the polyadenylation site leads to a reduction in the levels of Ctk1 kinase protein and activity
-
additional information
-
translation elongation of wild-type not inhibited by paromomycin
-
additional information
-
immobilization of holo-RNAPII via Rbp2 inhibits CTD hyperphosphorylation
-
additional information
-
Set1 is involved in disruption of the nucleosome at the 5' end, overview
-
additional information
the enzyme activity of CTD kinase Bur1 is repressed in the presence of a functional CTD kinase Kin28 complex
-
additional information
the enzyme activity of CTD kinase Bur1 is repressed in the presence of a functional CTD kinase Kin28 complex
-
additional information
the enzyme activity of CTD kinase Bur1 is repressed in the presence of a functional CTD kinase Kin28 complex
-
additional information
-
no inhibition by CTP, GTP, UTP, bovine serum albumin alone; no inhibition by EGTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CYCLINT protein
-
endogenous from Medicago sativa and from Medicago trunculata, the enzyme is organized in the CDKC-1/CYCLINT-1 kinase complex, CYCLINT protein is a specific interactor of the enzyme forming the active kinase complex which localizes to the nucleus
-
Mediator
-
stimulates the CTD kinase activity of TFIIH manyfold, immobilized holo-RNAPII can be separated into RNAPII and Mediator
-
Rsp5 protein
-
the unrelated CTD-binding protein, Rsp5, is capable of stimulating this CTD kinase activity
-
additional information
-
infection with human cytomegalovirus increases Cdk7 and Cdk9 activities and phosphorylation levels of the large subunit of RNA polymerase II CTD
-
additional information
-
UV irradiation and actinomycin D induce enzyme activity leading to inhibition of U2 snRNA transcription, inhibition by UV irrardiation can be rescued by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole and 1-(5-isoquinolinesulfonyl)-2-methylpiperazine
-
additional information
-
Epstein-Barr virus EBNA 2, stimulates both RNA polymerase II recruitment and RNA polymerase II phosphorylation by CDK9 on serine 5 of the C-terminal domain in vivo
-
additional information
-
DNA-PK is active only in the presence of DNA, no activity in absence of DNA
-
additional information
-
the level and activity of the enzyme is not cell cycle dependent
-
additional information
-
mediator-induced stimulation of C-terminal domain phosphorylation with TFIIH and CTDK1 kinase
-
additional information
-
binding of Spt6 to the P-TEFb/Ser2P CTD stimulates the kinetics of mRNA export. Because P-TEFb counteracts NELF- and DSIF-induced pausing in cell-free transcription reactions, at least part of its activity does not depend upon chromatin
-
additional information
the Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAPII) facilitate RNA polymerase II CTD dephosphorylation
-
additional information
the Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAPII) facilitate RNA polymerase II CTD dephosphorylation
-
additional information
the Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAPII) facilitate RNA polymerase II CTD dephosphorylation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000085
[DNA-directed RNA polymerase]
recombinant enzyme, pH 6.0-7.5, temperature not specified in the publication
0.01
ATP
recombinant enzyme, pH 6.0-7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03 - 0.099
(S)-2-(4-(4-chlorophenyl)-2,3,9-trimethyl-6H-thieno[3,2-f][1,2,4]triazolo[4,3-a][1,4]diazepin-6-yl)acetamide
Mus musculus
pH 6.0-7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
30
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Drosophila sp. (in: flies)
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
is associated with translating ribosomes in vivo
brenda
additional information
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)
brenda
distribution of hCDK12 on chromosomes, overview
brenda
-
Cdk7 and Cdk9 are distributed throughout the nuclei of infected cells
brenda
-
nuclear DYRK1A is associated with high molecular weight complexes that co-fractionate with RNAPII
brenda
-
-
brenda
additional information
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
-
brenda
additional information
-
Cdk9 localizes with the input viral DNA at early infection time, later aggregation of Cdk7, Cdk9, and S2-phosphorylated RNAP II CTD occurs, colocalized with IE1/IE2 proteins adjacent to promyelocytic leukemia protein oncogenic domains, overview
-
brenda
additional information
-
localization of cdk7 and cdk9 to the viral transcriptosome of human cytomegalovirus
-
brenda
additional information
localization of cdk7 and cdk9 to the viral transcriptosome of human cytomegalovirus
-
brenda
additional information
localization of cdk7 and cdk9 to the viral transcriptosome of human cytomegalovirus
-
brenda
additional information
-
human cytomegalovirus, HCMV, infection in the presence of roscovitine impairs the localization of cdk7, but not of IE2-86, at viral transcriptosomes
-
brenda
additional information
human cytomegalovirus, HCMV, infection in the presence of roscovitine impairs the localization of cdk7, but not of IE2-86, at viral transcriptosomes
-
brenda
additional information
human cytomegalovirus, HCMV, infection in the presence of roscovitine impairs the localization of cdk7, but not of IE2-86, at viral transcriptosomes
-
brenda
additional information
-
human cytomegalovirus, HCMV, infection in the presence of roscovitine impairs the localization of cdk9, but not of IE2-86, at viral transcriptosomes
-
brenda
additional information
human cytomegalovirus, HCMV, infection in the presence of roscovitine impairs the localization of cdk9, but not of IE2-86, at viral transcriptosomes
-
brenda
additional information
human cytomegalovirus, HCMV, infection in the presence of roscovitine impairs the localization of cdk9, but not of IE2-86, at viral transcriptosomes
-
brenda
additional information
-
the level and activity of the enzyme is not cell cycle dependent
-
brenda
additional information
profiling of the location of the RNAPII phosphorylated isoforms in wild-type cells and mutants for most CTD modifying enzymes. The CTD cycle is uniform across genes
-
brenda
additional information
profiling of the location of the RNAPII phosphorylated isoforms in wild-type cells and mutants for most CTD modifying enzymes. The CTD cycle is uniform across genes
-
brenda
additional information
profiling of the location of the RNAPII phosphorylated isoforms in wild-type cells and mutants for most CTD modifying enzymes. The CTD cycle is uniform across genes
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
the highly selective CDK9/P-TEFb inhibitor BAY1143572 shows strong potential as a treatment of adult T-cell leukemia/lymphoma (ATL)
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
protistan organisms, such as amoebozoa, kinetoplastids, trichomonads, and diplomonads, which have diverged very early from other eukaryotic lineages, lack repetitive CTD motifs
evolution
the human orthologue of Saccharomyces cerevisiae Ctk1 is one or both of the isozyme pair, hCDK12-hCDK13
evolution
the metazoan orthologue of Saccharomyces cerevisiae Ctk1 in Drosophila melanogaster is dCDK12
malfunction
-
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
malfunction
-
DYRK1A depletion leads to reduced Ser2/Ser5 phosphorylation at its target promoters. The combination of the loss of RNAPII association to the target promoters together with the reduced CTD phosphorylation of the elongating RNAPII is responsible for the reduced expression of the target genes upon DYRK1A depletion
malfunction
loss of the enzyme BRD4 is associated with metastatic breast cancer. BRD4 knockdown suppresses global transcription in murine embryonic fibroblasts, overview
malfunction
mutation of Cdk7 phosphorylation site Ser7 in substrate RNAPII CTD is lethal to human cells
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
malfunction
mutation of Thr4 in substrate RNAPII CTD is not lethal to fission yeast cells
malfunction
RNAi knockdown of dCDK12 in S2 cells alters the phosphorylation state of the CTD, reducing its Ser2 phosphorylation levels
malfunction
-
silencing the expression of Trypanosoma brucei cdc2-related kinase 9 (CRK9) leads to a loss of RPB1 phosphorylation, but that does not impair RNA Pol II transcription or cotranscriptional m7G capping. Instead, CRK9 silencing leads to a block of spliced leader (SL) trans splicing, an essential step in trypanosome mRNA maturation, that is caused by hypomethylation of the SL RNA's unique cap4.
