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Information on EC 2.7.11.22 - cyclin-dependent kinase and Organism(s) Homo sapiens

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IUBMB Comments
Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
cyclin-dependent kinase, cdk, p34cdc2, cdkl5, cdc2 kinase, cyclin-dependent kinase 5, cyclin-dependent kinase 2, cdc28, cyclin-dependent kinase 4, cyclin-dependent kinase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cdc2
-
-
CDC2 kinase
-
-
CDC2deltaT
a variant of human CDC2, that lacks 171 nucleotides corresponding to 57 amino acids, which compose most of the T-loop
Cdk 2
-
-
Cdk1/Cyclin B
-
-
Cdk1/cyclin B1 kinase
-
-
CDK10
-
-
CDK11
-
-
CDK11p110
-
CDK12
isoform
CDK13
isoform
CDK3
-
-
CDK4 kinase
-
-
cdk5/p25 kinase
-
-
cell division control protein 2 homolog
-
cell division cycle 2-related protein kinase 7
-
cell division protein kinase 10
-
cell division protein kinase 3
-
cell division protein kinase 4
-
cell division protein kinase 5
-
cell division protein kinase 6
-
cell division protein kinase 7
-
cell division protein kinase 9
-
cyclin A-cyclin-dependent kinase 2
-
-
cyclin A-dependent protein kinase 2
-
-
cyclin A/Cdk2
-
-
cyclin A2/Cdk2
-
-
cyclin dependent kinase 2
-
-
cyclin-dependent kinase
-
-
cyclin-dependent kinase 1
cyclin-dependent kinase 11p110
-
cyclin-dependent kinase 11p58
-
-
cyclin-dependent kinase 2
cyclin-dependent kinase 4
-
-
cyclin-dependent kinase 5
cyclin-dependent kinase 6
-
-
cyclin-dependent kinase 7
cyclin-dependent kinase 8
-
cyclin-dependent kinase 9
Cyclin-dependent kinase pef1
-
-
-
-
cyclin-dependent kinase-2
cyclin-dependent kinase-8
-
-
cyclin-dependent kinases 7
-
-
cyclin-dependent kinases 9
-
-
cyclin-dependent protein kinase 5
-
-
galactosyltransferase associated protein kinase p58/GTA
-
K-cyclin/cdk6 kinase
-
-
kinase Cdk6
-
male germ cell-associated kinase
-
MO15/CDK7
-
p25-Cdk5 kinase complex
-
-
p27 cyclin dependent kinase
-
-
p58clk-1 protein kinase
-
PFTK1
-
-
PFTK1/CCND3 complex
-
-
PHO85 homolog
-
-
-
-
PITSLRE
formerly
serine/threonine kinase p
-
serine/threonine protein kinase PCTAIRE-3
-
serine/threonine-protein kinase ALS2CR7
-
serine/threonine-protein kinase KKIALRE
-
serine/threonine-protein kinase MAK
-
serine/threonine-protein kinase PCTAIRE-1
-
serine/threonine-protein kinase PCTAIRE-2
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
show the reaction diagram
catalytic aspartate residue
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:cyclin phosphotransferase
Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.
CAS REGISTRY NUMBER
COMMENTARY hide
150428-23-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + phosphorylated protein
show the reaction diagram
-
-
-
-
?
ATP + axonal cytoskeleton protein
ADP + phosphorylated axonal cytoskeleton protein
show the reaction diagram
ATP + biotin-TVSEESNVLCLSKSPNKHNRLYMKARPFF
ADP + biotin-TVSEESNVLCLSKpSPNKHNRLYMKARPFF
show the reaction diagram
-
-
phosphorylated on Ser595
-
?
ATP + bloom syndrome helicase
ADP + phosphorylated bloom syndrome helicase
show the reaction diagram
ATP + BRCA2
ADP + phosphorylated BRCA2
show the reaction diagram
ATP + c-Jun N-terminal kinase 3
ADP + phosphorylated c-Jun N-terminal kinase 3
show the reaction diagram
ATP + C-terminal domain of RNA polymerase II
ADP + phosphorylated C-terminal domain of RNA polymerase II
show the reaction diagram
ATP + CALD1 protein
ADP + CALD1 phosphoprotein
show the reaction diagram
-
reccombinant human GST-tagged substrate, with CDK6
-
-
?
ATP + Cdc20
ADP + phosphorylated Cdc20
show the reaction diagram
ATP + Cdc6
ADP + phosphorylated Cdc6
show the reaction diagram
-
-
-
-
?
ATP + CDK1
ADP + phosphorylated CDK1
show the reaction diagram
-
CDK7 phosphorylates the activation segment or T-loop of CDK1
-
-
?
ATP + Cdk1
ADP + phosphorylated Cdk2
show the reaction diagram
-
Cdk7
-
-
?
ATP + cdk2
ADP + phosphorylated cdk2
show the reaction diagram
-
CDK7 phosphorylates the activation segment or T-loop of CDK2
-
-
?
ATP + CDK9
ADP + phosphorylated CDK9
show the reaction diagram
-
-
-
?
ATP + Cprk
ADP + phosphorylated Cprk
show the reaction diagram
-
i.e. Cdk5/p35-regulated kinase
-
-
?
ATP + CREB-binding protein
ADP + phosphorylated CREB-binding protein
show the reaction diagram
-
-
-
-
?
ATP + cyclin H protein
ADP + cyclin H phosphoprotein
show the reaction diagram
-
CDK8
-
-
?
ATP + Dab1 protein
ADP + Dab1 phosphoprotein
show the reaction diagram
ATP + dephosphin
ADP + phosphorylated dephosphin
show the reaction diagram
ATP + DNA polymerase alpha
ADP + phosphorylated DNA polymerase alpha
show the reaction diagram
-
-
-
-
?
ATP + DNA polymerase sigma
ADP + phosphorylated DNA polymerase sigma
show the reaction diagram
-
-
-
-
?
ATP + E2F1 protein
ADP + E2F1 phosphoprotein
show the reaction diagram
-
CDK8
-
-
?
ATP + early mitotic inhibitor 1 protein
ADP + early mitotic inhibitor 1 phosphoprotein
show the reaction diagram
ATP + ErbB2
ADP + phosphorylated ErbB2
show the reaction diagram
ATP + ErbB3
ADP + phosphorylated ErbB3
show the reaction diagram
ATP + estrogen receptor
ADP + phosphorylated estrogen receptor
show the reaction diagram
-
Cdk2 phosphorylation at Ser104 and Ser106
-
-
?
ATP + eukaryotic elongation factor 2
ADP + phosphorylated eukaryotic elongation factor 2
show the reaction diagram
ATP + ezrin
ADP + phosphorylated ezrin
show the reaction diagram
-
phosphorylation by cdk5 at Thr235 in the NH2-terminal region and consequent dissociation of Rho GDP dissociation inhibitor from an ezrin/Rho-GDI complex
-
-
?
ATP + glucocorticoid receptor
ADP + phosphorylated glucocorticoid receptor
show the reaction diagram
-
-
-
-
?
ATP + HHASPRK
ADP + HHAS(P)PRK
show the reaction diagram
-
-
-
-
?
ATP + HHASPRK
ADP + phosphorylated HHASPRK
show the reaction diagram
-
-
-
-
?
ATP + histone 1
ADP + phosphorylated histone 1
show the reaction diagram
ATP + histone H1
ADP + phosphorylated histone H1
show the reaction diagram
ATP + histone H1
ADP + phosphorylated steroid histone H1
show the reaction diagram
-
-
-
-
?
ATP + histone H1-derived peptide
ADP + histone H1-derived peptide phosphate
show the reaction diagram
-
-
-
-
?
ATP + histone H3 protein
ADP + histone H3 phosphoprotein
show the reaction diagram
-
CDK8
-
-
?
ATP + human cytomegalovirus tegument protein pp65
ADP + phosphorylated human cytomegalovirus tegument protein pp65
show the reaction diagram
-
-
-
-
?
ATP + huntingtin
ADP + phosphorylated huntingtin
show the reaction diagram
-
-
-
?
ATP + Mcm3
ADP + phosphorylated Mcm3
show the reaction diagram
-
-
-
-
?
ATP + Mcm4
ADP + phosphorylated Mcm4
show the reaction diagram
-
-
-
-
?
ATP + Med13 protein
ADP + Med13 phosphoprotein
show the reaction diagram
-
CDK8
-
-
?
ATP + MEK1
ADP + phosphorylated MEK1
show the reaction diagram
ATP + MEP50 protein
ADP + MEP50 phosphoprotein
show the reaction diagram
ATP + Munc-18
ADP + phosphorylated Munc-18
show the reaction diagram
ATP + NF-H
ADP + phosphorylated NF-H
show the reaction diagram
ATP + NF-M
ADP + phosphorylated NF-M
show the reaction diagram
ATP + NR1 receptor
ADP + phosphorylated NR1 receptor
show the reaction diagram
ATP + NR2 receptor
ADP + phosphorylated NR2 receptor
show the reaction diagram
ATP + Orc2
ADP + phosphorylated Orc2
show the reaction diagram
-
-
-
-
?
ATP + Orc6
ADP + phosphorylated Orc6
show the reaction diagram
-
-
-
-
?
ATP + p35 protein
ADP + p35 phosphoprotein
show the reaction diagram
-
a nuclear transcription factor, Cdk5-p25 phosphorylates p53 on Ser15, Ser33, and Ser44
-
-
?
ATP + parkin
ADP + phosphorylated parkin
show the reaction diagram
ATP + PKTPKKAKKL
ADP + PKpTPKKAKKL
show the reaction diagram
ATP + pocket protein p107
ADP + phosphorylated pocket protein 107
show the reaction diagram
ATP + pocket protein p130
ADP + phosphorylated pocket protein 130
show the reaction diagram
ATP + polymerase II C-terminal domain
ADP + phosphorylated polymerase II C-terminal domain
show the reaction diagram
-
-
-
?
ATP + progesterone receptor
ADP + phosphorylated progesterone receptor
show the reaction diagram
ATP + promyelocytic leukemia zinc finger
ADP + phosphorylated promyelocytic leukemia zinc finger
show the reaction diagram
can also be phosphorylated by CDK1 albeit in a less efficient fashion than by CDK2
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
ATP + protein tau
ADP + protein tau phosphate
show the reaction diagram
-
-
-
-
?
ATP + Rb peptide
ADP + Rb phosphopeptide
show the reaction diagram
-
from retinoblastoma-associated protein
-
-
?
ATP + replication factor C
ADP + phosphorylated replication factor C
show the reaction diagram
-
-
-
-
?
ATP + retinoblastoma protein
ADP + phosphorylated retinoblastoma protein
show the reaction diagram
ATP + retinoblastoma protein
ADP + retinoblastoma phosphoprotein
show the reaction diagram
ATP + RNA polymerase II
ADP + phosphorylated RNA polymerase II
show the reaction diagram
ATP + RNA polymerase II C-terminal domain
ADP + phosphorylated RNA polymerase II C-terminal domain
show the reaction diagram
ATP + RNA polymerase II C-terminal domain protein
ADP + RNA polymerase II C-terminal domain phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + RNA polymerase II carboxy-terminal domain
ADP + phosphorylated RNA polymerase II carboxy-terminal domain
show the reaction diagram
-
CDK8
-
-
?
ATP + RXL motif-containing peptide
ADP + RXL motif-containing phosphopeptide
show the reaction diagram
-
peptide sequence corresponding to amino acids 866-880 of RNA polymerase II C-terminal domain. Substrate phosphorylation by CDK6 with K-cyclin from Kaposi sarcoma herpesvirus, but addition of this peptide significantly reduces substrate phosphorylation by cyclin E-CDK2 and cyclin D2-CDK6
-
-
?
ATP + SCR-1
ADP + phosphorylated SCR-1
show the reaction diagram
ATP + SIRT2
ADP + phosphorylated SIRT2
show the reaction diagram
-
-
-
?
ATP + SMAD protein
ADP + SMAD phosphoprotein
show the reaction diagram
-
CDK8
-
-
?
ATP + STAT3
ADP + phosphorylated STAT3
show the reaction diagram
-
substrate of CDK5
-
-
?
ATP + STAT3 protein
ADP + STAT3 phosphoprotein
show the reaction diagram
-
Cdk5 phosphorylates at Ser727
-
-
?
ATP + STAU2
ADP + phosphorylated STAU2
show the reaction diagram
ATP + steroid receptor coactivator-1
ADP + phosphorylated steroid receptor coactivator-1
show the reaction diagram
-
-
-
-
?
ATP + steroidogenic factor 1
ADP + phosphorylated steroidogenic factor 1
show the reaction diagram
also known as Ad4BP, systematic name NR5A1, the phosphorylation site is at Ser203
-
-
?
ATP + T-cell protein tyrosine phosphatase
ADP + phosphorylated T-cell protein tyrosine phosphatase
show the reaction diagram
ATP + tau protein
ADP + phosphorylated tau protein
show the reaction diagram
ATP + Tau protein
ADP + Tau phosphoprotein
show the reaction diagram
ATP + tumor suppressor Rb
ADP + phosphorylated tumor suppressor Rb
show the reaction diagram
-
-
-
-
?
ATP + VGCC
ADP + phosphorylated NR1 receptor
show the reaction diagram
ATP + Wee1A
ADP + phosphorylated Wee1A
show the reaction diagram
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
show the reaction diagram
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + phosphorylated protein
show the reaction diagram
-
-
-
-
?
ATP + axonal cytoskeleton protein
ADP + phosphorylated axonal cytoskeleton protein
show the reaction diagram
-
regulated by integrin alpha1beta1
-
-
?
ATP + bloom syndrome helicase
ADP + phosphorylated bloom syndrome helicase
show the reaction diagram
-
-
-
-
?
ATP + BRCA2
ADP + phosphorylated BRCA2
show the reaction diagram
-
phosphorylates at Ser3291, phosphorylation reaches maximal levels in G2/M
-
-
?
ATP + c-Jun N-terminal kinase 3
ADP + phosphorylated c-Jun N-terminal kinase 3
show the reaction diagram
-
i.e. JNK3, phosphorylation inhibits JNK3 and leads to reduced phosphorylation of c-jun and to reduced apoptosis
-
-
?
ATP + Cdc20
ADP + phosphorylated Cdc20
show the reaction diagram
-
Cdk phosphorylation affects interaction of Cdc20 with Mad2 and the anaphase-promoting complex-cyclosome in HeLa cells
-
-
?
ATP + CDK1
ADP + phosphorylated CDK1
show the reaction diagram
-
CDK7 phosphorylates the activation segment or T-loop of CDK1
-
-
?
ATP + Cdk1
ADP + phosphorylated Cdk2
show the reaction diagram
-
Cdk7
-
-
?
ATP + cdk2
ADP + phosphorylated cdk2
show the reaction diagram
-
CDK7 phosphorylates the activation segment or T-loop of CDK2
-
-
?
ATP + CDK9
ADP + phosphorylated CDK9
show the reaction diagram
-
-
-
?
ATP + Cprk
ADP + phosphorylated Cprk
show the reaction diagram
-
i.e. Cdk5/p35-regulated kinase
-
-
?
ATP + Dab1 protein
ADP + Dab1 phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + dephosphin
ADP + phosphorylated dephosphin
show the reaction diagram
-
Cdk5 regulates endocytosis involving dephosphin activity, overview
-
-
?
ATP + early mitotic inhibitor 1 protein
ADP + early mitotic inhibitor 1 phosphoprotein
show the reaction diagram
-
i.e. Emi1, is phosphorylated by CDKs in mitotic but not S-phase cell extracts
-
-
?
ATP + ErbB2
ADP + phosphorylated ErbB2
show the reaction diagram
-
phosphorylation of the neuregulin receptor by Cdk5 is involved in regulation of neuregulin
-
-
?
ATP + ErbB3
ADP + phosphorylated ErbB3
show the reaction diagram
-
phosphorylation of the neuregulin receptor by Cdk5 is involved in regulation of neuregulin
-
-
?
ATP + eukaryotic elongation factor 2
ADP + phosphorylated eukaryotic elongation factor 2
show the reaction diagram
-
phosphorylation on Ser595 by Cdk2
-
-
?
ATP + histone H1
ADP + phosphorylated steroid histone H1
show the reaction diagram
-
-
-
-
?
ATP + MEK1
ADP + phosphorylated MEK1
show the reaction diagram
-
Cdk5 regulates the ERK1/2 pathway through phosphorylation of MEK1, overview
-
-
?
ATP + MEP50 protein
ADP + MEP50 phosphoprotein
show the reaction diagram
-
a PRMT5 co-regulatory factor
-
-
?
ATP + Munc-18
ADP + phosphorylated Munc-18
show the reaction diagram
-
involved in regulation of exocytosis involving SNARE proteins, Munc-18 is required for mediating secretory responsesoverview
-
-
?
ATP + NF-H
ADP + phosphorylated NF-H
show the reaction diagram
-
neurofilament protein that correlates neurit outgrowth, phosphorylation at the KSP repeats, regulated by the myelin-associate glycoprotein
-
-
?
ATP + NF-M
ADP + phosphorylated NF-M
show the reaction diagram
-
neurofilament protein, phosphorylation at the KSP repeats, regulated by the myelin-associate glycoprotein
-
-
?