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
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
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
malfunction
-
deletion of enzyme complex components in Neurospora leads to high CAT-3 expression level and resistance to H2O2-induced reactive oxygen species stress. Subunit CTK-1 deletion leads to dramatic decreases of SET-2 recruitment and histone H3 K36me3 modification
malfunction
-
enzyme GSK-3 inhibition only prevents CTD hyperphosphorylation triggered by UV but not basal phosphorylation. Enzyme inhibition abrogates both the reduction in RNA polymerase II elongation and changes in AS elicited by UV. GSK-3 inhibition prevents UV-induced apoptosis
malfunction
the deregulation of CDK9/PTEFb has important implications for many cancer types
malfunction
-
mutation of Thr4 in substrate RNAPII CTD is not lethal to fission yeast cells
-
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
-
malfunction
Neurospora crassa 87-3
-
deletion of enzyme complex components in Neurospora leads to high CAT-3 expression level and resistance to H2O2-induced reactive oxygen species stress. Subunit CTK-1 deletion leads to dramatic decreases of SET-2 recruitment and histone H3 K36me3 modification
-
metabolism
-
DYRK1A is a dosage-sensitive protein kinase that fulfills key roles during development and in tissue homeostasis. DYRK1A-bound promoters show a higher occurrence of activating chromatin modifications when compared with genes that do not associate with DYRK1A, including high levels of H3K4me3 and H3K4me2 surrounding TSSs or elevated H3K36me3 in the gene body
metabolism
phosphorylation state of the C-terminal domain of RNA polymerase II, detailed overview
metabolism
-
the enzyme is involved in the regulation of the Nrf2 signalling pathway
metabolism
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
metabolism
the universal RNA polymerase II CTD cycle is orchestrated by complex interplays between kinase, phosphatase, and isomerase enzymes along genes
metabolism
cyclin-dependent kinase 9 (CDK9) is a subunit of the positive transcription elongation factor b (P-TEFb) complex that regulates gene transcription elongation by phosphorylating the C-terminal domain (CTD) of RNA polymerase II
metabolism
-
the enzyme complex participates in the transcription elongation of cat-3 and is required for the regulation of the cat-3 and cat-1
metabolism
Neurospora crassa 87-3
-
the enzyme complex participates in the transcription elongation of cat-3 and is required for the regulation of the cat-3 and cat-1
-
physiological function
-
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
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
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
physiological function
CTDK-I is a yeast kinase complex that phosphorylates the C-terminal repeat domain (CTD) of RNA polymerase II (Pol II) to promote transcription elongation. CTDK-I contains the cyclin-dependent kinase Ctk1 (homologous to human CDK9/CDK12), the cyclin Ctk2 (human cyclin K), and the yeast-specific subunit Ctk3, which is required for CTDK-I stability and activity
physiological function
Ctk1, the main Ser2 kinase in coding and 3'-end regions, is required for cotranscriptional recruitment of the polyadenylation machinery. The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II as Rpb4/7 heterodimer is important to maintain proper levels of RNAPII phosphorylation, and it functions by a mechanism(s) that involves Rpb4/7-dependent association, recruitment and/or accessibility, of key CTD modifying enzymes, phosphorylation of RNAPII CTD is altered in Rpb4/7 mutants
physiological function
-
DNA-dependent protein kinase DNA-PK is a component of the RNAP II complex involved in HIV transcription, the enzyme interacts functionally with the RNA polymerase II complex recruited at the human immunodeficiency virus (HIV) long terminal repeat and plays an important specific role in HIV gene expression. Phosphorylation of residue Ser5 of the RNAP II CTD is linked with the initiation phase of HIV transcription, while phosphorylation of Ser-2 of the CTD is found to be correlated with the elongation phase of HIV gene expression. The transcription factor (TF) IIH complex does not play any role during the elongation phase of transcription. In the absence of TNF-alpha stimulation, the latent proviruses carry both DNA-PK and RNAP II at extremely low levels. TNF-alpha activation for 3 h results in a sixfold increase in the amount of RNAP II at the promoter, and also an increase in DNA-P level. Higher levels of DNA-PK and RNAP II up to the 5' region of the env gene, but lower levels further into the downstream regions. DNA-PK is involved in both the initiation and elongation phases of transcription, albeit more significantly during elongation. DNA-PK facilitates HIV-1 transcription essentially by phosphorylating the RNAP II CTD, and Tat phosphorylation also contributes significantly to HIV replication
physiological function
-
Down syndrome-associated kinase DYRK1A regulates transcription of a subset of genes by associating to their proximal promoter regions and phosphorylating the C-terminal domain of the RNA polymerase II. Protein kinase DYRK1A is recruited to proximal promoters of growth-related genes, genome-wide analysis, overview. DYRK1A recruitment to its target genes is independent of cell growth conditions and the enzyme is recruited to chromatin in both proliferating and resting cells. Enzyme DYRK1A shows ability to activate transcription when tethered to a minimal promoter, relationship between DYRK1A promoter occupancy and the transcriptional activity of its target genes, overview. The TCTCGCGAGA sequence is a regulatory motif in DYRK1A target promoters
physiological function
-
human parasite Trypanosoma brucei lacks the heptad repeats and a CDK7 orthologue. Characterization of trypanosome TFIIH does not identify a kinase component. The Trypanosoma brucei CTD nevertheless is phosphorylated by cdc2-related kinase 9 (CRK9) and is essential for transcription. RPB1 phosphorylation and SL RNA cap4 formation depend on CRK9 kinase activity. CRK9-dependent RPB1 phosphorylation is neither required for transcription initiation at the SLRNA promoter nor an essential modification for transcription elongation within the protein coding gene arrays
physiological function
Kin28 (mammalian Cdk7), a Ser5/Ser7 kinase, facilitates transcription and formation of the scaffold complex together with Ser2/Ser5 kinase Srb10 (mammalian Cdk8). Kin28 is part of the TFIIH initiation complex and phosphorylates Ser5 to promote cotranscriptional 5' mRNA capping, and in mammals also phosphorylates Ser7 during promoter-proximal pausing and perhaps during termination. The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II as Rpb4/7 heterodimer is important to maintain proper levels of RNAPII phosphorylation, and it functions by a mechanism(s) that involves Rpb4/7-dependent association, recruitment and/or accessibility, of key CTD modifying enzymes, phosphorylation of RNAPII CTD is altered in Rpb4/7 mutants
physiological function
Srb10 (mammalian Cdk8), a Ser2/Ser5 kinase, is part of the Mediator complex and inactivatesRNAPII prior to pre-initiation complex formation, and, together with Kin28 (a Ser5/Ser7 kinase), facilitates transcription and formation of the scaffold complex. The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II as Rpb4/7 heterodimer is important to maintain proper levels of RNAPII phosphorylation, and it functions by a mechanism(s) that involves Rpb4/7-dependent association, recruitment and/or accessibility, of key CTD modifying enzymes, phosphorylation of RNAPII CTD is altered in Rpb4/7 mutants
physiological function
the bromodomain protein BRD4 is an atypical kinase that phosphorylates serine 2 of the RNA polymerase II C-terminal domain directly both in vitro and in vivo under conditions where other CTD kinases are inactive. It is involved in acute myeloid leukemia, multiple myeloma, Burkitt's lymphoma, NUT midline carcinoma, colon cancer, and inflammatory disease. BRD4 also contributes to regulation of both cell cycle and transcription of oncogenes, HIV, and human papilloma virus. It is a regulator of eukaryotic transcription
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
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
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
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
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
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
physiological function
transcription by RNA polymerase II (RNAPII) is coupled to mRNA processing and chromatin modifications via the C-terminal domain (CTD) of its largest subunit, consisting of multiple repeats of the heptapeptide YSPTSPS involving a CTD kinase. The CTD cycle is uniform across genes. Proline isomerization is a key regulator of CTD dephosphorylation at the end of genes. Bur1 is a potent Ser5 and Ser7 kinase
physiological function
transcription by RNA polymerase II (RNAPII) is coupled to mRNA processing and chromatin modifications via the C-terminal domain (CTD) of its largest subunit, consisting of multiple repeats of the heptapeptide YSPTSPS involving a CTD kinase. The CTD cycle is uniform across genes. Proline isomerization is a key regulator of CTD dephosphorylation at the end of genes. Enzyme Ctk1 does not play any significant role in maintaining P-Ser5 and P-Ser7 levels in wild-type cells, the phosphorylation activity versus Ser5 and Ser7 is mainly in an opportunistic manner. Ctk1 is the major serine 2 kinase during transcription in vivo
physiological function
transcription by RNA polymerase II (RNAPII) is coupled to mRNA processing and chromatin modifications via the C-terminal domain (CTD) of its largest subunit, consisting of multiple repeats of the heptapeptide YSPTSPS involving a CTD kinase. The CTD cycle is uniform across genes. Proline isomerization is a key regulator of CTD dephosphorylation at the end of genes. Kin28 is the main CTD kinase. sThe kinase activity of Kin28 downregulates the activity of Bur1 against P-Ser5 and 7 along the coding region
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
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
physiological function
-
GSK-3 is a kinase involved in the transcriptional response to UV-induced DNA damage
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
-
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
-
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
-
additional information
structure and function of the CTDK-I complex, overview. Prediction of a possible CTD-binding domain (CID) in the N-terminal region of Ctk3 and of a three-helix bundle in the C-terminal region of Ctk3
additional information
-
structure and function of the CTDK-I complex, overview. Prediction of a possible CTD-binding domain (CID) in the N-terminal region of Ctk3 and of a three-helix bundle in the C-terminal region of Ctk3
Show AA Sequence and Transmembrane Helices (4006 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
-
tentatively alphabetagamma, 1 * 58000 + 1 * 38000 + 1 * 32000, SDS-PAGE
38000
-
tentatively alphabetagamma, 1 * 58000 + 1 * 38000 + 1 * 32000, SDS-PAGE
58000
-
tentatively alphabetagamma, 1 * 58000 + 1 * 38000 + 1 * 32000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
-
tentatively alphabetagamma, 1 * 58000 + 1 * 38000 + 1 * 32000, SDS-PAGE
additional information
additional information
cyclin K is associated with purified dCDK12, implicating it as the cyclin subunit of this CTD kinase
additional information
-
the three CTD kinase isozymes possess CDK-cyclin pairs, and TFIIH additionally forms a preinitiation complex, overview
additional information
-
enzymes from mouse consist of 2 components each: cdc2/p58: a cdc2 kinase (p34) and a p58 subunit, cdc2/p62: a cdc2 kinase and a p62 subunit (cyclin B), the latter is also called M phase-specific histone H1 kinase
additional information
-
enzymes from mouse consist of 2 components each: cdc2/p58: a cdc2 kinase (p34) and a p58 subunit, cdc2/p62: a cdc2 kinase and a p62 subunit (cyclin B), the latter is also called M phase-specific histone H1 kinase
additional information
BRD4 domain mapping by mass spectrometry, comparison of kinase subdomain architecture and organization of eukaryotic protein kinases and atypical protein kinases, overview
additional information
-
three specific subunits: Ctk1 is the catalytic subunit, Ctk2 is a catalytic subunit, Ctk3 is unknown in its function but the physical interaction betwenn Ctk2 and Ctk3 is neccesary for kinase activity and protects both subunits against degradation
additional information
the enzyme Ctk3 consists of a N-terminal CTD-interacting domain (CID) and a C-terminal three helix bundle domain. The structure reveals eight helices arranged into a right-handed superhelical fold. Ctk3 shows no binding to CTD peptides. Structure and function of the CTDK-I complex, overview. Ctk1 (Lsk1) associates with its cyclin partner Ctk2 (Lsc1) and a third subunit, Ctk3 (Lsg1), to form the CTD kinase I (CTDK-I) complex. This trimeric structure is unique amongst CDK complexes. The Ctk3 N-terminal domain has a noncanonical surface