ATP + NR1 receptor
ADP + phosphorylated NR1 receptor
show the reaction diagram
-
involved in synaptic transmission, overview
-
-
?
ATP + NR2 receptor
ADP + phosphorylated NR2 receptor
show the reaction diagram
-
involved in synaptic transmission, phosphorylation of Ser1232 on the A subunit upregulates NMCAR activity, overview
-
-
?
ATP + p35 protein
ADP + p35 phosphoprotein
show the reaction diagram
-
a nuclear transcription factor, Cdk5-p25 phosphorylates p53 on Ser15, Ser33, and Ser44
-
-
?
ATP + parkin
ADP + phosphorylated parkin
show the reaction diagram
-
Ser-131 located at the linker region of parkin is the major Cdk5 phosphorylation site, phosphorylation by Cdk5 decreases the auto-ubiquitylation of parkin, parkin S131A mutant has 40% lower phosphorylation levels in vivo than wild-type parkin
-
-
?
ATP + pocket protein p107
ADP + phosphorylated pocket protein 107
show the reaction diagram
-
hyperphosphorylation by CDK/cyclin contributes to the transactivation of genes with functional E2F-binding sites, including growth and cell-cycle regulators, i.e. c-myc, Rb protein, cdc2, cyclin E, and cyclin A, and genes encoding proteins required for nucleotide and DNA biosynthesis
-
-
?
ATP + pocket protein p130
ADP + phosphorylated pocket protein 130
show the reaction diagram
-
hyperphosphorylation by CDK/cyclin contributes to the transactivation of genes with functional E2F-binding sites, including growth and cell-cycle regulators, i.e. c-myc, Rb protein, cdc2, cyclin E, and cyclin A, and genes encoding proteins required for nucleotide and DNA biosynthesis
-
-
?
ATP + polymerase II C-terminal domain
ADP + phosphorylated polymerase II C-terminal domain
show the reaction diagram
-
-
-
?
ATP + progesterone receptor
ADP + phosphorylated progesterone receptor
show the reaction diagram
ATP + retinoblastoma protein
ADP + phosphorylated retinoblastoma protein
show the reaction diagram
ATP + retinoblastoma protein
ADP + retinoblastoma phosphoprotein
show the reaction diagram
-
a tumor suppressor protein
-
-
?
ATP + RNA polymerase II
ADP + phosphorylated RNA polymerase II
show the reaction diagram
-
CDK7 and CDK8 phosphorylate the C-terminal domain of RNA Pol II
-
-
?
ATP + RNA polymerase II C-terminal domain
ADP + phosphorylated RNA polymerase II C-terminal domain
show the reaction diagram
-
phosphorylation by Cdk7 and Cdk9, phosphorylation at serine residues 2 and 5
-
-
?
ATP + RNA polymerase II C-terminal domain protein
ADP + RNA polymerase II C-terminal domain phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + SCR-1
ADP + phosphorylated SCR-1
show the reaction diagram
-
Cdk2-cyclin A, phosphorylation at Lys5 regulates SCR-1 interaction with the progesterone receptor
-
-
?
ATP + STAT3
ADP + phosphorylated STAT3
show the reaction diagram
-
substrate of CDK5
-
-
?
ATP + STAT3 protein
ADP + STAT3 phosphoprotein
show the reaction diagram
-
Cdk5 phosphorylates at Ser727
-
-
?
ATP + STAU2
ADP + phosphorylated STAU2
show the reaction diagram
STAU2 is hyperphosphorylated during mitosis and that CDK1 participates in the process. Several phosphorylated amino acids residues are localized as clusters in the C-terminal region of STAU2
-
-
?
ATP + T-cell protein tyrosine phosphatase
ADP + phosphorylated T-cell protein tyrosine phosphatase
show the reaction diagram
-
phosphorylation of the two splicing varaints TC45 and TC48 at Ser304 in a cell cycle-dependent manner, optimally in mitosis, overview
-
-
?
ATP + tau protein
ADP + phosphorylated tau protein
show the reaction diagram
ATP + Tau protein
ADP + Tau phosphoprotein
show the reaction diagram
-
Cdk5-p25 has a stronger Tau-phosphorylating activity than Cdk5-p35 in neurons
-
-
?
ATP + VGCC
ADP + phosphorylated NR1 receptor
show the reaction diagram
-
a voltage-dependent calcium channel, phosphorylation within the intracellular loop of the channel inhibiting interaction with SNARE proteins, SNAP-25, and synaptotagmin I required for neurotransmitter release, overview
-
-
?
ATP + Wee1A
ADP + phosphorylated Wee1A
show the reaction diagram
-
phosphorylation at S123, S53, and S121 promotes binding of Wee1A by beta-TrCP, the beta-transducin repeat-containing protein, which is the substrate recognition component of the ubiquitin ligase, leading to proteasomal degradation of Wee1A, overview
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2]phosphate
show the reaction diagram
-
the enzyme phosphorylates Ser595. Ser595 phosphorylation varies during the cell cycle and is required for efficient Thr56 phosphorylation (by elongation factor 2 kinase) in vivo
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyclin
-
cyclin A
-
cyclin B
-
cyclin B1
-
required regulatory subunit of CDKs
-
cyclin C
-
cofactor of CDK3
-
cyclin D
-
cyclin D1
-
cyclin D2
-
cyclin D3
-
cyclin E
-
cyclin E2
-
cofactor of CDK3
-
cyclin H
-
cofactor of CDK7
-
cyclin K
-
-
cyclin L
-
cofactor of CDK11
-
cyclin T
-
cyclin V
-
regulatory subunit of CDK6
-
additional information
-
viral K-cyclin has a much longer half-life compared to cellular cyclins because it lacks the PEST degradation sequence, the viral K-cyclin can substitute the cellular cyclins in binding to the cellular CDKs, which is important for the virus development
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(-)-cis-5,7-dihydroxyphenyl-8-[4-(3-hydroxy-1-methyl)piperidinyl]-4H-1-benzopyran-4-one
-
(1S,2R,3R)-3-[[9-iso-propyl-6-[[4-(2-pyridyl)phenyl]methylamino]purin-2-yl]amino]cyclohexane-1,2-diol
-
-
(2R)-2-hydroxy-3-[[9-(propan-2-yl)-6-[[4-(pyridin-2-yl)benzyl]amino]-9H-purin-2-yl]amino]propyl L-valinate
-
-
(2R)-2-{[9-(propan-2-yl)-6-({[4-(pyridin-2-yl)phenyl]methyl}amino)-9H-purin-2-yl]amino}butan-1-ol
-
-
(2R)-3-[[9-iso-propyl-6-[[4-(2-pyridyl)phenyl]methylamino]purin-2-yl]amino]propane-1,2-diol
-
-
(2S)-4-[[9-iso-propyl-6-[[4-(2-pyridyl)phenyl]methylamino]purin-2-yl]amino]butane-1,2-diol
-
-
(3-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]phenyl)acetonitrile
-
-
(3-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]phenyl)methanol
-
-
(3-[[4-amino-6-(cyclohexylmethoxy)pyrimidin-2-yl]amino]phenyl)acetonitrile
-
41% inhibition at 0.01 mM
(3R,5S)-5-(hydroxymethyl)-1-[9-iso-propyl-6-[[4-(2-pyridyl)phenyl]methylamino]- purin-2-yl]pyrrolidin-3-ol
-
-
(3Z)-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
-
IC50 for CDK1 is above 0.016 mM
(3Z)-3-[2-(4-bromophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
IC50 for CDK1 is 0.012 mM
(3Z)-5-bromo-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
-
IC50 for CDK1 is 0.030 mM
(3Z)-5-bromo-3-[2-(4-fluorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
IC50 for CDK1 is 0.029 mM
(3Z)-5-bromo-3-[2-(4-methylphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
IC50 for CDK1 is 0.029 mM
(4,5-diphenyl-1H-pyrazolo[3,4-c]pyridazin-3-yl)hydrazine trihydrochloride
-
(4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]phenyl)acetonitrile
-
-
(4-[[4-amino-6-(cyclohexylmethoxy)pyrimidin-2-yl]amino]phenyl)acetonitrile
-
-
(5Z)-2-(benzylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-(butylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-(cyclopropylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-(methoxyamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-(methylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-(phenylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(2,6-dichlorobenzyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(2-bromobenzyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(2-chlorobenzyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(2-methoxybenzyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(2-phenylethyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(2-pyridin-2-ylethyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(3-hydroxy-2-phenylpropyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(3-phenylpropyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(pyridin-2-ylmethyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[methyl(thiophen-2-ylmethyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[(1R)-1-benzyl-2-hydroxyethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[(1R)-2-hydroxy-1-phenylethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[(1R)-2-methoxy-1-phenylethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[(1R,2S)-2-phenylcyclopropyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[(1S)-1-benzyl-2-hydroxyethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[(1S)-2-hydroxy-1-phenylethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(2-chlorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(2-ethoxyphenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(2-fluorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(2-methoxyphenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(3-chlorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(3-fluorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(4-bromophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(4-chlorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(4-fluorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-2-[[2-(4-methoxyphenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
(5Z)-5-(quinolin-6-ylmethylidene)-2-(thiophen-2-ylmethyl)-1,3-thiazol-4(5H)-one
-
(5Z)-5-(quinolin-6-ylmethylidene)-2-[(2-thiophen-2-ylethyl)amino]-1,3-thiazol-4(5H)-one
-
(5Z)-5-(quinolin-6-ylmethylidene)-2-[(thiophen-2-ylmethyl)amino]-1,3-thiazol-4(5H)-one
-
(R)-roscovitine
1,2-di(2-pyridyl)-1H-pyrazolo[3,4-c]pyridazine
-
1,2-dimethyl-1H-pyrazolo[3,4-c]pyridazine
-
1,25-dihydroxyvitamin D3
-
inhibition of CDK2 activity by 1,25-dihydroxyvitamin D3 is associated with decreased T160 phosphorylation, a residue whose phosphorylation in the nucleus is essential for CDK2 activity. 1,25-dihydroxyvitamin D3 increases the stability of the cyclin-dependent kinase inhibitor p27KIP1. Ectopic expression of cyclin E is sufficient to overcome 1,25-dihydroxyvitamin D3-mediated cytoplasmic mislocalization of CDK2 and all antiproliferative effects of 1,25-dihydroxyvitamin D3, yet endogenous levels of cyclin E or binding to CDK2 are not affected by 1,25-dihydroxyvitamin D3. Targeting CDK2 to the nucleus of 1,25-dihydroxyvitamin D3-sensitive cancer cells blocked G1 accumulation and growth inhibition by 1,25-dihydroxyvitamin D3
1-(1-acetylpiperidin-4-yl)-8-(cyclopentylamino)-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-(4,5-diphenyl-1H-pyrazolo[3,4-c]pyridazin-3-yl)-3-ethylurea
-
1-(4,5-diphenyl-1H-pyrazolo[3,4-c]pyridazin-3-yl)-3-phenylurea
-
1-(5-cyclobutyl-thiazol-2-yl)-3-isoquinolin-5-yl-urea
-
competitive inhibitor
1-acetyl-3-amino-4,5-diphenyl-1H-pyrazolo[3,4-c]pyridazine
-
1-amino-3H-dibenzo[f,h]pyrazolo[3,4-c]cinnoline
-
1-benzyl-8-(cyclopentylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]-quinazoline-3-carboxamide
-
-
1-methyl-8-([1-[(4-methylpiperazin-1-yl)carbonyl]piperidin-4-yl]amino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[(1-methylpiperidin-4-yl)amino]-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[(pyridin-2-ylmethyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[(pyridin-3-ylmethyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[(pyridin-4-ylmethyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[1-(methylsulfonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[1-(phenylcarbonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[1-(phenylsulfonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[2-(morpholin-4-yl)ethyl]amino]-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[2-(piperidin-1-yl)ethyl]amino]-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[3-(4-methylpiperazin-1-yl)benzyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[4-(4-methylpiperazin-1-yl)benzyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[4-(methylsulfonyl)benzyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-NMPP1
-
inhibits Cdk7, selective inhibition of Cdk7 in G1 prevents activation but not formation of Cdk2/cyclin complexes and delays S phase. Inhibiting Cdk7 in G2 blocks entry to mitosis and disrupts Cdk1/cyclin B complex assembly
1-[4-[(5-fluoro-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]-N,N-dimethyl-L-prolinamide
-
2,2'-[(6-([(4-methoxyphenyl)methyl]-amino)-9-(1-methylethyl)-9H-purin-2-yl)imino]bis(ethanol)
i.e. CVT-313, specific and potent inhibitor. Inhibits the growth of human lung carcinoma cell line A549 in a dose-dependent manner, with an IC50 of 0.0012 mM
-
2-(2-chlorophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
2-(3-bromophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
2-(3-chloro-4-piperazin-1-yl-phenylamino)-8-cyclopentyl-5-methyl-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
2-(3-chlorophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
2-(4-aminophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
2-(4-bromophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
2-(4-chlorophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
2-biphenyl-4-yl-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
2-[(3,4-dimethoxyphenyl)amino]-8-ethylpyrido[2,3-d]pyrimidin-7(8H)-one
-
2-[(3-amino-4,5-diphenyl-1H-pyrazolo[3,4-c]pyridazin-1-yl)methoxy]ethanol
-
2-[(4-[4-[(5-fluoro-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]piperazin-1-yl)sulfonyl]-2-oxoethanol
-
2-[(4-[4-[(6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]piperazin-1-yl)sulfonyl]-1-(methylsulfanyl)-2-oxoethanol
-
2-[(4-[4-[(6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]piperazin-1-yl)sulfonyl]-2-oxoethanol
-
2-[2-(3-amino-4,5-diphenyl-1H-pyrazolo[3,4-c]pyridazin-1-yl)ethoxy]ethanol
-
2-[4-(4-acetyl-piperazin-1-yl)-phenylamino]-8-cyclopentyl-5-methyl-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
2-[4-(diethylamino)phenyl]-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
2-[4-(dimethylamino)phenyl]-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
-
3-acetamide-1-acetyl-4,5-diphenyl-1H-pyrazolo[3,4-c]-pyridazine
-
3-acetamide-4,5-diphenyl-1H-pyrazolo[3,4-c]pyridazine
-
3-amino-1-benzyl-4,5-diphenyl-1H-pyrazolo[3,4-c]pyridazine
-
3-amino-4,5-bis(p-aminophenyl)-1H-pyrazolo[3,4-c]-pyridazine
-
3-amino-4,5-bis(p-methoxyphenyl)-1H-pyrazolo[3,4-c]-pyridazine
-
3-amino-4,5-bis(p-nitrophenyl)-1H-pyrazolo[3,4-c]pyridazine
-
3-amino-4,5-bis(p-tert-butylphenyl)-1H-pyrazolo[3,4-c]-pyridazine
-
3-amino-4,5-bis(p-trifluoromethylphenyl)-1H-pyrazolo-[3,4-c]pyridazine
-
3-amino-4,5-di(2-furyl)-1H-pyrazolo[3,4-c]pyridazine
-
3-amino-4-phenyl-1H-pyrazolo[3,4-c]pyridazine
-
3-amino-5-(2-furyl)-1H-pyrazolo[3,4-c]pyridazine
-
3-amino-5-methyl-4-phenyl-1H-pyrazolo[3,4-c]pyridazine
-
3-amino-5-phenyl-1H-pyrazolo[3,4-c]pyridazine
-
3-isopropyl-5(R)-(2-hydroxypropyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5(R)-[1-(hydroxymethyl)propyl]amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5,7-di[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(2,3-dihydroxypropyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(2-aminoethyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(2-hydroxy-2-methylpropyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(2-hydroxyethyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(3-amino-2-hydroxypropyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(4-methoxybenzyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(N-morpholinyl)-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(piperazin-1-yl)-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(thiomorpholinyl)-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(trans-2-aminocyclohexyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-(trans-4-aminocyclohexyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-methylsulfanyl-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-methylsulfonyl-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-[2-(2-hydroxyethyl)piperidin-1-yl]-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-[2-(dimethylamino)ethyl]amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-5-[4-(2-hydroxyethyl)piperazin-1-yl]-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-isopropyl-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