additional information
-
the enzyme Ctk3 consists of a N-terminal CTD-interacting domain (CID) and a C-terminal three helix bundle domain. The structure reveals eight helices arranged into a right-handed superhelical fold. Ctk3 shows no binding to CTD peptides. Structure and function of the CTDK-I complex, overview. Ctk1 (Lsk1) associates with its cyclin partner Ctk2 (Lsc1) and a third subunit, Ctk3 (Lsg1), to form the CTD kinase I (CTDK-I) complex. This trimeric structure is unique amongst CDK complexes. The Ctk3 N-terminal domain has a noncanonical surface
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
recombinant BRD4, purified from insect SF9 cells, autophosphorylates, and recombinant BRD4 purified from Escherichia coli also autophosphorylates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminal domain of the Ctk3 homologue, hanging drop vapor diffusion method, mixing of 14.5 mg/ml protein in 50 mM HEPES pH 8.0, 50 mM NaCl, 1 mM DTT, with reservoir solution containing 26% PEG 6000, 100 mM citric acid, pH 4.0, 0.8 M lithium chloride, and 5 mM Tris(2-carboxyethyl)phosphin, 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D167N
-
dominant-negative mutant of CDK9, inhibits transcriptional activation by EBNA 2
K41M
-
CDK7 mutant, both EBNA 2-activated and basal transcription from Cp reporter construct are not particularly dependent on CDK7 kinase activity with only small effects observed in the presence of high levels of mutant K41M
D324N
T162A
the kin28-T162A allele, which does not display a slow growth phenotype, has reduced activity in vitro, but does not detectably affect CTD phosphorylation and capping enzymes recruitment in vivo
T17D
the mutant has decreased CTD kinase activity, a defect in capping enzyme recruitment, and is slow growing at 25°C and 37°C
T338A
-
amino acid substitution that does not affect catalytic function
T338A
-
amino acid substitution that does not affect catalytic function
-
additional information
additional information
-
loss of Ser2 phosphorylation through inactivation of the CTD kinase Cdk9 leads to a defect in processing but not in transcription elongation
additional information
-
knockdown of Cdk12 by expression of hairpin RNA
additional information
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)
additional information
-
DYRK1A expression is downregulated by lentiviral delivery of a DYRK1A-specific shRNA, reduction in expression of DYRK1A target genes in T98G and HeLa cells after DYRK1A knockdown with two shRNAs targeting different regions of DYRK1A
additional information
RNAi knockdown of hCDK12 in HeLa 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). siRNA knockdown of hCDK12 in HeLa cells results in alterations in the CTD phosphorylation state
additional information
RNAi knockdown of hCDK12 in HeLa 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). siRNA knockdown of hCDK12 in HeLa cells results in alterations in the CTD phosphorylation state
additional information
-
RNAi knockdown of hCDK12 in HeLa 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). siRNA knockdown of hCDK12 in HeLa cells results in alterations in the CTD phosphorylation state
additional information
RNAi knockdown of hCDK13 in HeLa 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)
additional information
RNAi knockdown of hCDK13 in HeLa 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)
additional information
-
RNAi knockdown of hCDK13 in HeLa 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)
additional information
-
the CDKC-1/CYCLINT-1 kinase complex can recombinantly restore the transcription activity of HeLA nuclear cell extracts depleted of endogenous CDK9 kinase complexes
additional information
-
construction of an enzyme-deficient ctk1DELTA mutant strain which shows selective abolishment of histone H3 Lys36 methylation
additional information
-
construction of several enzyme-deficient disruption mutant strains, overview, CTK1 can rescue the growth defects of an Ess1-deficient mutant at low concentration, but enhances the defects if overexpressed
additional information
-
ctk1 deletion affects pre-mRNA processing in vivo due to a defective recruitment of polyadenylation factors to the 3' end, but the mutation does not affect transcription termination, overview
additional information
-
the ctk1DELTA cells are defective in splicing
additional information
-
ctk1delta, CTK1 deletion, which nearly abolishes H3K4 monomethylation, but causes a significant increase in H3K4 di- and trimethylation, spread of H3K4 methylation in the ctk1delta strain is independent of Set2/K36 methylation, increased levels of cryptic initiation, RNA polymerase II elongation defects, or transcriptional stress
additional information
-
depletion of Ctk1, causes a defect in translation, impairment of growth, hypersensitivity to inhibitors of translation elongation, addition of increasing amounts of CTDK-I complex to the Ctk1-depleted extracts restores the translation elongation defect as well as the defect in correct decoding of the message in a dose-dependent manner
additional information
-
loss of Ser2 phosphorylation through inactivation of the CTD kinase Ctk1 in yeast leads to a defect in processing but not in transcription elongation, crosslinking of 3' end processing factors to the 3' end region of genes is dramatically decreased
additional information
-
a temperature-sensitive mutant and the analog-sensitive mutant of Kin28 is that upon heat inactivation, Kin28ts alleles are unable to retain protein interactions with other subunits of the TFIIH complex
additional information
-
Ctk1-depleted as well as substrate rps2 S238A mutant cells show a dfect in translation elongation through an increase in the frequency of miscoding, phenotype, overview
additional information
-
TK1 deletion nearly abolishes H3K4 monomethylation causing a significant increase in H3K4 di- and trimethylation. Both in individual genes and genome-wide, loss of CTK1 disrupts the H3K4 methylation patterns normally observed, H3K4me2 and H3K4me3 spread 3' into the bodies of genes, because H3K4 monomethylation is diminished, but restricted to the coding regions of RNAP II transcribed genes, overview
additional information
generation of a bur1 knockout mutant bur1DELTA
additional information
generation of a bur1 knockout mutant bur1DELTA
additional information
generation of a bur1 knockout mutant bur1DELTA