-
-
3-[[(2,2-dioxido-1,3-dihydro-2-benzothien-5-yl)amino]methylene]-5-(1,3-oxazol-5-yl)-1,3-dihydro-2H-indol-2-one
-
-
3-[[4-([[amino(imino)methyl]amino]sulfonyl)anilino]methylene]-2-oxo-2,3-dihydro-1H-indole
-
-
4-(1,3-benzothiazol-2-yl)-N-(1,3-thiazol-2-yl)thiophene-2-sulfonamide
-
4-(1,3-benzothiazol-2-yl)-N-(2-fluoroethyl)thiophene-2-sulfonamide
poor inhibition of cdk5/p25
4-(1,3-benzothiazol-2-yl)-N-(4,5-dimethyl-1,3-thiazol-2-yl)thiophene-2-sulfonamide
-
4-(1,3-benzothiazol-2-yl)-N-(4-methylpyridin-2-yl)thiophene-2-sulfonamide
-
4-(1,3-benzothiazol-2-yl)-N-(5-hydroxypyridin-2-yl)thiophene-2-sulfonamide
-
4-(1,3-benzothiazol-2-yl)-N-(pyridin-2-ylmethyl)thiophene-2-sulfonamide
-
4-(1,3-benzothiazol-2-yl)-N-hydroxythiophene-2-sulfonamide
-
4-(1,3-benzothiazol-2-yl)-N-[5-(morpholin-4-yl)pyridin-2-yl]thiophene-2-sulfonamide
-
4-(1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
binds to Ile10 and Asp86 in the active site of cdk2
4-(1,4-dioxo-1,4-dihydro-naphthalen-2-ylamino)-N-(2-hydroxy-ethyl)-benzenesulfonamide
-
-
4-(1-ethyl-2-methyl-1H-imidazol-5-yl)-N-[4-(methylsulfonyl)phenyl]pyrimidin-2-amine
-
4-(6-acetyl-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
poor inhibition of cdk2/cyclin E
4-(6-amino-4-cyclohexylmethoxy-5-nitrosopyrimidin-2-ylamino)-benzenesulfonamide
-
-
4-(6-amino-4-cyclohexylmethoxy-5-nitrosopyrimidin-2-ylamino)-N-(2,3-dihydroxypropyl)-benzenesulfonamide
-
-
4-(6-amino-4-cyclohexylmethoxy-5-nitrosopyrimidin-2-ylamino)-N-(2-hydroxyethyl)benzenesulfonamide
-
-
4-(6-chloro-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
-
4-(6-fluoro-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
-
4-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
-
4-(6-nitro-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
-
4-chloro-N-(cis-3-[4-[(naphthalen-1-ylacetyl)amino]-1H-imidazol-1-yl]cyclobutyl)benzamide
-
4-[(4-imidazo[1,2-a]pyridin-3-ylpyrimidin-2-yl)amino]-N-(2-methoxyethyl)benzenesulfonamide
-
4-[(4-imidazo[1,2-a]pyridin-3-ylpyrimidin-2-yl)amino]benzenesulfonamide
-
4-[(4-imidazo[1,2-b]pyridazin-3-ylpyrimidin-2-yl)amino]-N-methylbenzenesulfonamide
-
4-[2-(5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)hydrazino]benzenesulfonamide
-
-
4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]-N-(4-[[3-(1,3-oxazetidin-3-yl)propyl]sulfonyl]phenyl)pyrimidin-2-amine
-
4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]-N-[4-(methylsulfonyl)phenyl]pyrimidin-2-amine
-
4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]-N-[4-(propylsulfonyl)phenyl]pyrimidin-2-amine
-
4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]-N-[4-[(tetrahydrofuran-2-ylmethyl)sulfonyl]phenyl]pyrimidin-2-amine
-
4-[4-(8-cyclopentyl-5-methyl-7-oxo-7,8-dihydro-pyrido-[2,3-d]pyrimidin-2-ylamino)-phenyl]-piperazine-1-carbaldehyde
-
-
4-[4-(8-cyclopentyl-5-methyl-7-oxo-7,8-dihydro-pyrido-[2,3-d]pyrimidin-2-ylamino)-phenyl]-piperazine-1-carboxylic acid tert-butyl ester
-
-
4-[4-(8-cyclopentyl-7-oxo-5-trifluoromethyl-7,8-dihydropyrido[2,3-d]pyrimidin-2-ylamino)-phenyl]-piperazine-1-carboxylic acid tert-butyl ester
-
-
4-[7-(4-chloro-3-fluorophenyl)-1,3-benzothiazol-2-yl]thiophene-2-sulfonamide
-
4-[7-(4-fluorophenyl)-1,3-benzothiazol-2-yl]thiophene-2-sulfonamide
poor inhibition of cdk2/cyclin E
4-[[(2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]amino]-N-(1,3-thiazol-2-yl)benzenesulfonamide
-
-
4-[[(7-oxo-6,7-dihydro-8H-[1,3]thiazolo[5,4-e]indol-8-ylidene)methyl]amino]-N-(2-pyridinyl)benzenesulfonamide
-
-
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)-N-methylbenzenesulfonamide
-
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)benzenesulfonamide
-
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-methylbenzenesulfonamide
-
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-[3-(1-methylethoxy)propyl]benzenesulfonamide
-
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]benzenesulfonamide
-
4-[[4-(1-cyclopentyl-2-methyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)benzenesulfonamide
-
4-[[4-(1-cyclopropyl-2-methyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)benzenesulfonamide
-
4-[[4-(1-ethyl-2-methyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)benzenesulfonamide
-
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N,N-diethylbenzamide
-
-
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N,N-diethylbenzenesulfonamide
-
-
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N,N-dimethylbenzamide
-
-
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N-(2-hydroxypropyl)benzenesulfonamide
-
-
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N-(tetrahydrofuran-2-ylmethyl)benzenesulfonamide
-
-
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N-1,3-thiazol-2-ylbenzenesulfonamide
-
-
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]phenol
-
-
4-[[4-amino-6-(cyclohexylmethoxy)pyrimidin-2-yl]amino]-N,N-diethylbenzamide
-
29% inhibition at 0.001 mM
4-[[4-amino-6-(cyclohexylmethoxy)pyrimidin-2-yl]amino]-N,N-diethylbenzenesulfonamide
-
33% inhibition at 0.01 mM
4-[[4-amino-6-(cyclohexylmethoxy)pyrimidin-2-yl]amino]-N,N-dimethylbenzamide
-
49% inhibition at 0.1 mM
4-[[4-amino-6-(cyclohexylmethoxy)pyrimidin-2-yl]amino]benzamide
-
-
5,6-dichloro-1-beta-D-ribofuranosyl benzimidazole
-
cdk9 inhibitor
5,6-dichloro-1-beta-D-ribofuranosyl-benzimidazole
-
-
5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole
-
specific CDK7 and 9 inhibition drives resolution of neutrophil-dominant inflammation
5-fluoro-6,8-dimethyl-N-(4-morpholin-4-ylphenyl)-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
-
6,7-dimethoxy-N-(3hydroxyphenyl)quinazolin-4-amine
-
-
6,8-dimethyl-N-(4-morpholin-4-ylphenyl)-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
-
6,8-dimethyl-N-[4-[4-(methylsulfonyl)piperazin-1-yl]phenyl]-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
-
6-(cyclohexylmethoxy)-N2-(3-methoxyphenyl)-5-nitrosopyrimidine-2,4-diamine
-
-
6-(cyclohexylmethoxy)-N2-(4-methoxyphenyl)-5-nitrosopyrimidine-2,4-diamine
-
-
6-(cyclohexylmethoxy)-N2-[3-(methylsulfanyl)phenyl]-5-nitrosopyrimidine-2,4-diamine
-
-
6-(cyclohexylmethoxy)-N2-[3-(methylsulfanyl)phenyl]pyrimidine-2,4-diamine
-
-
6-(cyclohexylmethoxy)-N2-[4-(methylsulfanyl)phenyl]-5-nitrosopyrimidine-2,4-diamine
-
-
6-acetyl-8-cyclopentyl-5-methyl-2-(4-piperazin-1-ylphenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
6-bromo-8-cyclopentyl-5-methyl-2-(4-piperazin-1-ylphenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
6-chloro-8-cyclopentyl-5-methyl-2-(4-piperazin-1-ylphenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
6-dimethylamino purine
-
potent inhibitor of CDK1/cyclin B
8-(1-ethyl-propyl)-5-methyl-2-(4-piperazin-1-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-(benzylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclohexylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]-quinazoline-3-carboxamide
-
-
8-(cyclohexylamino)-N-1-dimethyl-4,5-dihydro-1H-pyrazolo-[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-1-(2,2,2-trifluoroethyl)-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-1-(2-hydroxyethyl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-1-(4-methoxyphenyl)-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-1-(4-sulfamoylphenyl)-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-1-(pyridin-2-yl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-1-phenyl-4,5-dihydro-1H-pyrazolo[4,3-h]-quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-N-1-dimethyl-4,5-dihydro-1H-pyrazolo-[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-N-hydroxy-N,1-dimethyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-N-methyl-1-(1-methylpiperidin-4-yl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-N-[1-(dimethylamino)propan-2-yl]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-(cyclopentylamino)-N-[2-(dimethylamino)ethyl]-N-1-dimethyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-amino-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-cyclopentyl-2-(4-morpholin-4-yl-phenylamino)-8Hpyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-2-(4-piperazin-1-yl-phenylamino)-5-trifluoromethyl-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-2-(4-piperazin-1-yl-phenylamino)-8Hpyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-2-(4-piperidin-1-yl-phenylamino)-8Hpyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-2-(4-[1,4]diazepan-1-yl-phenylamino)-5-methyl-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-2-[4-(3,3-dimethyl-piperazin-1-yl)-phenylamino]-5-methyl-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-2-[4-(3,5-dimethyl-piperazin-1-yl)-phenylamino]-5-methyl-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-2-[4-(3-hydroxy-pyrrolidin-1-yl)-phenylamino]-5-methyl-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-2-{4-[4-(3-hydroxy-propyl)-piperidin-1-yl]-phenylamino}-5-methyl-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-5,6-dimethyl-2-(4-piperazin-1-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-5-ethyl-2-(4-piperazin-1-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-5-methyl-2-(4-morpholin-4-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-5-methyl-2-(4-piperazin-1-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-5-methyl-2-(4-piperidin-1-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-5-methyl-2-[4-(4-methyl-piperazin-1-yl)-phenylamino]-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-5-methyl-7-oxo-2-(4-piperazin-1-yl-phenylamino)-7,8-dihydro-pyrido[2,3-d]pyrimidine-6-carboxylic acid
-
-
8-cyclopentyl-5-methyl-7-oxo-2-(4-piperazin-1-yl-phenylamino)-7,8-dihydro-pyrido[2,3-d]pyrimidine-6-carboxylic acid ethyl ester
-
-
8-cyclopentyl-5-methyl-7-oxo-2-(4-piperazin-1-yl-phenylamino)-7,8-dihydro-pyrido[2,3-d]pyrimidine-6-carboxylic acid methyl ester
-
-
8-cyclopentyl-6-ethyl-5-methyl-2-(4-piperazin-1-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-6-fluoro-5-methyl-2-(4-piperazin-1-ylphenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-cyclopentyl-6-iodo-5-methyl-2-(4-piperazin-1-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-ethyl-2-[4-(4-methylpiperazin-1-yl)phenylamino]-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-isopropyl-5-methyl-2-(4-piperazin-1-yl-phenylamino)-8H-pyrido[2,3-d]pyrimidin-7-one
-
-
8-[(1-acetylpiperidin-4-yl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(1-acetylpiperidin-4-yl)amino]-N,1-dimethyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(1-acetylpiperidin-4-yl)amino]-N,1-dimethyl-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(1-ethylpiperidin-4-yl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(2-hydroxyethyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo-[4,3-h]quinazoline-3-carboxamide
-
-
8-[(3-methoxybenzyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(4-bromobenzyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo-[4,3-h]quinazoline-3-carboxamide
-
-
8-[(4-methoxybenzyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[[4-(acetylamino)benzyl]amino]-1-methyl-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
actinomycin D
-
is less effective than 1-NMPP1 at inhibiting Cdk2 T loop phosphorylation
aloisine-A
-
alsterpaullone
aminopurvalanol
-
-
AMP
-
competitive inhibitor
anilinopyrimidine 32
-
apigenin
-
a flavonoid inhibitor of CDK6, CDK5, and CDK1
arylazopyrazole 31b
-
BMS-387032
-
-
BS-181
butyrolactone-1
-
-
CDK inhibitory proteins
-
members of the family of CDK inhibitory proteins, e.g. INK4 proteins, overview, CKIs may play a role as regulators in neointimal hyperplasia
-
Cdk2 inhibitor II
-
-
Cdk2DN
-
inhibition of Cdk2, induces phosphorylation of ataxia-telangiectasia mutated substrates
-
Cdk4/'6 Inhibitor IV
-
-
chrysin
-
a flavonoid inhibitor of CDK6, CDK5, and CDK1
CIP (154-279)
-
-
-
Cks1
-
Cks 1 protein inactivates Cdk2, activation of Chk1 leads to inactivation of Cdk2 by promoting phosphorylation-dependent turnover of the Cdk activating phosphatase Cdc25A
-
cyclin D1
-
inhibits the association and activation of androgen receptor by CDK6
-
cyclin-dependent kinase inhibitor p27KIP1
-
-
-
deoxyvariolin B
-
dinaciclib
-
-
DN-CDK2
suppresses CDK2 activity and partially increases erlotinib sensitivity
-
E2F1 peptide
-
81PALGRPPVKRRLDLE95
-
erlotinib
erlotinib treatment of breast cancer cells suppresses CDK2 activity; suppresses CDK2 activity, which is critical for cellular sensitivity to erlotinib, regardless of EGFR expression level. CDK1, CDK4 and CDK6 is not associated with erlotinib sensitivity
ethyl 4-[[1-methyl-3-(methylcarbamoyl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazolin-8-yl]amino]piperidine-1-carboxylate
-
-
ethyl [2-([[4-(1,3-benzothiazol-2-yl)thiophen-2-yl]sulfonyl]amino)-1,3-thiazol-4-yl]acetate
-
FAALS
five amino-acid peptide inhibitor that is directed toward a noncatalytic binding pocket and which disrupts the cdk2/cyklin E complex
fascaplysin
-
CDK4- and CDK6-specific inhibitor
fisetin
-
a flavonol inhibitor of CDK6, CDK5, and CDK1, binding structure with CDK6 involving V101, E61, K43, D163, and E99 of CDK6, overview
flavopiridol
ginsenoside F1
-
noncompetitive inhibition
ginsenoside Rb1
-
noncompetitive inhibition
ginsenoside Re
-
noncompetitive inhibition
ginsenoside Rf
-
noncompetitive inhibition
ginsenoside Rg1
-
noncompetitive inhibition
ginsenoside Rg2
-
noncompetitive inhibition
ginsenoside Rh1
-
noncompetitive inhibition
H1PAla
-
noncompetitive inhibitor
H1PPO4
-
noncompetitive inhibitor
hymenialdisine
-
-
IkappaBalpha
-
human protein, competes with INK4 proteins for binding sites on CDK4, CDK4 is bound at the N-terminal ankyrin repeats, while the C-terminal ankyrin repeats bind NF-kappaB, structure analysis
-
indirubin 3'-monoxime
-
indirubin-3'-monoxime
indirubin-3'-oxime
-
indirubin-5-sulfonic acid
-
-
INK4 proteins
-
inhibit CDK4
-
insulin-like growth factor binding protein-3
-
decreases the phosphorylation activity of CDK2 and CDK4
-
isopentenyladenine
kaempferol
-
a less potent flavonoid inhibitor of CDK6, CDK5, and CDK1
kenpaullone
-
78% inhibition of CDK2 at 0.01 mM
KSLNRPFPDKIPELK
-
-
LAALS
five amino-acid peptide inhibitor that is directed toward a noncatalytic binding pocket and which disrupts the cdk2/cyklin E complex
LDC000067
LiCl
-
slight inhibition of T231 phosphorylation by p25-Cdk5 kinase complex
luteolin
-
a flavonoid inhibitor of CDK5 and CDK1
meridianin A
-
meridianin G
-
meriolin
-
-
meriolin 1
-
meriolin 2
-
meriolin 3
-
Myt1
-
Cdk1 inhibitor
-
N-(1-[4-[(5-fluoro-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]azetidin-3-yl)acetamide
-
N-(2-methoxyethyl)-4-([4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-yl]amino)benzenesulfonamide
-
N-(2-methoxyethyl)-4-([4-[2-methyl-1-(2-methylpropyl)-1H-imidazol-5-yl]pyrimidin-2-yl]amino)benzenesulfonamide
-
N-(2-methoxyethyl)-4-[[4-(1,2,4-trimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]benzenesulfonamide
-
N-(3-{[5-chloro-4-(1H-indol-3-yl)pyrimidin-2-yl]amino}phenyl)-4-{[(2E)-4-(dimethylamino)but-2-enoyl]amino}benzamide
-
-
N-(4-[4-[(2-methoxyethyl)sulfonyl]piperazin-1-yl]phenyl)-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
-
N-(4-[[3-(dimethylamino)propyl]sulfonyl]phenyl)-4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-amine
-
N-(4-[[3-(dimethylamino)propyl]sulfonyl]phenyl)-4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-amine
-
N-(5-nitro-1H-indazol-3-yl)-2-phenylacetamide
-
N-(6-amino-pyrimidin-4-yl)-sulfanilic acid amide
-
-
N-1-dimethyl-8-([1-[(4-methylpiperazin-1-yl)carbonyl]piperidin-4-yl]amino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-1-dimethyl-8-[(1-methylpiperidin-4-yl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-1-dimethyl-8-[[1-(methylsulfonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-1-dimethyl-8-[[1-(phenylcarbonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-benzyl-8-(cyclopentylamino)-N-hydroxy-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-cyclohexyl-8-(cyclopentylamino)-N-hydroxy-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-methyl-4-[[(2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]amino]benzenesulfonamide
-
-
N-methyl-[4-[2-(7-oxo-6,7-dihydro-8H-[1,3]thiazolo[5,4-e]indol-8-ylidene)hydrazino]phenyl]methanesulfonamide
-
-
N-[(3R)-1-[4-[(5-fluoro-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]pyrrolidin-3-yl]acetamide
-
N-[(9bR)-5-oxo-2,3,5,9b-tetrahydro-1H-pyrrolo[2,1-alpha]isoindol-9-yl]-N'-pyridin-2-yl urea
-
-
N-[(9bR)-5-oxo-2,3,5,9b-tetrahydro-1H-pyrrolo[2,1-alpha]isoindol-9-yl]-N'-{5-[(2S)-pyrrolidin-2-yl]-1H-pyrazol-3-yl urea
-
-
N-[2-(1-aminohydrazino)ethyl]-4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]benzenesulfonamide
-
N-[2-(dimethylamino)ethyl]-4-[(4-imidazo[1,2-b]pyridazin-3-ylpyrimidin-2-yl)amino]benzenesulfonamide
-
N-[4-(4-[[(diethylamino)acetyl]sulfonyl]piperazin-1-yl)phenyl]-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
-
N-[4-(4-[[(dimethylamino)acetyl]sulfonyl]piperazin-1-yl)phenyl]-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
-
N-[4-(4-[[2-(dimethylamino)ethyl]sulfonyl]piperazin-1-yl)phenyl]-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
-
N-[4-(benzylsulfonyl)phenyl]-4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-amine
-
N-[4-[(2-methoxyethyl)sulfonyl]phenyl]-4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-amine
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(3-fluorophenyl)acetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(3-methylphenyl)acetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-fluorophenyl)acetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-hydroxyphenyl)acetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-methylphenyl)acetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-piperidin-1-ylphenyl)acetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-pyridin-4-ylphenyl)acetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-naphthalen-1-ylacetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-naphthalen-2-ylacetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-phenylacetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-[4-(methylsulfanyl)phenyl]acetamide
-
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-[4-(methylsulfonyl)phenyl]acetamide
-
N-[5-(2,5-dioxoimidazolidin-1-yl)-1H-indazol-3-yl]-2-phenylacetamide
-
N-[5-(2-oxopiperidin-1-yl)-1H-indazol-3-yl]-2-phenylacetamide
-
N-[5-(2-oxopyrrolidin-1-yl)-1H-indazol-3-yl]-2-phenylacetamide
-
N-[5-(dibutylamino)-1H-indazol-3-yl]-2-phenylacetamide
-
N-[5-(diethylamino)-1H-indazol-3-yl]-2-phenylacetamide
-
N-[5-(dipropylamino)-1H-indazol-3-yl]-2-phenylacetamide
-
N-[5-(ethylamino)-1H-indazol-3-yl]-2-phenylacetamide
-
N2-(3-bromophenyl)-6-(cyclohexylmethoxy)-5-nitrosopyrimidine-2,4-diamine
-
-
N2-(3-bromophenyl)-6-(cyclohexylmethoxy)pyrimidine-2,4-diamine
-
-
N4-(6-aminopyrimidin-4-yl)-sulfanilamide
-
competitive inhibitor
NU-2058
-
-
NU-6027
-
-
NU2058
-
-
NU6027
-
-
NU6102
-
highly potent and selective ATP-competitive inhibitor of CDK2
Olomoucine
olomoucine II
-
-
p15Ink4b
-
INK4 protein
-
p16Ink4a
-
p18
-
wild-type and D76A mutant human INK4 protein, the mutant is only slightly inhibitory, p18 competes with IkappaBalpha for binding sites on CDK4, structure analysis
-
p18Ink4c
-
INK4 protein
-
p19Ink4d
-
INK4 protein
-
p21
-
p21 protein
-
i.e. Cip1 or Waf1, a Cdk-inhibitor
-
p21CIP
-
as recombinant GST-tagged protein
-
p21Cip1
-
inhibits phosphorylation of tumor suppressor Rb
-
p21Clp1
-
forms a ternary complex with and is negatively regulated by p21Cip1, but not by its truncated fragment p21Cip1-D3
-
p21v1
-
endogenous CDK inhibitor
-
p21v2
-
endogenous CDK inhibitor
-
p21WAF1/CIP1
-
specific Cdk inhibitor, efficiently prevents etoposide-induced apoptotic cell death
-
p27
-
p27Kip1
-
p27Kip1 cyclin-dependent-kinase inhibitor
-
-
palbociclib
-
-
PD-0332991
-
-
PD183812
-
-
PHA-848125
-
-
PKF049-365
-
-
pRb peptide
-
866SNPPKPLKKLRFDIE880
-
progesterone
-
-
protopanaxatriol
-
noncompetitive inhibition
purvalanol
purvalanol A
-
-
purvalanol B
-
specific inhibitor of CDK1, 2, 5, and 7
pyrazolopyridazine
-
quercetin
-
a less potent flavonoid inhibitor of CDK6, CDK5, and CDK1
RBG-286147
-
RO-3306
-
-
roscovitine
RXL motif-containing peptide
-
addition of this peptide significantly reduces substrate phosphorylation by cyclin E-CDK2 and cyclin D2-CDK6
-
SCH-727965
-
-
shRNA
-
cdk5 shRNA is able to efficiently inhibit the expression of endogenous cdk5
-
simvastatin
-
inhibition of CDK2
siRNA
-
SNS-032
staurosporine
SU-9516
-
-
SU9516
TAACS
five amino-acid peptide inhibitor that is directed toward a noncatalytic binding pocket and which disrupts the cdk2/cyklin E complex
TAALD
five amino-acid peptide inhibitor that is directed toward a noncatalytic binding pocket and which disrupts the cdk2/cyklin E complex
TAALE
five amino-acid peptide inhibitor that is directed toward a noncatalytic binding pocket and which disrupts the cdk2/cyklin E complex
TAALS
disrupts the cdk2/cyclin E complex
tranilast
-
inhibition of CDK2 and CDK4
tumour suppressor p16INK4a
-
-
UCN-01
-
-
variolin B
-
Wee1
-
Cdk1 inhibitor
-
[(2R)-1-[[4-(1,3-benzothiazol-2-yl)thiophen-2-yl]sulfonyl]pyrrolidin-2-yl]methanol
poor inhibition of cdk2/cyclin E
[8-(cyclopentylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazolin-3-yl](4-methylpiperazin-1-yl)methanone
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cdc25A
-
-
-
CDK-activating kinase
-
the CDK-activating kinase (having three subunits, CDK7, cyclin H, and MAT1) plays a critical role in regulating cell cycle by mediating the activating phosphorylation of CDK1, CDK2, CDK4, and CDK6
-
Cks2
-
Cks 2 proteins activates Cdk2
-
cyclin
-
dependent on, forms complexes with cyclin A
-
cyclin A
-
cyclin B
-
cyclin D1
-
cyclin D2
-
-
-
cyclin D3
-
cyclin E
-
cyclin H
-
activates Cdk7
-
cyclin I
-
-
-
cyclin T
-
CDK9 activating partner cyclin T1
-
cyclin T1
-
activates Cdk9
-
dynein light chain 1
-
interacts with cdk2 and enhances Cdk2 kinase activity in vivo, dynein light chain 1 accelerates the G1-S transition by enhancing the activity of Cdk2
-
E2F1
-
-
-
etoposide
-
activity of Cdk2 selectively increases after 6-9 h and then continues to increase over the 24 h time course of etopside treatment
p25
-
p34SEI-1
-
i.e. TRIP-Br1, the protein binds directly to CDK4 and activates it at lower concentrations, but inhibits the enzyme at higher concentrations, p34SEI-1 has regulatory function, the binding is not affected by INK4 proteins p16 and p18, complex formation of CDK4, cyclin D2, p16, and p34SEI-1, p34SEI-1 has a LexA-mediated transactivation activity, determination of functional sequence units/fragments in the protein, overview
-
p35
-
p39
-
p58
-
regulatory subunit of CDK11
-
progestin
-
-
Protein phosphatase 2A
-
PP2A, enhances CDK8 kinase activity in vitro for the RNA polymerase II carboxy-terminal domain but not for histone H3. PP2A enhancement of CDK8 is independent of RV-cyclin expression and likely plays a role in the normal regulation of CDK8
-
RV-cyclin
-
retroviral cyclin from Walleye dermal sarcoma virus, enhances CDK8 kinase activity in vitro for RNA polymerase II carboxy-terminal domain and histone H3. It is specific for cdk8, no activation of Cdk7 or Cdk9. The majority of the RV-cyclin structure is comprised of a cyclin box fold, which is responsible for binding to cyclin-dependent kinase-8. Two-hybrid interaction analysis in Saccharomyces cerevisiae strain Y190
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00522 - 0.017
ATP
0.00285
PKTPKKAKKL
-
pH 7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
ATP
-
in 20 mM MOPS (pH 7.5), at 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015
(5Z)-2-(benzylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00031
(5Z)-2-(butylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00027
(5Z)-2-(cyclopropylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.002
(5Z)-2-(methoxyamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
Ki above 0.002 mM
0.00027
(5Z)-2-(methylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.002
(5Z)-2-(phenylamino)-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
Ki above 0.002 mM
0.00104
(5Z)-2-[(2,6-dichlorobenzyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.000038
(5Z)-2-[(2-bromobenzyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.000052
(5Z)-2-[(2-chlorobenzyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.000086
(5Z)-2-[(2-methoxybenzyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00006
(5Z)-2-[(2-phenylethyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00028
(5Z)-2-[(2-pyridin-2-ylethyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00039
(5Z)-2-[(3-hydroxy-2-phenylpropyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00024
(5Z)-2-[(3-phenylpropyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00031
(5Z)-2-[(pyridin-2-ylmethyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.002
(5Z)-2-[methyl(thiophen-2-ylmethyl)amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
Ki above 0.002 mM
0.00023
(5Z)-2-[[(1R)-1-benzyl-2-hydroxyethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00035
(5Z)-2-[[(1R)-2-hydroxy-1-phenylethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.002
(5Z)-2-[[(1R)-2-methoxy-1-phenylethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
Ki above 0.002 mM
0.000023
(5Z)-2-[[(1R,2S)-2-phenylcyclopropyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.002
(5Z)-2-[[(1S)-1-benzyl-2-hydroxyethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00058
(5Z)-2-[[(1S)-2-hydroxy-1-phenylethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.000046
(5Z)-2-[[2-(2-chlorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.000087
(5Z)-2-[[2-(2-ethoxyphenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00012
(5Z)-2-[[2-(2-fluorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.000063
(5Z)-2-[[2-(2-methoxyphenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00013
(5Z)-2-[[2-(3-chlorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00006
(5Z)-2-[[2-(3-fluorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00064
(5Z)-2-[[2-(4-bromophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00041
(5Z)-2-[[2-(4-chlorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.000062
(5Z)-2-[[2-(4-fluorophenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.00039
(5Z)-2-[[2-(4-methoxyphenyl)ethyl]amino]-5-(quinolin-6-ylmethylidene)-1,3-thiazol-4(5H)-one
-
0.000089
(5Z)-5-(quinolin-6-ylmethylidene)-2-(thiophen-2-ylmethyl)-1,3-thiazol-4(5H)-one
-
0.000045
(5Z)-5-(quinolin-6-ylmethylidene)-2-[(2-thiophen-2-ylethyl)amino]-1,3-thiazol-4(5H)-one
-
0.000035
(5Z)-5-(quinolin-6-ylmethylidene)-2-[(thiophen-2-ylmethyl)amino]-1,3-thiazol-4(5H)-one
-
0.012
NU2058
-
-
0.0013
NU6027
-
-
0.000006
NU6102
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00027 - 0.00061
(1S,2R,3R)-3-[[9-iso-propyl-6-[[4-(2-pyridyl)phenyl]methylamino]purin-2-yl]amino]cyclohexane-1,2-diol
0.00018 - 0.00087
(2R)-2-hydroxy-3-[[9-(propan-2-yl)-6-[[4-(pyridin-2-yl)benzyl]amino]-9H-purin-2-yl]amino]propyl L-valinate
0.000062 - 0.000225
(2R)-2-{[9-(propan-2-yl)-6-({[4-(pyridin-2-yl)phenyl]methyl}amino)-9H-purin-2-yl]amino}butan-1-ol
0.00015 - 0.00048
(2R)-3-[[9-iso-propyl-6-[[4-(2-pyridyl)phenyl]methylamino]purin-2-yl]amino]propane-1,2-diol
0.00082 - 0.00101
(2S)-4-[[9-iso-propyl-6-[[4-(2-pyridyl)phenyl]methylamino]purin-2-yl]amino]butane-1,2-diol
0.033
(3-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]phenyl)acetonitrile
Homo sapiens
-
with isozyme CDK2
0.000045
(3-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]phenyl)methanol
Homo sapiens
-
with isozyme CDK2
0.00045 - 0.00065
(3R,5S)-5-(hydroxymethyl)-1-[9-iso-propyl-6-[[4-(2-pyridyl)phenyl]methylamino]- purin-2-yl]pyrrolidin-3-ol
0.016
(3Z)-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
IC50 for CDK1 is above 0.016 mM
0.012
(3Z)-3-[2-(4-bromophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
IC50 for CDK1 is 0.012 mM
0.03
(3Z)-5-bromo-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
IC50 for CDK1 is 0.030 mM
0.029
(3Z)-5-bromo-3-[2-(4-fluorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
IC50 for CDK1 is 0.029 mM
0.029
(3Z)-5-bromo-3-[2-(4-methylphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
IC50 for CDK1 is 0.029 mM
0.000064
(4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]phenyl)acetonitrile
Homo sapiens
-
with isozyme CDK2
0.024
(4-[[4-amino-6-(cyclohexylmethoxy)pyrimidin-2-yl]amino]phenyl)acetonitrile
Homo sapiens
-
with isozyme CDK2
0.00013 - 0.0142
(R)-roscovitine
0.000007
1-(1-acetylpiperidin-4-yl)-8-(cyclopentylamino)-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000023
1-benzyl-8-(cyclopentylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]-quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000012
1-methyl-8-([1-[(4-methylpiperazin-1-yl)carbonyl]piperidin-4-yl]amino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000351
1-methyl-8-[(1-methylpiperidin-4-yl)amino]-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000087
1-methyl-8-[(pyridin-2-ylmethyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000021
1-methyl-8-[(pyridin-3-ylmethyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000021
1-methyl-8-[(pyridin-4-ylmethyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000001
1-methyl-8-[[1-(methylsulfonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000001 - 0.000003
1-methyl-8-[[1-(phenylcarbonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000004
1-methyl-8-[[1-(phenylsulfonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000209
1-methyl-8-[[2-(morpholin-4-yl)ethyl]amino]-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.00249
1-methyl-8-[[2-(piperidin-1-yl)ethyl]amino]-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000104
1-methyl-8-[[3-(4-methylpiperazin-1-yl)benzyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000017
1-methyl-8-[[4-(4-methylpiperazin-1-yl)benzyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000038
1-methyl-8-[[4-(methylsulfonyl)benzyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000046
1-[4-[(5-fluoro-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]-N,N-dimethyl-L-prolinamide
Homo sapiens
with isozyme CDK2
0.00008 - 0.00089
2-(2-chlorophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.000007 - 0.0018
2-(3-bromophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.000034 - 0.00105
2-(3-chlorophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.000016 - 0.0022
2-(4-aminophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.000007 - 0.002
2-(4-bromophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.000012 - 0.002
2-(4-chlorophenyl)-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.000014 - 0.0022
2-biphenyl-4-yl-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.00003 - 0.00054
2-[(3,4-dimethoxyphenyl)amino]-8-ethylpyrido[2,3-d]pyrimidin-7(8H)-one
0.000006
2-[(4-[4-[(5-fluoro-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]piperazin-1-yl)sulfonyl]-2-oxoethanol
Homo sapiens
with isozyme CDK2
0.000017
2-[(4-[4-[(6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]piperazin-1-yl)sulfonyl]-1-(methylsulfanyl)-2-oxoethanol
Homo sapiens
with isozyme CDK2
0.000017
2-[(4-[4-[(6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]piperazin-1-yl)sulfonyl]-2-oxoethanol
Homo sapiens
with isozyme CDK2
0.00004 - 0.001
2-[4-(diethylamino)phenyl]-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.00001 - 0.00021
2-[4-(dimethylamino)phenyl]-N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]acetamide
0.000005 - 0.000021
3-isopropyl-5(R)-(2-hydroxypropyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000009 - 0.000054
3-isopropyl-5(R)-[1-(hydroxymethyl)propyl]amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.00145 - 0.0036
3-isopropyl-5,7-di[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000012 - 0.000021
3-isopropyl-5-(2,3-dihydroxypropyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000008 - 0.000018
3-isopropyl-5-(2-aminoethyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000001 - 0.000009
3-isopropyl-5-(2-hydroxy-2-methylpropyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000031 - 0.000049
3-isopropyl-5-(2-hydroxyethyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000017 - 0.000051