additional information
generation of a ctk1 knockout mutant ctk1DELTA
additional information
generation of a ctk1 knockout mutant ctk1DELTA
additional information
generation of a ctk1 knockout mutant ctk1DELTA
additional information
-
construction of an enzyme-deficient ctk1DELTA mutant strain which shows selective abolishment of histone H3 Lys36 methylation
-
additional information
-
ctk1delta, CTK1 deletion, which nearly abolishes H3K4 monomethylation, but causes a significant increase in H3K4 di- and trimethylation, spread of H3K4 methylation in the ctk1delta strain is independent of Set2/K36 methylation, increased levels of cryptic initiation, RNA polymerase II elongation defects, or transcriptional stress
-
additional information
-
TK1 deletion nearly abolishes H3K4 monomethylation causing a significant increase in H3K4 di- and trimethylation. Both in individual genes and genome-wide, loss of CTK1 disrupts the H3K4 methylation patterns normally observed, H3K4me2 and H3K4me3 spread 3' into the bodies of genes, because H3K4 monomethylation is diminished, but restricted to the coding regions of RNAP II transcribed genes, overview
-
additional information
-
construction of ctk-disruption mutant strains displaying defects in nucleolar structure, the RNA polymerase I functions less effective in the mutant cells, the in vitro transcription is impaired
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified mouse enzymes are rather unstable with a half-life of several days, bovine serum albumin does not stabilize
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native hCDK13 from nuclear extracts of HeLa cells by Ion exchange chromatography and affinity chromatography, recombinant His-tagged chimeric mutant Ctk1/13 kinase from Saccharomyces cerevisiae strain FY23 by cation exchange chromatography and nickel affinity chromatography
native TFIIK, and native CTD kinase 1 by a tandem affinity purification method
-
partial
purification of either recombinant Myc-tagged Ctk1 and recombinant HA-tagged Ctk1 in complex with RNA polymerase I by several chromatographic steps
-
recombinant BRD4 from Escherichia coli and from Spodoptera frugiperda Sf9 insect cells
recombinant C-terminally His6-tagged wildtype and selenomethionine-labeled Ctk3 and the Ctk3 N-terminal domain from Escherichia coli strain BL21(DE3)RIL or strain B834 by nickel affinity chromatography, dialysis, tag removal by thrombin cleavage, followed by anion exchange chromatography and gel filtration
recombinant His-tagged CDKC-1 from Escherichia coli by nickel affinity chromatography, native CDKC-1 partially from cell suspension cultured cells by immunoprecipitation, immobilization of the enzyme on protein A agarose
-
recombinant His-tagged chimeric mutant Ctk1/12 kinase from Saccharomyces cerevisiae strain FY23 by cation exchange chromatography and nickel affinity chromatography
recombinant His-tagged chimeric mutant Ctk1/12 kinase from Saccharomyces cerevisiae strain FY23 by cation exchange chromatographyand nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of genetic interaction between ESS1 and CTD kinase genes, overexpression of wild-type and mutant CTD kinases Ctk1, Bur1, Kin28, and Srb10 in wild-type or mutant yeast strains, the latter being deficient in enzyme activity or in Ess1, overview
-
cDNA copy of cdk9HA placed into a lentiviral vector where its transcription is driven by an EF1alpha promoter, overexpression in HFF cells
dCDK12, recombinant expression of the His-tagged chimeric mutant Ctk1/12 kinase in Saccharomyces cerevisiae strain FY23
expression of HA-tagged Ctk1 and of Myc-tagged Ctk1 in strain HIS5
-
expression of plasmid-encoded Ctk1 in enzyme-deficient ctk1DELTA mutant strain
-
expression of the substrate as GST-CTD fusion protein in Escherichia coli
-
gene CRK9, quantitative real-time reverse transcription-PCR expression analysis
-
hCDK12, recombinant expression of the His-tagged chimeric mutant Ctk1/12 kinase in Saccharomyces cerevisiae strain FY23
hCDK13, recombinant expression of the His-tagged chimeric mutant Ctk1/13 kinase in Saccharomyces cerevisiae strain FY23
in vitro transcription of CDKC-1, transient co-expression of Myc-tagged CDKC-1 and HA-tagged CYCLINT in Arabidopsis thaliana protoplasts for transcription analysis, expression of CDKC-1 as His-tagged and as GST-tagge protein in Escherichia coli strain BL21(DE3)
-
recombinant expression of BRD4 in Escherichia coli and in Spodoptera frugiperda Sf9 insect cells, in vitro transcription was done using HeLa nuclear extract and the MHC I gene promoter in the presence of ATP
recombinant expression of C-terminally His6-tagged Ctk3 (residues 1-218) and the Ctk3 N-terminal domain (residues 1-140) in Escherichia coli strain BL21(DE3)RIL or in strain B834 for the selenomethionine-labeled variants
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
medicine
IE2 and multiple cellular factors needed for viral RNA synthesis accumulate within the first 8 h at the viral transcriptosome, functional cdk activity is required for the specific recruitment of cdk7 and cdk9 during this time interval
medicine
the bromodomain protein, BRD4, is a therapeutic target in acute myeloid leukemia, multiple myeloma, Burkitts lymphoma, NUT midline carcinoma, colon cancer, and inflammatory disease. Loss of the enzyme BRD4 is a prognostic signature for metastatic breast cancer
additional information
-
Ctk1 controls the maintenance of suppressive chromatin in the coding regions of genes by both promoting H3K36 methylation, which leads to histone deacetylation, and preventing the 3' spread of H3K4 trimethylation, a mark associated with transcriptional initiation
additional information
-
functions in translation by enhancing decoding fidelity, Ctk1 interacts with the transcription and mRNA export complex, which couples transcription to mRNA export, may bind to correctly processed mRNPs during transcription and accompany the mRNP to the ribosomes in the cytoplasm, where Ctk1 enhances efficient and accurate translation of the mRNA, function of Ctk1 in translation seems to be conserved in evolution
additional information
-
required for accurate transcription initiation and transcription elongation
additional information
-
Ctk1 controls the maintenance of suppressive chromatin in the coding regions of genes by both promoting H3K36 methylation, which leads to histone deacetylation, and preventing the 3' spread of H3K4 trimethylation, a mark associated with transcriptional initiation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cisek, L.J.; Corden, J.L.