3-isopropyl-5-(3-amino-2-hydroxypropyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.001486 - 0.004415
3-isopropyl-5-(4-methoxybenzyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000005 - 0.000018
3-isopropyl-5-(N-morpholinyl)-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.00005 - 0.000119
3-isopropyl-5-(piperazin-1-yl)-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000061 - 0.000114
3-isopropyl-5-(thiomorpholinyl)-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000044 - 0.000046
3-isopropyl-5-(trans-2-aminocyclohexyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000096 - 0.000179
3-isopropyl-5-(trans-4-aminocyclohexyl)amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000048 - 0.000229
3-isopropyl-5-methylsulfanyl-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.00007 - 0.000165
3-isopropyl-5-methylsulfonyl-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000024 - 0.000037
3-isopropyl-5-[2-(2-hydroxyethyl)piperidin-1-yl]-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000467 - 0.002136
3-isopropyl-5-[2-(dimethylamino)ethyl]amino-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000132 - 0.000422
3-isopropyl-5-[4-(2-hydroxyethyl)piperazin-1-yl]-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.000183 - 0.000197
3-isopropyl-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidine
0.001764 - 0.00548
4-(1,3-benzothiazol-2-yl)-N-(1,3-thiazol-2-yl)thiophene-2-sulfonamide
0.00822
4-(1,3-benzothiazol-2-yl)-N-(4,5-dimethyl-1,3-thiazol-2-yl)thiophene-2-sulfonamide
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.008274
4-(1,3-benzothiazol-2-yl)-N-(4-methylpyridin-2-yl)thiophene-2-sulfonamide
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.00994
4-(1,3-benzothiazol-2-yl)-N-(5-hydroxypyridin-2-yl)thiophene-2-sulfonamide
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.00547 - 0.00672
4-(1,3-benzothiazol-2-yl)-N-(pyridin-2-ylmethyl)thiophene-2-sulfonamide
0.00742
4-(1,3-benzothiazol-2-yl)-N-hydroxythiophene-2-sulfonamide
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.007704
4-(1,3-benzothiazol-2-yl)-N-[5-(morpholin-4-yl)pyridin-2-yl]thiophene-2-sulfonamide
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.000551 - 0.0045
4-(1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
0.000023
4-(1-ethyl-2-methyl-1H-imidazol-5-yl)-N-[4-(methylsulfonyl)phenyl]pyrimidin-2-amine
Homo sapiens
with isozyme CDK2
0.00631
4-(6-acetyl-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.000001
4-(6-amino-4-cyclohexylmethoxy-5-nitrosopyrimidin-2-ylamino)-benzenesulfonamide
Homo sapiens
-
-
0.0000008 - 0.000034
4-(6-amino-4-cyclohexylmethoxy-5-nitrosopyrimidin-2-ylamino)-N-(2,3-dihydroxypropyl)-benzenesulfonamide
0.0000007
4-(6-amino-4-cyclohexylmethoxy-5-nitrosopyrimidin-2-ylamino)-N-(2-hydroxyethyl)benzenesulfonamide
Homo sapiens
-
-
0.000355 - 0.00086
4-(6-chloro-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
0.000331 - 0.00072
4-(6-fluoro-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
0.000226 - 0.00126
4-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
0.000452 - 0.00127
4-(6-nitro-1,3-benzothiazol-2-yl)thiophene-2-sulfonamide
0.000006 - 0.000204
4-chloro-N-(cis-3-[4-[(naphthalen-1-ylacetyl)amino]-1H-imidazol-1-yl]cyclobutyl)benzamide
0.000012
4-[(4-imidazo[1,2-a]pyridin-3-ylpyrimidin-2-yl)amino]-N-(2-methoxyethyl)benzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000002
4-[(4-imidazo[1,2-a]pyridin-3-ylpyrimidin-2-yl)amino]benzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000003
4-[(4-imidazo[1,2-b]pyridazin-3-ylpyrimidin-2-yl)amino]-N-methylbenzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000033 - 0.00021
4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]-N-(4-[[3-(1,3-oxazetidin-3-yl)propyl]sulfonyl]phenyl)pyrimidin-2-amine
0.000006 - 0.00045
4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]-N-[4-(methylsulfonyl)phenyl]pyrimidin-2-amine
0.000008
4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]-N-[4-(propylsulfonyl)phenyl]pyrimidin-2-amine
Homo sapiens
with isozyme CDK2
0.000013 - 0.00053
4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]-N-[4-[(tetrahydrofuran-2-ylmethyl)sulfonyl]phenyl]pyrimidin-2-amine
0.000492 - 0.000672
4-[7-(4-chloro-3-fluorophenyl)-1,3-benzothiazol-2-yl]thiophene-2-sulfonamide
0.00678
4-[7-(4-fluorophenyl)-1,3-benzothiazol-2-yl]thiophene-2-sulfonamide
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.0004
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)-N-methylbenzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000008 - 0.0056
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)benzenesulfonamide
0.000003
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-methylbenzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000006
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-[3-(1-methylethoxy)propyl]benzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000011
4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]benzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000003
4-[[4-(1-cyclopentyl-2-methyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)benzenesulfonamide
Homo sapiens
with isozyme CDK2, IC50 less than 0.000003 mM
0.000083 - 0.009
4-[[4-(1-cyclopropyl-2-methyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)benzenesulfonamide
0.000004 - 0.0013
4-[[4-(1-ethyl-2-methyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]-N-(2-methoxyethyl)benzenesulfonamide
0.0002
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N,N-diethylbenzamide
Homo sapiens
-
with isozyme CDK2
0.000086
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N,N-diethylbenzenesulfonamide
Homo sapiens
-
with isozyme CDK2
0.00008
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N,N-dimethylbenzamide
Homo sapiens
-
with isozyme CDK2
0.0000013
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N-(2-hydroxypropyl)benzenesulfonamide
Homo sapiens
-
with isozyme CDK2
0.0000081
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N-(tetrahydrofuran-2-ylmethyl)benzenesulfonamide
Homo sapiens
-
with isozyme CDK2
0.000019
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]-N-1,3-thiazol-2-ylbenzenesulfonamide
Homo sapiens
-
with isozyme CDK2
0.000016
4-[[4-amino-6-(cyclohexylmethoxy)-5-nitrosopyrimidin-2-yl]amino]phenol
Homo sapiens
-
with isozyme CDK2
0.059
4-[[4-amino-6-(cyclohexylmethoxy)pyrimidin-2-yl]amino]benzamide
Homo sapiens
-
with isozyme CDK2
0.001942
5,6-dichloro-1-beta-D-ribofuranosyl-benzimidazole
Homo sapiens
-
isoform CDK9, at pH 7.5 and 37°C
0.000008
5-fluoro-6,8-dimethyl-N-(4-morpholin-4-ylphenyl)-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
Homo sapiens
with isozyme CDK2
0.000009
6,8-dimethyl-N-(4-morpholin-4-ylphenyl)-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
Homo sapiens
with isozyme CDK2
0.000003
6,8-dimethyl-N-[4-[4-(methylsulfonyl)piperazin-1-yl]phenyl]-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
Homo sapiens
with isozyme CDK2, IC50 less than 0.000003 mM
0.00034
6-(cyclohexylmethoxy)-N2-(3-methoxyphenyl)-5-nitrosopyrimidine-2,4-diamine
Homo sapiens
-
with isozyme CDK2
0.000215
6-(cyclohexylmethoxy)-N2-(4-methoxyphenyl)-5-nitrosopyrimidine-2,4-diamine
Homo sapiens
-
-
0.0004
6-(cyclohexylmethoxy)-N2-[3-(methylsulfanyl)phenyl]-5-nitrosopyrimidine-2,4-diamine
Homo sapiens
-
with isozyme CDK2
0.06
6-(cyclohexylmethoxy)-N2-[3-(methylsulfanyl)phenyl]pyrimidine-2,4-diamine
Homo sapiens
-
with isozyme CDK2
0.00012
6-(cyclohexylmethoxy)-N2-[4-(methylsulfanyl)phenyl]-5-nitrosopyrimidine-2,4-diamine
Homo sapiens
-
with isozyme CDK2
0.000051
8-(benzylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000004
8-(cyclohexylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]-quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000039
8-(cyclohexylamino)-N-1-dimethyl-4,5-dihydro-1H-pyrazolo-[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000005 - 0.000006
8-(cyclopentylamino)-1-(2,2,2-trifluoroethyl)-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
0.000008
8-(cyclopentylamino)-1-(2-hydroxyethyl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000006
8-(cyclopentylamino)-1-(4-methoxyphenyl)-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000005
8-(cyclopentylamino)-1-(4-sulfamoylphenyl)-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000052
8-(cyclopentylamino)-1-(pyridin-2-yl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000002
8-(cyclopentylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.00002
8-(cyclopentylamino)-1-phenyl-4,5-dihydro-1H-pyrazolo[4,3-h]-quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000097
8-(cyclopentylamino)-N-1-dimethyl-4,5-dihydro-1H-pyrazolo-[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000175
8-(cyclopentylamino)-N-hydroxy-N,1-dimethyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000059
8-(cyclopentylamino)-N-methyl-1-(1-methylpiperidin-4-yl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.00176
8-(cyclopentylamino)-N-[1-(dimethylamino)propan-2-yl]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.01
8-(cyclopentylamino)-N-[2-(dimethylamino)ethyl]-N-1-dimethyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.01
8-amino-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000002
8-[(1-acetylpiperidin-4-yl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000032
8-[(1-acetylpiperidin-4-yl)amino]-N,1-dimethyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000149
8-[(1-ethylpiperidin-4-yl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000019
8-[(2-hydroxyethyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo-[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000066
8-[(3-methoxybenzyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000081
8-[(4-bromobenzyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo-[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000058
8-[(4-methoxybenzyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000013
8-[[4-(acetylamino)benzyl]amino]-1-methyl-4,5-dihydro-1Hpyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000035 - 0.01
alsterpaullone
0.00002 - 0.000033
aminopurvalanol
0.000021 - 0.047
BS-181
0.00509
ethyl [2-([[4-(1,3-benzothiazol-2-yl)thiophen-2-yl]sulfonyl]amino)-1,3-thiazol-4-yl]acetate
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.00035 - 0.1
fascaplysin
0.0000052 - 0.0004
flavopiridol
0.0069
ginsenoside F1
Homo sapiens
-
pH 7.5, 37°C
0.02496
ginsenoside Rb1
Homo sapiens
-
pH 7.5, 37°C
0.00901
ginsenoside Re
Homo sapiens
-
pH 7.5, 37°C
0.00976
ginsenoside Rf
Homo sapiens
-
pH 7.5, 37°C
0.00785
ginsenoside Rg1
Homo sapiens
-
pH 7.5, 37°C
0.0108
ginsenoside Rg2
Homo sapiens
-
pH 7.5, 37°C
0.00728
ginsenoside Rh1
Homo sapiens
-
pH 7.5, 37°C
0.00005 - 0.00023
H717
0.000022 - 0.0006
hymenialdisine
0.00426
LAALS
Homo sapiens
-
0.000044
LDC000067
Homo sapiens
-
isoform CDK9, at pH 7.5 and 37°C
0.000026 - 0.00078
meriolin
0.0000005
N-(1-[4-[(5-fluoro-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]azetidin-3-yl)acetamide
Homo sapiens
with isozyme CDK2
0.000001 - 0.0002
N-(2-methoxyethyl)-4-([4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-yl]amino)benzenesulfonamide
0.000015
N-(2-methoxyethyl)-4-([4-[2-methyl-1-(2-methylpropyl)-1H-imidazol-5-yl]pyrimidin-2-yl]amino)benzenesulfonamide
Homo sapiens
with isozyme CDK2
0.00068 - 0.0086
N-(2-methoxyethyl)-4-[[4-(1,2,4-trimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]benzenesulfonamide
0.000003
N-(4-[4-[(2-methoxyethyl)sulfonyl]piperazin-1-yl]phenyl)-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
Homo sapiens
with isozyme CDK2, IC50 less than 0.000003 mM
0.000295
N-(4-[[3-(dimethylamino)propyl]sulfonyl]phenyl)-4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-amine
Homo sapiens
with isozyme CDK2
0.000036 - 0.00014
N-(4-[[3-(dimethylamino)propyl]sulfonyl]phenyl)-4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-amine
0.002
N-(5-nitro-1H-indazol-3-yl)-2-phenylacetamide
Homo sapiens
with isozyme CDK2
0.001122
N-1-dimethyl-8-([1-[(4-methylpiperazin-1-yl)carbonyl]piperidin-4-yl]amino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.004585
N-1-dimethyl-8-[(1-methylpiperidin-4-yl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000002 - 0.000005
N-1-dimethyl-8-[[1-(methylsulfonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000025
N-1-dimethyl-8-[[1-(phenylcarbonyl)piperidin-4-yl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.001372
N-benzyl-8-(cyclopentylamino)-N-hydroxy-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.000296
N-cyclohexyl-8-(cyclopentylamino)-N-hydroxy-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
pH 7.5, 30°C
0.0000003
N-[(3R)-1-[4-[(5-fluoro-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-yl)amino]phenyl]pyrrolidin-3-yl]acetamide
Homo sapiens
with isozyme CDK2, IC50 above 0.0000003 mM
0.000025
N-[2-(1-aminohydrazino)ethyl]-4-[[4-(1,2-dimethyl-1H-imidazol-5-yl)pyrimidin-2-yl]amino]benzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000008
N-[2-(dimethylamino)ethyl]-4-[(4-imidazo[1,2-b]pyridazin-3-ylpyrimidin-2-yl)amino]benzenesulfonamide
Homo sapiens
with isozyme CDK2
0.000016
N-[4-(4-[[(dimethylamino)acetyl]sulfonyl]piperazin-1-yl)phenyl]-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
Homo sapiens
with isozyme CDK2
0.000003
N-[4-(4-[[2-(dimethylamino)ethyl]sulfonyl]piperazin-1-yl)phenyl]-6,8-dimethyl-5,6-dihydroimidazo[1',5':1,2]pyrido[3,4-d]pyrimidin-2-amine
Homo sapiens
with isozyme CDK2
0.000019 - 0.0015
N-[4-(benzylsulfonyl)phenyl]-4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-amine
0.000014 - 0.00049
N-[4-[(2-methoxyethyl)sulfonyl]phenyl]-4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-amine
0.00003 - 0.00071
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(3-fluorophenyl)acetamide
0.00001 - 0.004
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(3-methylphenyl)acetamide
0.00005 - 0.003
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-fluorophenyl)acetamide
0.000009 - 0.00175
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-hydroxyphenyl)acetamide
0.000007 - 0.0018
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-methylphenyl)acetamide
0.00003 - 0.00075
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-piperidin-1-ylphenyl)acetamide
0.00003 - 0.00133
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-(4-pyridin-4-ylphenyl)acetamide
0.00002 - 0.003
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-naphthalen-1-ylacetamide
0.000009 - 0.0016
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-naphthalen-2-ylacetamide
0.000036 - 0.0037
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-phenylacetamide
0.00001 - 0.0013
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-[4-(methylsulfanyl)phenyl]acetamide
0.000022 - 0.0014
N-[5-(1,1-dioxidoisothiazolidin-2-yl)-1H-indazol-3-yl]-2-[4-(methylsulfonyl)phenyl]acetamide
0.002
N-[5-(2,5-dioxoimidazolidin-1-yl)-1H-indazol-3-yl]-2-phenylacetamide
Homo sapiens
with isozyme CDK2
0.0071
N-[5-(2-oxopiperidin-1-yl)-1H-indazol-3-yl]-2-phenylacetamide
Homo sapiens
with isozyme CDK2
0.00017
N-[5-(2-oxopyrrolidin-1-yl)-1H-indazol-3-yl]-2-phenylacetamide
Homo sapiens
with isozyme CDK2
0.1
N-[5-(dibutylamino)-1H-indazol-3-yl]-2-phenylacetamide
Homo sapiens
with isozyme CDK2, IC50 above 0.1 mM
0.0002
N-[5-(diethylamino)-1H-indazol-3-yl]-2-phenylacetamide
Homo sapiens
with isozyme CDK2
0.0018
N-[5-(dipropylamino)-1H-indazol-3-yl]-2-phenylacetamide
Homo sapiens
with isozyme CDK2
0.0005
N-[5-(ethylamino)-1H-indazol-3-yl]-2-phenylacetamide
Homo sapiens
with isozyme CDK2
0.0005
N2-(3-bromophenyl)-6-(cyclohexylmethoxy)-5-nitrosopyrimidine-2,4-diamine
Homo sapiens
-
with isozyme CDK2
0.026
N2-(3-bromophenyl)-6-(cyclohexylmethoxy)pyrimidine-2,4-diamine
Homo sapiens
-
with isozyme CDK2
0.0036
N4-(6-aminopyrimidin-4-yl)-sulfanilamide
Homo sapiens
-
in 20 mM MOPS (pH 7.5), at 30°C
0.005 - 0.012
NU-2058
0.0013 - 0.0025
NU-6027
0.0000022
NU6027
Homo sapiens
-
-
0.00023
OL567
Homo sapiens
-
CDK1
0.003 - 1
Olomoucine
0.00006 - 0.0198
olomoucine II
0.000008 - 0.04
PD183812
0.00431
protopanaxatriol
Homo sapiens
-
pH 7.5, 37°C
0.000006 - 0.01
purvalanol B
0.0001 - 0.028
roscovitine
0.0000014
SNS-032
Homo sapiens
-
isoform CDK9, at pH 7.5 and 37°C
0.000006 - 0.01
staurosporine
0.00004 - 0.0002
SU-9516
0.0261
TAALS
Homo sapiens
-
0.00888
[(2R)-1-[[4-(1,3-benzothiazol-2-yl)thiophen-2-yl]sulfonyl]pyrrolidin-2-yl]methanol
Homo sapiens
pH 7.35, temperature not specified in the publication, inhibition of cdk5/p25
0.01
[8-(cyclopentylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazolin-3-yl](4-methylpiperazin-1-yl)methanone
Homo sapiens
-
pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.35
assay at
7.4 - 7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
-
assay at room temperature
23
-
assay at
25
-
assay at
3
-
assay at
30 - 37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
primary effusion lymphoma cell line with Kaposi sarcoma-associated herpesvirus-infection, constitutively active K-cyclin/cdk6 kinase
Manually annotated by BRENDA team
-
primary effusion lymphoma cell line with Kaposi sarcoma-associated herpesvirus-infection, constitutively active K-cyclin/cdk6 kinase
Manually annotated by BRENDA team
-
primary effusion lymphoma cell line with Kaposi sarcoma-associated herpesvirus-infection, constitutively active K-cyclin/cdk6 kinase
Manually annotated by BRENDA team
-
CDK5 together with p35
Manually annotated by BRENDA team
mRNA levels of CDK7 are statistically overexpressed in gastric cancer cells when compared with matched normal tissues. Upregulation of cyclin-dependent kinase 7 contributes to metastatic properties of gastric cancer. High expression of MMP14 and CDK7 are independent prognostic factors for overall survival in patients with gastric cancer
Manually annotated by BRENDA team
highly expressed at and after meiosis
Manually annotated by BRENDA team
-
teratocarcinoma cell line
Manually annotated by BRENDA team
-
fibroblasts
Manually annotated by BRENDA team
-
embryonic lung cell line, infected with herpes simplex virus type 1, HSV-1, or an IPO- mutant 7134
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
neuronal
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CDK1_HUMAN
297
0
34095
Swiss-Prot
other Location (Reliability: 1)
MOK_HUMAN
419
0
48014
Swiss-Prot
other Location (Reliability: 1)
CDK6_HUMAN
326
0
36938
Swiss-Prot
other Location (Reliability: 1)
CDK7_HUMAN
346
0
39038
Swiss-Prot
other Location (Reliability: 2)
CDK15_HUMAN
435
0
49023
Swiss-Prot
other Location (Reliability: 1)
CDK16_HUMAN
496
0
55716
Swiss-Prot
other Location (Reliability: 3)
CDK17_HUMAN
523
0
59582
Swiss-Prot
other Location (Reliability: 4)
CDK18_HUMAN
474
0
54424
Swiss-Prot
other Location (Reliability: 4)
CDK19_HUMAN
502
0
56802
Swiss-Prot
other Location (Reliability: 1)
CDKL4_HUMAN
379
0
43384
Swiss-Prot
other Location (Reliability: 2)
CDKL5_HUMAN
960
0
107519
Swiss-Prot
other Location (Reliability: 2)
CDKL1_HUMAN
358
0
41803
Swiss-Prot
other Location (Reliability: 2)
CDKL2_HUMAN
493
0
56019
Swiss-Prot
other Location (Reliability: 1)
CDKL3_HUMAN
592
0
67514
Swiss-Prot
other Location (Reliability: 1)
CDK8_HUMAN
464
0
53284
Swiss-Prot
other Location (Reliability: 1)
CDK9_HUMAN
372
0
42778
Swiss-Prot
other Location (Reliability: 1)
CDK2_HUMAN
298
0
33930
Swiss-Prot
other Location (Reliability: 1)
CDK3_HUMAN
305
0
35046
Swiss-Prot
other Location (Reliability: 1)
CDK4_HUMAN
303
0
33730
Swiss-Prot
other Location (Reliability: 2)
CD11A_HUMAN
783
0
91362
Swiss-Prot
other Location (Reliability: 1)
CD11B_HUMAN
795
0
92620
Swiss-Prot
other Location (Reliability: 1)
CDK10_HUMAN
360
0
41038
Swiss-Prot
other Location (Reliability: 1)
CDK12_HUMAN
1490
0
164155
Swiss-Prot
other Location (Reliability: 1)
CDK13_HUMAN
1512
0
164923
Swiss-Prot
other Location (Reliability: 2)
CDK14_HUMAN
469
0
53057
Swiss-Prot
other Location (Reliability: 2)
CDK20_HUMAN
346
0
38695
Swiss-Prot
other Location (Reliability: 1)
D6RF14_HUMAN
69
0
7719
TrEMBL
other Location (Reliability: 2)
D6RIG9_HUMAN
77
0
8760
TrEMBL
other Location (Reliability: 2)
D6RI01_HUMAN
58
0
6601
TrEMBL
other Location (Reliability: 2)
D6RFL0_HUMAN
43
0
4945
TrEMBL
other Location (Reliability: 2)
D6RGG9_HUMAN
55
0
6249
TrEMBL
other Location (Reliability: 2)
D6R9G1_HUMAN
253
0
28502
TrEMBL
other Location (Reliability: 2)
D6RAD4_HUMAN
309
0
34643
TrEMBL
other Location (Reliability: 2)
D6REC6_HUMAN
149
0
17001
TrEMBL
other Location (Reliability: 2)
A0A0S2Z3F9_HUMAN
346
0
39038
TrEMBL
other Location (Reliability: 2)
D6R9Z2_HUMAN
58
0
6499
TrEMBL
other Location (Reliability: 2)
MAK_HUMAN
623
0
70581
Swiss-Prot
-
CDK5_HUMAN
292
0
33304
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
x * 110000, recombinant CDK11p110, SDS-PAGE
34000
x * 34000
43000
x * 43000
50000
58000
-
x * 58000, CDK11p58
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
cellular GCN5 and P/CAF, members of the GCN5-related N-acetyltransferase family of histone acetyltransferases, regulate CDK9 function by specifically acetylating the catalytic core of the enzyme and, in particular, a lysine that is essential for ATP coordination and the phosphotransfer reaction
lipoprotein
-
membrane association of Cdk5 via myristoylation of p35
phosphoprotein
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal structure of the phosphorylated CDK2-cyclin A/substrate peptide complex, PDB-AC 1QMZ
-
cdk5 in complex with inhibitor 4a, X-ray diffraction structure determination and analysis at 1.90 A resolution
CDK6/cyclin V in complex with flavonol inhibitor fisetin, X-ray diffraction structure determination and analysis at 2.9 A resolution, modeling
-
crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
crystal structure of a complex between CDK2 and (-)-cis-5,7-dihydroxyphenyl-8-[4-(3-hydroxy-1-methyl)piperidinyl] -4H-1-benzopyran-4-one hydrochloride hemihydrate, L868276
crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex determined at 2.3 A resolution
crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
crystal structure of the phosphorylated CDK2-cyclinA-ATP gamma S complex determined at 2.6 A resolution
crystal structures of the human CDK2 apoenzyme and its Mg2+ ATP complex, determined to 2.4 A resolution. The structure is bi-lobate, but contains a unique helix-loop segment that interferes with ATP and protein substrate binding and probably plays a key part in the regulation of all cyclin-dependent kinases
cyclin-dependent kinase-2 complex with mitogen-activated protein kinase-activated protein kinase 2 inhibitor TEI-I01800, sitting drop vapor diffusion method, using 0.1 M HEPES pH 7.4, 10-15% (w/v) PEG 3350 and 50 mM ammonium acetate
-
hanging-drop vapor-diffusion method at 18°C, the crystal structure of CDK2 bound to 2-[2-hydroxyethyl-[6-[(4-methoxyphenyl)methylamino]-9-propan-2-ylpurin-2-yl]amino]ethanol (CVT-313) is determined to a resolution of 1.74 A
high-resolution crystal structures of cyclin-dependent kinase 2 with and without ATP
molecular modeling of CDK2-cyclin A crystal structure, PDB code 1hck, with bound pyrazolo[3,4-c]pyridazine inhibitors
p27KIP1-cyclin A-CDK2 complex, X-ray diffraction structure determination and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D144N
-
dominant-negative CDK5 mutant, results in a loss of motility of the cells through effects on the cytoskeleton, which correlates with dramatically lower invasive potential, leads to 79% reduction in the number of lung metastases per milligram of primary xenograft tumors
F91G
-
replacement of wild-type Cdk7 with a version sensitive to bulky ATP analogs in human cancer cells, designated Cdk7as
K146A
K178A
the mutant shows reduced affinity for inhibitory peptide TAALS
K22Q
-
site-directed mutagenesis, analysis of alterations in binding of INK4 proteins and IkappaBalpha compared to the wild-type enzyme
K35m
-
site-directed mutagenesis of CDK4
K41R
catalytically inactive
N41S
-
site-directed mutagenesis, analysis of alterations in binding of INK4 proteins and IkappaBalpha compared to the wild-type enzyme
R24H
-
naturally occurring activating point mutations R24C and R24H in CDK4 are not seen in sporadic pituitary adenomas, insulinomas, or Leydig cell tumours, but in melanomas, overview
S159E
-
the mutation of Cdk5 inhibits p35 binding
S227A
site-directed mutagenesis, phosphorylation site mutant
T160A
-
site-directed mutagenesis of CDK2, phosphorylation site mutant, the mutant is activated upon binding of cyclin E
T177A
-
site-directed mutagenesis of CDK6
Y180A
the mutant shows reduced affinity for inhibitory peptide TAALS
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
melting temperature (Tm). The Tm shifts are 6.8°C and 10.2°C at 10 mM and 100 mM CVT-313
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the PEST degradation sequence determines the short half-life of cyclin enzyme cofactors
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by immunoprecipitation
-
co-purification of recombinant His-tagged Cdk2/CycE from insect cells
-
glutathione-Sepharose column chromatography
-
native and active CDK1 and CDK2 from NT2 cells by affinity chromatography
-
Ni-NTA column chromatography
-
protein G/protein A-agarose bead chromatography
recombinant C-terminally His6-tagged CDK4 from insect cells by affinity chromatography
-
recombinant Cdk5 from Spodoptera frugiperda Sf9 cells
-
recombinant GST-tagged Cdk2 and GST-tagged cyclin A from Sf9 insect cellsby glutathione affinity chromatography
-
recombinant His6-tagged wild-type and mutant CDK11p110 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, co-purification of CK2, overview
subcellular fractionation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
293T cells transfected with PFTK1 or mutant K146A, overexpression of PFTK1 by retroviral infection of U2OS cells
-
CDK4, DNA and amino acid sequence determinations in pituitary adenomas, insulinomas, or Leydig cell tumours
-
Cdk5 cDNA subcloned into pcDNA 3.1/HisA vector, HEK-293 cells cotransfected with tau protein, GSK3beta, and Cdk5
-
Cdk5, DNA sequence determination and analysis, co-expression of Cdk5 and p35 in HEK293 cells
-
Cdk7as expressed in HCT116 cells
-
co-expression of His-tagged Cdk2/CycE in insect cells
-
co-transfection of HEK 293 cells with myc-Cdk5, His-p25, and either wild-type or parkin mutants
-
DNA and amino acid sequence determination of isozyme alpha2-2, expression of FLAG-tagged or HA-tagged CDK11p110 in COS-7 or HEK293 cells, expression of CDK11p110 in Spodoptera frugiperda Sf9 cells via baculovirus infection system, expression of His6-tagged wild-type and mutant CDK11p110 in Escherichia coli strain BL21(DE3), optimization of an expression system producing enzyme free of CK2, overview
dominant-negative CDK5 mutant subcloned into a bidirectional vector expressing GFP in a Tet-Off system and expressed in AT6.3 cells, mice subcutaneous xenografts of AT6.3 cells expressing the dominant-negative CDK5 mutant
-
expressed from Escherichia coli as GST fusion protein
-
expressed in HEK-293T cells
-
expressed in Sf8 insect cells
-
expressed in Sf9 insect cells
-
expressed in Tn5 insect cells
-
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
expression of C-terminally His6-tagged wild-type and mutant CDK4 in insect cells using the baculovirus infection system with co-expression of cyclin D2, expression of CDK4 and inhibitor IkappaBalpha in the two-hybrid system in Saccharomyces cerevisiae
-
expression of CDK11p58 and HBO1 in the two-hydrid system using Saccharomyces cerevisiae strain EGY48, overexpression of GST- or HA-tagged CDK11p58 in HeLa and COS-1 cells leads to increased histone acetyltransferase HBO1 activity towards free histones
-
expression of CDK2/cyclin A, CDK7/cyclin H, and CDK9/cyclin T in baculovirus-infected insect cells, and expression of CDK5/p25 in Escherichia coli
-
expression of Cdk5 in Spodoptera frugiperda Sf9 cells
-
expression of GFP- and Myc-tagged CDK2 in 293 cells
-
expression of GST-tagged Cdk2 and GST-tagged cyclin A in Spodoptera frugiperda Sf9 cells using the baculovirus infection system
-
expression of HA-tagged CDK6 in 293T cells, stable overexpression of CDK6 in LNCaP cells leads to altered cell colony formation and stimulation of cell growth
-
functional co-expression of CDK2 in 293A, 293T or U2OS cells with myc- or GST-tagged cyclin A or E and with FLAG-tagged human eEF2
-
HeLa cells co-transfected with pCMV-GFP, pCMV-Cyclin A, mutant pCMV-Cdk2-dn or pCMV-p21WAF1/CIP1
-
in vitro transcription and translation of CDK2 in rabbit reticulocyte lysate, expression of HA-tagged wild-type and mutant CDK2 in Sf9 insect cells
-
isolation of cDNA
overexpressed in CHO cells
overexpression in HeLa cells
-
overexpression of wild-type cyclin D1/CDK4 in HeLa cells, coexpression of cyclin D1 or cyclin D1T286A along with either CDK4 or CDK4(K35M) in HeLa cells
-
regulation of p35 expression, overview
-
site-directed mutant proteins, expressed by transient transfection of COS cells
transfection of the erlotinib-sensitive A-431, SK-BR-3, and BT-474 cells with wild-type CDK2, restoration of CDK2 activity and partially restoration of cell proliferation
transient expression of FLAG-CDK8 or kinase-deficient FLAG-CDK8 in HeLa cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
knockout of Cdk5 by siRNA
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the methodologies embodied in transitional dynamic analysis and positional impact vertex for entropy transfer provide a quick approach to identify local fluctuation change important for protein function and residue contacts of CDK2 that contributes to these changes. Further, these approaches can be used to check for possible errors in protein dynamic simulations of CDK2 and have the potential to facilitate a better understanding of the contribution of entropy to protein allostery and function
drug development
medicine
pharmacology
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, L.N.; Noble, M.E.M.; Owen, D.J.
Active and inactive protein kinases: structural basis for regulation
Cell
85
149-158
1996
Homo sapiens
Manually annotated by BRENDA team
Hanks, S.K.
Homology probing: identification of cDNA clones encoding members of the protein-serine kinase family
Proc. Natl. Acad. Sci. USA
84
388-392
1987
Homo sapiens (P11802)
Manually annotated by BRENDA team
Montini, E.; Andolfi, G.; Caruso, A.; Buchner, G.; Walpole, S.M.; Mariani, M.; Consalez, G.; Trump, D.; Ballabio, A.; Franco, B.
Identification and characterization of a novel serine-threonine kinase gene from the Xp22 region
Genomics
51
427-433
1998
Homo sapiens (O76039)
Manually annotated by BRENDA team
Ohta, T.; Okamoto, K.; Isohashi, F.; Shibata, K.; Fukuda, M.; Yamaguchi, S.; Xiong, Y.
T-loop deletion of CDC2 from breast cancer tissues eliminates binding to cyclin B1 and cyclin-dependent kinase inhibitor p21
Cancer Res.
58
1095-1098
1998
Homo sapiens (P06493), Homo sapiens
Manually annotated by BRENDA team
Draetta, G.; Beach, D.
Activation of cdc2 protein kinase during mitosis in human cells: cell cycle-dependent phosphorylation and subunit rearrangement
Cell
54
17-26
1988
Homo sapiens (P06493)
Manually annotated by BRENDA team
Lee, M.G.; Nurse, P.
Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2
Nature
327
31-35
1987
Homo sapiens (P06493)
Manually annotated by BRENDA team
Soufir, N.; Avril, M.F.; Chompret, A.; Demenais, F.; Bombled, J.; Spatz, A.; Stoppa-Lyonnet, D.; Benard, J.; Bressac-de Paillerets, B.
Prevalence of p16 and CDK4 germline mutations in 48 melanoma-prone families in France. The French Familial Melanoma Study Group
Hum. Mol. Genet.
7
209-216
1998
Homo sapiens (P11802)
Manually annotated by BRENDA team
Elkahloun, A.G.; Krizman, D.B.; Wang, Z.; Hofmann, T.A.; Roe, B.; Meltzer, P.S.
Transcript mapping in a 46-kb sequenced region at the core of 12q13.3 amplification in human cancers
Genomics
42
295-301
1997
Homo sapiens (P11802)
Manually annotated by BRENDA team
Zuo, L.; Weger, J.; Yang, Q.; Goldstein, A.M.; Tucker, M.A.; Walker, G.J.; Hayward, N.; Dracopoli, N.C.
Germline mutations in the p16INK4a binding domain of CDK4 in familial melanoma
Nat. Genet.
12
97-99
1996
Homo sapiens (P11802)
Manually annotated by BRENDA team
Wolfel, T.; Hauer, M.; Schneider, J.; Serrano, M.; Wolfel, C.; Klehmann-Hieb, E.; De Plaen, E.; Hankeln, T.; Meyer zum Buschenfelde, K.H.; Beach, D.