Purification of protein kinases that phosphorylate the repetitive carboxyl-terminal domain of eukaryotic RNA polymerase II
Methods Enzymol.
200
301-325
1991
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Triticum aestivum
brenda
Lee, J.M.; Greenleaf, A.L.
A protein kinase that phosphorylates the C-terminal repeat domain of the largest subunit of RNA polymerase II
Proc. Natl. Acad. Sci. USA
86
3624-3628
1989
Saccharomyces cerevisiae, Drosophila sp. (in: flies), Homo sapiens, Drosophila sp. (in: flies) Kc
brenda
Stevens, A.; Maupin, M.K.
5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits a HeLa protein kinase that phosphorylates an RNA polymerase II-derived peptide
Biochem. Biophys. Res. Commun.
159
508-515
1989
Homo sapiens
brenda
Feuerstein, N.
Phosphorylation of numatrin and other nuclear proteins by cdc2 containing CTD kinase cdc2/p58
J. Biol. Chem.
266
16200-16206
1991
Mus musculus
brenda
Payne, J.M.; Dahmus, M.E.
Partial purification and characterization of two distinct protein kinases that differentially phosphorylate the carboxyl-terminal domain of RNA polymerase subunit IIa
J. Biol. Chem.
268
80-87
1993
Homo sapiens
brenda
Dvir, A.; Stein, L.Y.; Calore, B.L.; Dynan, W.S.
Purification and characterization of a template-associated protein kinase that phosphorylates RNA polymerase II
J. Biol. Chem.
268
10440-10447
1993
Homo sapiens
brenda
Guilfoyle, T.J.
A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II
Plant Cell
1
827-836
1989
Triticum aestivum
brenda
Stone, N.; Reinberg, D.
Protein kinases from Aspergillus nidulans that phosphorylate the carboxyl-terminal domain of the largest subunit of RNA polymerase II
J. Biol. Chem.
267
6353-6360
1992
Aspergillus sp.
brenda
Morris, D.P.; Lee, J.M.; Sterner, D.E.; Brickey, W.J.; Greenleaf, A.L.
Assaying CTD kinases in vitro and phosphorylation-modulated properties of RNA polymerase II in vivo
Methods
12
264-275
1997
Saccharomyces cerevisiae
brenda
Baskaran, R.; Escobar, S.R.; Wang, J.Y.
Nuclear c-Abl is a COOH-terminal repeated domain (CTD)-tyrosine (CTD)-tyrosine kinase-specific for the mammalian RNA polymerase II: possible role in transcription elongation
Cell Growth Differ.
10
387-396
1999
Mus musculus
brenda
Skaar, D.A.; Greenleaf, A.L.
The RNA polymerase II CTD kinase CTDK-I affects pre-mRNA 3' cleavage/polyadenylation through the processing component Pti1p
Mol. Cell
10
1429-1439
2002
Saccharomyces cerevisiae
brenda
Jona, G.; Wittschieben, B.O.; Svejstrup, J.Q.; Gileadi, O.
Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in transcription elongation in vivo
Gene
267
31-36
2001
Saccharomyces cerevisiae
brenda
Prelich, G.
RNA polymerase II carboxy-terminal domain kinases: emerging clues to their function
Eukaryot. Cell
1
153-162
2002
Saccharomyces cerevisiae, Drosophila sp. (in: flies), Mus musculus
brenda
Hautbergue, G.; Goguel, V.
Activation of the cyclin-dependent kinase CTDK-I requires the heterodimerization of two unstable subunits
J. Biol. Chem.
276
8005-8013
2001
Saccharomyces cerevisiae
brenda
Patturajan, M.; Conrad, N.K.; Bregman, D.B.; Corden, J.L.
Yeast carboxyl-terminal domain kinase I positively and negatively regulates RNA polymerase II carboxyl-terminal domain phosphorylation
J. Biol. Chem.
274
27823-27828
1999
Saccharomyces cerevisiae
brenda
Phatnani, H.P.; Jones, J.C.; Greenleaf, A.L.
Expanding the functional repertoire of CTD kinase I and RNA polymerase II: novel phosphoCTD-associating proteins in the yeast proteome
Biochemistry
43
15702-15719
2004
Saccharomyces cerevisiae
brenda
Medlin, J.E.; Uguen, P.; Taylor, A.; Bentley, D.L.; Murphy, S.
The C-terminal domain of pol II and a DRB-sensitive kinase are required for 3' processing of U2 snRNA
EMBO J.
22
925-934
2003
Homo sapiens
brenda
Kim, M.; Ahn, S.H.; Krogan, N.J.; Greenblatt, J.F.; Buratowski, S.
Transitions in RNA polymerase II elongation complexes at the 3' ends of genes
EMBO J.
23
354-364
2004
Saccharomyces cerevisiae
brenda
Palancade, B.; Bensaude, O.
Investigating RNA polymerase II carboxyl-terminal domain (CTD) phosphorylation
Eur. J. Biochem.
270
3859-3870
2003
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Schizosaccharomyces pombe
brenda
Xiao, T.; Hall, H.; Kizer, K.O.; Shibata, Y.; Hall, M.C.; Borchers, C.H.; Strahl, B.D.
Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast
Genes Dev.
17
654-663
2003
Saccharomyces cerevisiae, Saccharomyces cerevisiae AS4
brenda
Wilcox, C.B.; Rossettini, A.; Hanes, S.D.