A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma
Science
269
1281-1284
1995
Homo sapiens (P11802), Homo sapiens
Manually annotated by BRENDA team
Khatib, Z.A.; Matsushime, H.; Valentine, M.; Shapiro, D.N.; Sherr, C.J.; Look, A.T.
Coamplification of the CDK4 gene with MDM2 and GLI in human sarcomas
Cancer Res.
53
5535-5541
1993
Homo sapiens (P11802), Homo sapiens
Manually annotated by BRENDA team
Matsushime, H.; Jinno, A.; Takagi, N.; Shibuya, M.
A novel mammalian protein kinase gene (mak) is highly expressed in testicular germ cells at and after meiosis
Mol. Cell. Biol.
10
2261-2268
1990
Rattus norvegicus (P20793), Homo sapiens (P20794)
Manually annotated by BRENDA team
Eipers, P.G.; Lahti, J.M.; Kidd, V.J.
Structure and expression of the human p58clk-1 protein kinase chromosomal gene
Genomics
13
613-621
1992
Homo sapiens (P21127), Homo sapiens
Manually annotated by BRENDA team
Bunnell, B.A.; Heath, L.S.; Adams, D.E.; Lahti, J.M.; Kidd, V.J.
Increased expression of a 58-kDa protein kinase leads to changes in the CHO cell cycle
Proc. Natl. Acad. Sci. USA
87
7467-7471
1990
Homo sapiens (P21127), Homo sapiens
Manually annotated by BRENDA team
Gray, N.S.; Wodicka, L.; Thunnissen, A.M.; Norman, T.C.; Kwon, S.; Espinoza, F.H.; Morgan, D.O.; Barnes, G.; LeClerc, S.; Meijer, L.; Kim, S.H.; Lockhart, D.J.; Schultz, P.G.
Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors
Science
281
533-538
1998
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Lawrie, A.M.; Noble, M.E.; Tunnah, P.; Brown, N.R.; Johnson, L.N.; Endicott, J.A.
Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2
Nat. Struct. Biol.
4
796-801
1997
Homo sapiens (P24941)
Manually annotated by BRENDA team
Schulze-Gahmen, U.; De Bondt, H.L.; Kim, S.H.
High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design
J. Med. Chem.
39
4540-4546
1996
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Russo, A.A.; Jeffrey, P.D.; Pavletich, N.P.
Structural basis of cyclin-dependent kinase activation by phosphorylation
Nat. Struct. Biol.
3
696-700
1996
Homo sapiens (P24941)
Manually annotated by BRENDA team
Russo, A.A.; Jeffrey, P.D.; Patten, A.K.; Massague, J.; Pavletich, N.P.
Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
Nature
382
325-331
1996
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
De Azevedo, W.F., Jr.; Mueller-Dieckmann, H.J.; Schulze-Gahmen, U.; Worland, P.J.; Sausville, E.; Kim, S.H.
Structural basis for specificity and potency of a flavonoid inhibitor of human CDK2, a cell cycle kinase
Proc. Natl. Acad. Sci. USA
93
2735-2740
1996
Homo sapiens (P24941)
Manually annotated by BRENDA team
Bourne, Y.; Watson, M.H.; Hickey, M.J.; Holmes, W.; Rocque, W.; Reed, S.I.; Tainer, J.A.
Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
Cell
84
863-874
1996
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Jeffrey, P.D.; Russo, A.A.; Polyak, K.; Gibbs, E.; Hurwitz, J.; Massague, J.; Pavletich, N.P.
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Nature
376
313-320
1995
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
De Bondt, H.L.; Rosenblatt, J.; Jancarik, J.; Jones, H.D.; Morgan, D.O.; Kim, S.H.
Crystal structure of cyclin-dependent kinase 2
Nature
363
595-602
1993
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Gu, Y.; Rosenblatt, J.; Morgan, D.O.
Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15
EMBO J.
11
3995-4005
1992
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Tsai, L.H.; Harlow, E.; Meyerson, M.
Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase
Nature
353
174-177
1991
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Ninomiya-Tsuji, J.; Nomoto, S.; Yasuda, H.; Reed, S.I.; Matsumoto, K.
Cloning of a human cDNA encoding a CDC2-related kinase by complementation of a budding yeast cdc28 mutation
Proc. Natl. Acad. Sci. USA
88
9006-9010
1991
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Elledge, S.J.; Spottswood, M.R.
A new human p34 protein kinase, CDK2, identified by complementation of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus Eg1
EMBO J.
10
2653-2659
1991
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Tassan, J.P.; Jaquenoud, M.; Leopold, P.; Schultz, S.J.; Nigg, E.A.
Identification of human cyclin-dependent kinase 8, a putative protein kinase partner for cyclin C
Proc. Natl. Acad. Sci. USA
92
8871-8875
1995
Homo sapiens (P49336), Homo sapiens
Manually annotated by BRENDA team
Tirode, F.; Busso, D.; Coin, F.; Egly, J.M.
Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7
Mol. Cell
3
87-95
1999
Homo sapiens (P50613)
Manually annotated by BRENDA team
Akoulitchev, S.; Reinberg, D.
The molecular mechanism of mitotic inhibition of TFIIH is mediated by phosphorylation of CDK7
Genes Dev.
12
3541-3550
1998
Homo sapiens (P50613)
Manually annotated by BRENDA team
Wu, L.; Yee, A.; Liu, L.; Carbonaro-Hall, D.; Venkatesan, N.; Tolo, V.T.; Hall, F.L.
Molecular cloning of the human CAK1 gene encoding a cyclin-dependent kinase-activating kinase
Oncogene
9
2089-2096
1994
Homo sapiens (P50613)
Manually annotated by BRENDA team
Tassan, J.P.; Schultz, S.J.; Bartek, J.; Nigg, E.A.
Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase)
J. Cell. Biol.
127
467-478
1994
Homo sapiens (P50613), Homo sapiens
Manually annotated by BRENDA team
Levedakou, E.N.; He, M.; Baptist, E.W.; Craven, R.J.; Cance, W.G.; Welcsh, P.L.; Simmons, A.; Naylor, S.L.; Leach, R.J.; Lewis, T.B.; et al.
Two novel human serine/threonine kinases with homologies to the cell cycle regulating Xenopus MO15, and NIMA kinases: cloning and characterization of their expression pattern
Oncogene
9
1977-1988
1994
Homo sapiens (P50613), Homo sapiens
Manually annotated by BRENDA team
Fisher, R.P.; Morgan, D.O.
A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase
Cell
78
713-724
1994
Homo sapiens (P50613)
Manually annotated by BRENDA team
Darbon, J.M.; Devault, A.; Taviaux, S.; Fesquet, D.; Martinez, A.M.; Galas, S.; Cavadore, J.C.; Doree, M.; Blanchard, J.M.
Cloning, expression and subcellular localization of the human homolog of p40MO15 catalytic subunit of cdk-activating kinase
Oncogene
9
3127-3138
1994
Homo sapiens (P50613), Homo sapiens
Manually annotated by BRENDA team
Liu, H.; Rice, A.P.
Genomic organization and characterization of promoter function of the human CDK9 gene
Gene
252
51-59
2000
Homo sapiens (P50750)
Manually annotated by BRENDA team
Fu, T.J.; Peng, J.; Lee, G.; Price, D.H.; Flores, O.
Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription
J. Biol. Chem.
274
34527-34530
1999
Homo sapiens (P50750)
Manually annotated by BRENDA team
Best, J.L.; Presky, D.H.; Swerlick, R.A.; Burns, D.K.; Chu, W.
Cloning of a full-length cDNA sequence encoding a cdc2-related protein kinase from human endothelial cells
Biochem. Biophys. Res. Commun.
208
562-568
1995
Homo sapiens (P50750), Homo sapiens
Manually annotated by BRENDA team
Grana, X.; De Luca, A.; Sang, N.; Fu, Y.; Claudio, P.P.; Rosenblatt, J.; Morgan, D.O.; Giordano, A.
PITALRE, a nuclear CDC2-related protein kinase that phosphorylates the retinoblastoma protein in vitro
Proc. Natl. Acad. Sci. USA
91
3834-3838
1994
Homo sapiens (P50750), Homo sapiens
Manually annotated by BRENDA team
Meyerson, M.; Enders, G.H.; Wu, C.L.; Su, L.K.; Gorka, C.; Nelson, C.; Harlow, E.; Tsai, L.H.
A family of human cdc2-related protein kinases
EMBO J.
11
2909-2917
1992
Homo sapiens (Q00526), Homo sapiens (Q00532), Homo sapiens (Q00534), Homo sapiens (Q00535), Homo sapiens (Q00536), Homo sapiens (Q00537), Homo sapiens (Q07002), Homo sapiens
Manually annotated by BRENDA team
Russo, A.A.; Tong, L.; Lee, J.O.; Jeffrey, P.D.; Pavletich, N.P.
Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a
Nature
395
237-243
1998
Homo sapiens (Q00534)
Manually annotated by BRENDA team
Crawford, J.; Ianzano, L.; Savino, M.; Whitmore, S.; Cleton-Jansen, A.M.; Settasatian, C.; d'apolito, M.; Seshadri, R.; Pronk, J.C.; Auerbach, A.D.; Verlander, P.C.; Mathew, C.G.; Tipping, A.J.; Doggett, N.A.; Zelante, L.; Callen, D.F.; Savoia, A.
The PISSLRE gene: structure, exon skipping, and exclusion as tumor suppressor in breast cancer
Genomics
56
90-97
1999
Homo sapiens (Q15131)
Manually annotated by BRENDA team
Grana, X.; Claudio, P.P.; De Luca, A.; Sang, N.; Giordano, A.
PISSLRE, a human novel CDC2-related protein kinase
Oncogene
9
2097-2103
1994
Homo sapiens (Q15131), Homo sapiens
Manually annotated by BRENDA team
Brambilla, R.; Draetta, G.
Molecular cloning of PISSLRE, a novel putative member of the cdk family of protein serine/threonine kinases
Oncogene
9
3037-3041
1994
Homo sapiens (Q15131), Homo sapiens
Manually annotated by BRENDA team
Hadano, S.; Hand, C.K.; Osuga, H.; Yanagisawa, Y.; Otomo, A.; Devon, R.S.; Miyamoto, N.; Showguchi-Miyata, J.; Okada, Y.; Singaraja, R.; Figlewicz, D.A.; Kwiatkowski, T.; Hosler, B.A.; Sagie, T.; Skaug, J.; Nasir, J.; Brown, R.H., Jr.; Scherer, S.W.; Rouleau, G.A.; Hayden, M.R.; Ikeda, J.E.
A gene encoding a putative GTPase regulator is mutated in familial amyotrophic lateral sclerosis 2
Nat. Genet.
29
166-173
2001
Homo sapiens (Q96Q40)
Manually annotated by BRENDA team
Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.; Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.
Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
DNA Res.
5
355-364
1998
Homo sapiens (Q9NYV4)
Manually annotated by BRENDA team
Bain, J.; McLauchlan, H.; Elliott, M.; Cohen, P.
The specificities of protein kinase inhibitors: an update
Biochem. J.
371
199-204
2003
Homo sapiens
Manually annotated by BRENDA team
Hamdane, M.; Sambo, A.V.; Delobel, P.; Begard, S.; Violleau, A.; Delacourte, A.; Bertrand, P.; Benavides, J.; Buee, L.
Mitotic-like tau phosphorylation by p25-Cdk5 kinase complex
J. Biol. Chem.
278
34026-34034
2003
Homo sapiens
Manually annotated by BRENDA team
Lambourne, S.L.; Sellers, L.A.; Bush, T.G.; Choudhury, S.K.; Emson, P.C.; Suh, Y.H.; Wilkinson, L.S.
Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: evidence for distinct molecular processes underlying tau abnormalities
Mol. Cell. Biol.
25
278-293
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Bukczynska, P.; Klingler-Hoffmann, M.; Mitchelhill, K.I.; Lam, M.H.C.; Ciccomancini, M.; Tonks, N.K.; Sarcevic, B.; Kemp, B.E.; Tiganis, T.
The T-cell protein tyrosine phosphatase is phosphorylated on Ser-304 by cyclin-dependent protein kinases in mitosis
Biochem. J.
380
939-949
2004
Homo sapiens
Manually annotated by BRENDA team
Li, J.; Joo, S.H.; Tsai, M.D.
An NF-kappaB-specific inhibitor, IkappaBalpha, binds to and inhibits cyclin-dependent kinase 4
Biochemistry
42
13476-13483
2003
Homo sapiens
Manually annotated by BRENDA team
Li, J.; Melvin, W.S.; Tsai, M.D.; Muscarella, P.
The nuclear protein p34SEI-1 regulates the kinase activity of cyclin-dependent kinase 4 in a concentration-dependent manner
Biochemistry
43
4394-4399
2004
Homo sapiens
Manually annotated by BRENDA team
Sachs, N.A.; Vaillancourt, R.R.
Cyclin-dependent kinase 11p110 activity in the absence of CK2
Biochim. Biophys. Acta
1624
98-108
2003
Homo sapiens (P21127)
Manually annotated by BRENDA team
Kesavapany, S.; Li, B.S.; Amin, N.; Zheng, Y.L.; Grant, P.; Pant, H.C.
Neuronal cyclin-dependent kinase 5: role in nervous system function and its specific inhibition by the Cdk5 inhibitory peptide
Biochim. Biophys. Acta
1697
143-153
2004
Danio rerio, Saccharomyces cerevisiae, Caenorhabditis elegans, Canis lupus familiaris, Drosophila melanogaster, Homo sapiens, Doryteuthis pealeii, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Andres, V.
Control of vascular cell proliferation and migration by cyclin-dependent kinase signalling: new perspectives and therapeutic potential
Cardiovasc. Res.
63
11-21
2004
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Furet, P.
X-ray crystallographic studies of CDK2, a basis for cyclin-dependent kinase inhibitor design in anti-cancer drug research
Curr. Med. Chem. Anticancer Agents
3
15-23
2003
Homo sapiens
Manually annotated by BRENDA team
Zong, H.; Li, Z.; Liu, L.; Hong, Y.; Yun, X.; Jiang, J.; Chi, Y.; Wang, H.; Shen, X.; Hu, Y.; Niu, Z.; Gu, J.
Cyclin-dependent kinase 11(p58) interacts with HBO1 and enhances its histone acetyltransferase activity
FEBS Lett.
579
3579-3588
2005
Homo sapiens
Manually annotated by BRENDA team
D'Angiolella, V.; Mari, C.; Nocera, D.; Rametti, L.; Grieco, D.
The spindle checkpoint requires cyclin-dependent kinase activity
Genes Dev.
17
2520-2525
2003
Homo sapiens, Xenopus laevis
Manually annotated by BRENDA team
Harwell, R.M.; Mull, B.B.; Porter, D.C.; Keyomarsi, K.
Activation of cyclin-dependent kinase 2 by full length and low molecular weight forms of cyclin E in breast cancer cells
J. Biol. Chem.
279
12695-12705
2004
Homo sapiens
Manually annotated by BRENDA team
Vax, V.V.; Bibi, R.; Diaz-Cano, S.; Gueorguiev, M.; Kola, B.; Borboli, N.; Bressac-de Paillerets, B.; Walker, G.J.; Dedov, II; Grossman, A.B.; Korbonits, M.
Activating point mutations in cyclin-dependent kinase 4 are not seen in sporadic pituitary adenomas, insulinomas or Leydig cell tumours
J. Endocrinol.
178
301-310
2003
Homo sapiens
Manually annotated by BRENDA team
Woodard, C.L.; Li, Z.; Kathcart, A.K.; Terrell, J.; Gerena, L.; Lopez-Sanchez, M.; Kyle, D.E.; Bhattacharjee, A.K.; Nichols, D.A.; Ellis, W.; Prigge, S.T.; Geyer, J.A.; Waters, N.C.
Oxindole-based compounds are selective inhibitors of Plasmodium falciparum cyclin dependent protein kinases
J. Med. Chem.
46
3877-3882
2003
Homo sapiens, Plasmodium falciparum
Manually annotated by BRENDA team
VanderWel, S.N.; Harvey, P.J.; McNamara, D.J.; Repine, J.T.; Keller, P.R.; Quin, J.3rd.; Booth, R.J.; Elliott, W.L.; Dobrusin, E.M.; Fry, D.W.; Toogood, P.L.
Pyrido[2,3-d]pyrimidin-7-ones as specific inhibitors of cyclin-dependent kinase 4
J. Med. Chem.
48
2371-2387
2005
Homo sapiens
Manually annotated by BRENDA team
Brana, M.F.; Cacho, M.; Garcia, M.L.; Mayoral, E.P.; Lopez, B.; de Pascual-Teresa, B.; Ramos, A.; Acero, N.; Llinares, F.; Munoz-Mingarro, D.; Lozach, O.; Meijer, L.
Pyrazolo[3,4-c]pyridazines as novel and selective inhibitors of cyclin-dependent kinases
J. Med. Chem.
48
6843-6854
2005
Marthasterias glacialis, Homo sapiens (P24941)
Manually annotated by BRENDA team
Lu, H.; Chang, D.J.; Baratte, B.; Meijer, L.; Schulze-Gahmen, U.
Crystal structure of a human cyclin-dependent kinase 6 complex with a flavonol inhibitor, fisetin
J. Med. Chem.
48
737-743
2005
Homo sapiens
Manually annotated by BRENDA team
Van Dross, R.; Yao, S.; Asad, S.; Westlake, G.; Mays, D.J.; Barquero, L.; Duell, S.; Pietenpol, J.A.; Browning, P.J.