Genetic interactions with C-terminal domain (CTD) kinases and the CTD of RNA Pol II suggest a role for ESS1 in transcription initiation and elongation in Saccharomyces cerevisiae
Genetics
167
93-105
2004
Saccharomyces cerevisiae
brenda
Jones, J.C.; Phatnani, H.P.; Haystead, T.A.; MacDonald, J.A.; Alam, S.M.; Greenleaf, A.L.
C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA polymerase II C-terminal domain repeats
J. Biol. Chem.
279
24957-24964
2004
Saccharomyces cerevisiae
brenda
Kong, S.E.; Kobor, M.S.; Krogan, N.J.; Somesh, B.P.; Sogaard, T.M.; Greenblatt, J.F.; Svejstrup, J.Q.
Interaction of Fcp1 phosphatase with elongating RNA polymerase II holoenzyme, enzymatic mechanism of action, and genetic interaction with elongator
J. Biol. Chem.
280
4299-4306
2005
Saccharomyces cerevisiae
brenda
Tamrakar, S.; Kapasi, A.J.; Spector, D.H.
Human cytomegalovirus infection induces specific hyperphosphorylation of the carboxyl-terminal domain of the large subunit of RNA polymerase II that is associated with changes in the abundance, activity, and localization of cdk9 and cdk7
J. Virol.
79
15477-15493
2005
Homo sapiens
brenda
Jacobs, E.Y.; Ogiwara, I.; Weiner, A.M.
Role of the C-terminal domain of RNA polymerase II in U2 snRNA transcription and 3' processing
Mol. Cell. Biol.
24
846-855
2004
Homo sapiens
brenda
Ahn, S.H.; Kim, M.; Buratowski, S.
Phosphorylation of serine 2 within the RNA polymerase II C-terminal domain couples transcription and 3' end processing
Mol. Cells
13
67-76
2004
Saccharomyces cerevisiae
brenda
Bouchoux, C.; Hautbergue, G.; Grenetier, S.; Carles, C.; Riva, M.; Goguel, V.
CTD kinase I is involved in RNA polymerase I transcription
Nucleic Acids Res.
32
5851-5860
2004
Schizosaccharomyces pombe
brenda
Fulop, K.; Pettko-Szandtner, A.; Magyar, Z.; Miskolczi, P.; Kondorosi, E.; Dudits, D.; Bako, L.
The Medicago CDKC;1-CYCLINT;1 kinase complex phosphorylates the carboxy-terminal domain of RNA polymerase II and promotes transcription
Plant J.
42
810-820
2005
Medicago sativa
brenda
Roether, S.; Straesser, K.
The RNA polymerase II CTD kinase Ctk1 functions in translation elongation
Genes Dev.
21
1409-1421
2007
Saccharomyces cerevisiae
brenda
Hirose, Y.; Ohkuma, Y.
Phosphorylation of the C-terminal domain of RNA polymerase II plays central roles in the integrated events of eucaryotic gene expression
J. Biochem.
141
601-608
2007
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Xenopus laevis
brenda
Sogaard, T.M.; Svejstrup, J.Q.
Hyperphosphorylation of the C-terminal repeat domain of RNA polymerase II facilitates dissociation of its complex with mediator
J. Biol. Chem.
282
14113-14120
2007
Saccharomyces cerevisiae
brenda
Kapasi, A.J.; Spector, D.H.
Inhibition of the cyclin-dependent kinases at the beginning of the human cytomegalovirus infection specifically alters the levels and localization of the RNA polymerase II carboxyl-terminal domain kinases cdk9 and cdk7 at the viral transcriptosome
J. Virol.
82
394-407
2007
Homo sapiens, Homo sapiens (P50613), Homo sapiens (P50750)
brenda
Xiao, T.; Shibata, Y.; Rao, B.; Laribee, R.N.; ORourke, R.; Buck, M.J.; Greenblatt, J.F.; Krogan, N.J.; Lieb, J.D.; Strahl, B.D.
The RNA polymerase II kinase Ctk1 regulates positioning of a 5 histone methylation boundary along genes
Mol. Cell. Biol.
27
721-731
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Bark-Jones, S.J.; Webb, H.M.; West, M.J.
EBV EBNA 2 stimulates CDK9-dependent transcription and RNA polymerase II phosphorylation on serine 5
Oncogene
25
1775-1785
2006
Homo sapiens
brenda
Bres, V.; Yoh, S.M.; Jones, K.A.
The multi-tasking P-TEFb complex
Curr. Opin. Cell Biol.
20
334-340
2008
Saccharomyces cerevisiae
brenda
Ni, Z.; Saunders, A.; Fuda, N.J.; Yao, J.; Suarez, J.R.; Webb, W.W.; Lis, J.T.
P-TEFb is critical for the maturation of RNA polymerase II into productive elongation in vivo
Mol. Cell. Biol.
28
1161-1170
2008
Drosophila melanogaster
brenda
Youdell, M.L.; Kizer, K.O.; Kisseleva-Romanova, E.; Fuchs, S.M.; Duro, E.; Strahl, B.D.; Mellor, J.
Roles for Ctk1 and Spt6 in regulating the different methylation states of histone H3 lysine 36
Mol. Cell. Biol.
28
4915-4926
2008
Saccharomyces cerevisiae (Q03957)
brenda
Bennett, C.B.; Westmoreland, T.J.; Verrier, C.S.; Blanchette, C.A.; Sabin, T.L.; Phatnani, H.P.; Mishina, Y.V.; Huper, G.; Selim, A.L.; Madison, E.R.; Bailey, D.D.; Falae, A.I.; Galli, A.; Olson, J.A.; Greenleaf, A.L.; Marks, J.R.
Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction
PLoS ONE
3
e1448
2008
Saccharomyces cerevisiae
brenda
Kanin, E.I.; Kipp, R.T.; Kung, C.; Slattery, M.; Viale, A.; Hahn, S.; Shokat, K.M.; Ansari, A.Z.
Chemical inhibition of the TFIIH-associated kinase Cdk7/Kin28 does not impair global mRNA synthesis
Proc. Natl. Acad. Sci. USA
104
5812-5817
2007
Saccharomyces cerevisiae
brenda
Heidemann, M.; Hintermair, C.; Vo, K.; Eick, D.
Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription
Biochim. Biophys. Acta
1829
55-62
2013
Schizosaccharomyces pombe (O14098), Schizosaccharomyces pombe (Q12126), Schizosaccharomyces pombe (Q96WV9), Saccharomyces cerevisiae (P06242), Saccharomyces cerevisiae (P23293), Saccharomyces cerevisiae (P39073), Saccharomyces cerevisiae (Q03957), Homo sapiens (P49336), Homo sapiens (P50613), Homo sapiens (P50750), Homo sapiens (Q9H4B4), Drosophila melanogaster (Q24216), Drosophila melanogaster (Q9VT57), Schizosaccharomyces pombe ATCC 24843 (O14098), Schizosaccharomyces pombe ATCC 24843 (Q12126), Schizosaccharomyces pombe ATCC 24843 (Q96WV9)
brenda
Bartkowiak, B.; Liu, P.; Phatnani, H.P.; Fuda, N.J.; Cooper, J.J.; Price, D.H.; Adelman, K.; Lis, J.T.; Greenleaf, A.L.
CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1
Genes Dev.
24
2303-2316
2010
Homo sapiens (Q14004), Homo sapiens (Q9NYV4), Homo sapiens, Drosophila melanogaster (Q9VP22)
brenda
Tyagi, S.; Ochem, A.; Tyagi, M.
DNA-dependent protein kinase interacts functionally with the RNA polymerase II complex recruited at the human immunodeficiency virus (HIV) long terminal repeat and plays an important role in HIV gene expression
J. Gen. Virol.
92
1710-1720
2011
Homo sapiens
brenda
Badjatia, N.; Ambrosio, D.L.; Lee, J.H.; Guenzl, A.
Trypanosome cdc2-related kinase 9 controls spliced leader RNA cap4 methylation and phosphorylation of the RNA polymerase II subunit RPB1
Mol. Cell. Biol.
33
1965-1975
2013
Trypanosoma brucei
brenda
Bataille, A.R.; Jeronimo, C.; Jacques, P.E.; Laramee, L.; Fortin, M.E.; Forest, A.; Bergeron, M.; Hanes, S.D.; Robert, F.
A universal RNA polymerase II CTD cycle is orchestrated by complex interplays between kinase, phosphatase, and isomerase enzymes along genes
Mol. Cell
45
158-170
2012
Saccharomyces cerevisiae (P06242), Saccharomyces cerevisiae (P23293), Saccharomyces cerevisiae (Q03957)
brenda
Di Vona, C.; Bezdan, D.; Islam, A.B.; Salichs, E.; Lopez-Bigas, N.; Ossowski, S.; de la Luna, S.
Chromatin-wide profiling of DYRK1A reveals a role as a gene-specific RNA polymerase II CTD kinase
Mol. Cell
57
506-520
2015
Homo sapiens
brenda
Allepuz-Fuster, P.; Martinez-Fernandez, V.; Garrido-Godino, A.I.; Alonso-Aguado, S.; Hanes, S.D.; Navarro, F.; Calvo, O.
Rpb4/7 facilitates RNA polymerase II CTD dephosphorylation
Nucleic Acids Res.
42
13674-13688
2014
Saccharomyces cerevisiae (P06242), Saccharomyces cerevisiae (P39073), Saccharomyces cerevisiae (Q03957)
brenda
Devaiah, B.N.; Lewis, B.A.; Cherman, N.; Hewitt, M.C.; Albrecht, B.K.; Robey, P.G.; Ozato, K.; Sims, R.J.; Singer, D.S.
BRD4 is an atypical kinase that phosphorylates serine2 of the RNA polymerase II carboxy-terminal domain
Proc. Natl. Acad. Sci. USA
109
6927-6932
2012
Mus musculus (Q9ESU6)
brenda
Muehlbacher, W.; Mayer, A.; Sun, M.; Remmert, M.; Cheung, A.C.; Niesser, J.; Soeding, J.; Cramer, P.
Structure of Ctk3, a subunit of the RNA polymerase II CTD kinase complex, reveals a noncanonical CTD-interacting domain fold
Proteins
83
1849-1858
2015
Schizosaccharomyces pombe (Q9USJ8), Schizosaccharomyces pombe
brenda
Li, X.; Chatterjee, N.; Spirohn, K.; Boutros, M.; Bohmann, D.
Cdk12 is a gene-selective RNA polymerase II kinase that regulates a subset of the transcriptome, including Nrf2 target genes
Sci. Rep.
6
21455
2016
Drosophila melanogaster
brenda
Narita, T.; Ishida, T.; Ito, A.; Masaki, A.; Kinoshita, S.; Suzuki, S.; Takino, H.; Yoshida, T.; Ri, M.; Kusumoto, S.; Komatsu, H.; Imada, K.; Tanaka, Y.; Takaori-Kondo, A.; Inagaki, H.; Scholz, A.; Lienau, P.; Kuroda, T.; Ueda, R.; Iida, S.
Cyclin-dependent kinase 9 is a novel specific molecular target in adult T-cell leukemia/lymphoma
Blood
130
1114-1124
2017
Mus musculus (Q99J95)
brenda
Duan, J.; Liu, Q.; Su, S.; Cha, J.; Zhou, Y.; Tang, R.; Liu, X.; Wang, Y.; Liu, Y.; He, Q.
The Neurospora RNA polymerase II kinase CTK negatively regulates catalase expression in a chromatin context-dependent manner
Environ. Microbiol.
22
76-90
2020
Neurospora crassa, Neurospora crassa 87-3
brenda
Donnio, L.M.; Lagarou, A.; Sueur, G.; Mari, P.O.; Giglia-Mari, G.
CSB-dependent cyclin-dependent kinase 9 degradation and RNA polymerase II phosphorylation during transcription-coupled repair
Mol. Cell. Biol.
39
e00225-18
2019
Homo sapiens (P50750)
brenda
Nieto Moreno, N.; Villafanez, F.; Giono, L.E.; Cuenca, C.; Soria, G.; Munoz, M.J.; Kornblihtt, A.R.
GSK-3 is an RNA polymerase II phospho-CTD kinase
Nucleic Acids Res.
48
6068-6080
2020
Homo sapiens
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.11.23)
Transporter Classification Database (TCDB): 1.I.1.1.3
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