Constitutively active K-cyclin/cdk6 kinase in Kaposi sarcoma-associated herpesvirus-infected cells
J. Natl. Cancer Inst.
97
656-666
2005
Homo sapiens
Manually annotated by BRENDA team
Davido, D.J.; Von Zagorski, W.F.; Maul, G.G.; Schaffer, P.A.
The differential requirement for cyclin-dependent kinase activities distinguishes two functions of herpes simplex virus type 1 ICP0
J. Virol.
77
12603-12616
2003
Homo sapiens
Manually annotated by BRENDA team
Sanchez, V.; McElroy, A.K.; Spector, D.H.
Mechanisms governing maintenance of Cdk1/cyclin B1 kinase activity in cells infected with human cytomegalovirus
J. Virol.
77
13214-13224
2003
Homo sapiens
Manually annotated by BRENDA team
Sanchez, V.; McElroy, A.K.; Yen, J.; Tamrakar, S.; Clark, C.L.; Schwartz, R.A.; Spector, D.H.
Cyclin-dependent kinase activity is required at early times for accurate processing and accumulation of the human cytomegalovirus UL122-123 and UL37 immediate-early transcripts and at later times for virus production
J. Virol.
78
11219-11232
2004
Homo sapiens
Manually annotated by BRENDA team
Narayanan, R.; Adigun, A.A.; Edwards, D.P.; Weigel, N.L.
Cyclin-dependent kinase activity is required for progesterone receptor function: novel role for cyclin A/Cdk2 as a progesterone receptor coactivator
Mol. Cell. Biol.
25
264-277
2005
Homo sapiens
Manually annotated by BRENDA team
Hisanaga, S.; Saito, T.
The regulation of cyclin-dependent kinase 5 activity through the metabolism of p35 or p39 Cdk5 activator
Neurosignals
12
221-229
2003
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Gompel, M.; Soulie, C.; Ceballos-Picot, I.; Meijer, L.
Expression and activity of cyclin-dependent kinases and glycogen synthase kinase-3 during NT2 neuronal differentiation
Neurosignals
13
134-143
2004
Homo sapiens
Manually annotated by BRENDA team
Watanabe, N.; Arai, H.; Iwasaki, J.i.; Shiina, M.; Ogata, K.; Hunter, T.; Osada, H.
Cyclin-dependent kinase (CDK) phosphorylation destabilizes somatic wee1 via multiple pathways
Proc. Natl. Acad. Sci. USA
102
11663-11668
2005
Homo sapiens
Manually annotated by BRENDA team
Lim, J.T.; Mansukhani, M.; Weinstein, I.B.
Cyclin-dependent kinase 6 associates with the androgen receptor and enhances its transcriptional activity in prostate cancer cells
Proc. Natl. Acad. Sci. USA
102
5156-5161
2005
Homo sapiens
Manually annotated by BRENDA team
Bartova, I.; Otyepka, M.; Kriz, Z.; Koca, J.
The mechanism of inhibition of the cyclin-dependent kinase-2 as revealed by the molecular dynamics study on the complex CDK2 with the peptide substrate HHASPRK
Protein Sci.
14
445-451
2005
Homo sapiens
Manually annotated by BRENDA team
Choi, J.S.; Shin, S.; Jin, Y.H.; Yim, H.; Koo, K.T.; Chun, K.H.; Oh, Y.T.; Lee, W.H.; Lee, S.K.
Cyclin-dependent protein kinase 2 activity is required for mitochondrial translocation of Bax and disruption of mitochondrial transmembrane potential during etoposide-induced apoptosis
Apoptosis
12
1229-1241
2007
Homo sapiens
Manually annotated by BRENDA team
Li, T.; Hawkes, C.; Qureshi, H.Y.; Kar, S.; Paudel, H.K.
Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta
Biochemistry
45
3134-3145
2006
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Gu, J.; Bourne, P.E.
Identifying allosteric fluctuation transitions between different protein conformational states as applied to cyclin dependent kinase 2
BMC Bioinformatics
8
45
2007
Homo sapiens
Manually annotated by BRENDA team
Yang, H.S.; Hinds, P.W.
Phosphorylation of ezrin by cyclin-dependent kinase 5 induces the release of Rho GDP dissociation inhibitor to inhibit Rac1 activity in senescent cells
Cancer Res.
66
2708-2715
2006
Homo sapiens
Manually annotated by BRENDA team
den Hollander, P.; Kumar, R.
Dynein light chain 1 contributes to cell cycle progression by increasing cyclin-dependent kinase 2 activity in estrogen-stimulated cells
Cancer Res.
66
5941-5949
2006
Homo sapiens
Manually annotated by BRENDA team
Strock, C.J.; Park, J.I.; Nakakura, E.K.; Bova, G.S.; Isaacs, J.T.; Ball, D.W.; Nelkin, B.D.
Cyclin-dependent kinase 5 activity controls cell motility and metastatic potential of prostate cancer cells
Cancer Res.
66
7509-7515
2006
Homo sapiens
Manually annotated by BRENDA team
Bayart, E.; Dutertre, S.; Jaulin, C.; Guo, R.B.; Xi, X.G.; Amor-Gueret, M.
The Bloom syndrome helicase is a substrate of the mitotic Cdc2 kinase
Cell Cycle
5
1681-1686
2006
Homo sapiens
Manually annotated by BRENDA team
Sengupta, A.; Novak, M.; Grundke-Iqbal, I.; Iqbal, K.
Regulation of phosphorylation of tau by cyclin-dependent kinase 5 and glycogen synthase kinase-3 at substrate level
FEBS Lett.
580
5925-5933
2006
Homo sapiens
Manually annotated by BRENDA team
Enders, G.H.; Maude, S.L.
Traffic safety for the cell: influence of cyclin-dependent kinase activity on genomic stability
Gene
371
1-6
2006
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Avraham, E.; Rott, R.; Liani, E.; Szargel, R.; Engelender, S.
Phosphorylation of Parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation
J. Biol. Chem.
282
12842-12850
2007
Homo sapiens, Rattus norvegicus, Rattus norvegicus (Q03114)
Manually annotated by BRENDA team
Sanchez, V.; Spector, D.H.
Cyclin-dependent kinase activity is required for efficient expression and posttranslational modification of human cytomegalovirus proteins and for production of extracellular particles
J. Virol.
80
5886-5896
2006
Homo sapiens
Manually annotated by BRENDA team
Yamasaki, F.; Zhang, D.; Bartholomeusz, C.; Sudo, T.; Hortobagyi, G.N.; Kurisu, K.; Ueno, N.T.
Sensitivity of breast cancer cells to erlotinib depends on cyclin-dependent kinase 2 activity
Mol. Cancer Ther.
6
2168-2177
2007
Homo sapiens, Homo sapiens (P24941)
Manually annotated by BRENDA team
Larochelle, S.; Merrick, K.A.; Terret, M.E.; Wohlbold, L.; Barboza, N.M.; Zhang, C.; Shokat, K.M.; Jallepalli, P.V.; Fisher, R.P.
Requirements for Cdk7 in the assembly of Cdk1/cyclin B and activation of Cdk2 revealed by chemical genetics in human cells
Mol. Cell
25
839-850
2007
Homo sapiens
Manually annotated by BRENDA team
Shu, F.; Lv, S.; Qin, Y.; Ma, X.; Wang, X.; Peng, X.; Luo, Y.; Xu, B.E.; Sun, X.; Wu, J.
Functional characterization of human PFTK1 as a cyclin-dependent kinase
Proc. Natl. Acad. Sci. USA
104
9248-9253
2007
Homo sapiens
Manually annotated by BRENDA team
Moore, N.L.; Narayanan, R.; Weigel, N.L.
Cyclin dependent kinase 2 and the regulation of human progesterone receptor activity
Steroids
72
202-209
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Liu, M.; Choi, S.; Cuny, G.D.; Ding, K.; Dobson, B.C.; Glicksman, M.A.; Auerbach, K.; Stein, R.L.
Kinetic studies of Cdk5/p25 kinase: phosphorylation of tau and complex inhibition by two prototype inhibitors
Biochemistry
47
8367-8377
2008
Homo sapiens
Manually annotated by BRENDA team
Chen, S.; Chen, L.; Le, N.T.; Zhao, C.; Sidduri, A.; Lou, J.P.; Michoud, C.; Portland, L.; Jackson, N.; Liu, J.J.; Konzelmann, F.; Chi, F.; Tovar, C.; Xiang, Q.; Chen, Y.; Wen, Y.; Vassilev, L.T.
Synthesis and activity of quinolinyl-methylene-thiazolinones as potent and selective cyclin-dependent kinase 1 inhibitors
Bioorg. Med. Chem. Lett.
17
2134-2138
2007
Homo sapiens (P06493), Homo sapiens
Manually annotated by BRENDA team
Lee, J.; Choi, H.; Kim, K.H.; Jeong, S.; Park, J.W.; Baek, C.S.; Lee, S.H.
Synthesis and biological evaluation of 3,5-diaminoindazoles as cyclin-dependent kinase inhibitors
Bioorg. Med. Chem. Lett.
18
2292-2295
2008
Homo sapiens, Homo sapiens (P06493), Homo sapiens (P24941)
Manually annotated by BRENDA team
Finlay, M.R.; Acton, D.G.; Andrews, D.M.; Barker, A.J.; Dennis, M.; Fisher, E.; Graham, M.A.; Green, C.P.; Heaton, D.W.; Karoutchi, G.; Loddick, S.A.; Morgentin, R.; Roberts, A.; Tucker, J.A.; Weir, H.M.
Imidazole piperazines: SAR and development of a potent class of cyclin-dependent kinase inhibitors with a novel binding mode
Bioorg. Med. Chem. Lett.
18
4442-4446
2008
Homo sapiens (P24941)
Manually annotated by BRENDA team
Anderson, M.; Andrews, D.M.; Barker, A.J.; Brassington, C.A.; Breed, J.; Byth, K.F.; Culshaw, J.D.; Finlay, M.R.; Fisher, E.; McMiken, H.H.; Green, C.P.; Heaton, D.W.; Nash, I.A.; Newcombe, N.J.; Oakes, S.E.; Pauptit, R.A.; Roberts, A.; Stanway, J.J.; Thomas, A.P.; Tucker, J.A.; Walker, M.; Weir, H.M.
Imidazoles: SAR and development of a potent class of cyclin-dependent kinase inhibitors
Bioorg. Med. Chem. Lett.
18
5487-5492
2008
Homo sapiens (P11802), Homo sapiens (P24941)
Manually annotated by BRENDA team
De Vivo, M.; Cavalli, A.; Carloni, P.; Recanatini, M.
Computational study of the phosphoryl transfer catalyzed by a cyclin-dependent kinase
Chemistry
13
8437-8444
2007
Homo sapiens
Manually annotated by BRENDA team
North, B.J.; Verdin, E.
Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation
J. Biol. Chem.
282
19546-19555
2007
Homo sapiens (P06493), Homo sapiens
Manually annotated by BRENDA team
Paoletti, P.; Vila, I.; Rife, M.; Lizcano, J.M.; Alberch, J.; Gines, S.
Dopaminergic and glutamatergic signaling crosstalk in Huntingtons disease neurodegeneration: the role of p25/cyclin-dependent kinase 5
J. Neurosci.
28
10090-10101
2008
Mus musculus, Homo sapiens (Q00535), Homo sapiens
Manually annotated by BRENDA team
Sanchez, V.; Mahr, J.A.; Orazio, N.I.; Spector, D.H.
Nuclear export of the human cytomegalovirus tegument protein pp65 requires cyclin-dependent kinase activity and the Crm1 exporter
J. Virol.
81
11730-11736
2007
Homo sapiens
Manually annotated by BRENDA team
Sabo, A.; Lusic, M.; Cereseto, A.; Giacca, M.
Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulates transcription
Mol. Cell. Biol.
28
2201-2212
2008
Homo sapiens (P50750)
Manually annotated by BRENDA team
Lewis, A.E.; Rusten, M.; Hoivik, E.A.; Vikse, E.L.; Hansson, M.L.; Wallberg, A.E.; Bakke, M.
Phosphorylation of steroidogenic factor 1 is mediated by cyclin-dependent kinase 7
Mol. Endocrinol.
22
91-104
2008
Homo sapiens (P50613), Mus musculus (Q03147)
Manually annotated by BRENDA team
Costoya, J.A.; Hobbs, R.M.; Pandolfi, P.P.
Cyclin-dependent kinase antagonizes promyelocytic leukemia zinc-finger through phosphorylation
Oncogene
27
3789-3796
2008
Homo sapiens (P06493), Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Marchetti, F.; Sayle, K.L.; Bentley, J.; Clegg, W.; Curtin, N.J.; Endicott, J.A.; Golding, B.T.; Griffin, R.J.; Haggerty, K.; Harrington, R.W.; Mesguiche, V.; Newell, D.R.; Noble, M.E.; Parsons, R.J.; Pratt, D.J.; Wang, L.Z.; Hardcastle, I.R.
Structure-based design of 2-arylamino-4-cyclohexylmethoxy-5-nitroso-6-aminopyrimidine inhibitors of cyclin-dependent kinase 2
Org. Biomol. Chem.
5
1577-1585
2007
Homo sapiens
Manually annotated by BRENDA team
Bartova, I.; Koca, J.; Otyepka, M.
Functional flexibility of human cyclin-dependent kinase-2 and its evolutionary conservation
Protein Sci.
17
22-33
2008
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Chen, H.; Van Duyne, R.; Zhang, N.; Kashanchi, F.; Zeng, C.
A novel binding pocket of cyclin-dependent kinase 2
Proteins
74
122-132
2008
Homo sapiens (P24941)
Manually annotated by BRENDA team
Wang, S.; Fischer, P.M.
Cyclin-dependent kinase 9: a key transcriptional regulator and potential drug target in oncology, virology and cardiology
Trends Pharmacol. Sci.
29
302-313
2008
Homo sapiens (P50750)
Manually annotated by BRENDA team
Chen, R.; Wierda, W.G.; Chubb, S.; Hawtin, R.E.; Fox, J.A.; Keating, M.J.; Gandhi, V.; Plunkett, W.
Mechanism of action of SNS-032, a novel cyclin-dependent kinase inhibitor, in chronic lymphocytic leukemia
Blood
113
4637-4645
2009
Homo sapiens
Manually annotated by BRENDA team
Leitch, A.E.; Haslett, C.; Rossi, A.G.
Cyclin-dependent kinase inhibitor drugs as potential novel anti-inflammatory and pro-resolution agents
Br. J. Pharmacol.
158
1004-1016
2009
Homo sapiens
Manually annotated by BRENDA team
Ali, S.; Heathcote, D.A.; Kroll, S.H.; Jogalekar, A.S.; Scheiper, B.; Patel, H.; Brackow, J.; Siwicka, A.; Fuchter, M.J.; Periyasamy, M.; Tolhurst, R.S.; Kanneganti, S.K.; Snyder, J.P.; Liotta, D.C.; Aboagye, E.O.; Barrett, A.G.; Coombes, R.C.
The development of a selective cyclin-dependent kinase inhibitor that shows antitumor activity
Cancer Res.
69
6208-6215
2009
Homo sapiens
Manually annotated by BRENDA team
Uchiyama, H.; Sowa, Y.; Wakada, M.; Yogosawa, M.; Nakanishi, R.; Horinaka, M.; Shimazaki, C.; Taniwaki, M.; Sakai, T.
Cyclin-dependent kinase inhibitor SU9516 enhances sensitivity to methotrexate in human T-cell leukemia Jurkat cells
Cancer Sci.
101
728-734
2010
Homo sapiens
Manually annotated by BRENDA team
Bonvini, P.; Zorzi, E.; Mussolin, L.; Monaco, G.; Pigazzi, M.; Basso, G.; Rosolen, A.
The effect of the cyclin-dependent kinase inhibitor flavopiridol on anaplastic large cell lymphoma cells and relationship with NPM-ALK kinase expression and activity
Haematologica
94
944-955
2009
Homo sapiens
Manually annotated by BRENDA team
Kim, H.S.; Lee, W.J.; Lee, S.W.; Chae, H.W.; Kim, D.H.; Oh, Y.
Insulin-like growth factor binding protein-3 induces G1 cell cycle arrest with inhibition of cyclin-dependent kinase 2 and 4 in MCF-7 human breast cancer Ccells
Horm. Metab. Res.
42
165-172
2009
Homo sapiens
Manually annotated by BRENDA team
Mohapatra, S.; Chu, B.; Zhao, X.; Djeu, J.; Cheng, J.Q.; Pledger, W.J.
Apoptosis of metastatic prostate cancer cells by a combination of cyclin-dependent kinase and AKT inhibitors
Int. J. Biochem. Cell Biol.
41
595-602
2009
Homo sapiens
Manually annotated by BRENDA team
Moss, S.C.; Lightell, D.J.; Marx, S.O.; Marks, A.R.; Woods, T.C.
Rapamycin regulates endothelial cell migration through regulation of the cyclin-dependent kinase inhibitor, p27Kip1
J. Biol. Chem.
285
11991-11997
2010
Homo sapiens
Manually annotated by BRENDA team
Tan, V.B.; Zhang, B.; Lim, K.M.; Tay, T.E.
Explaining the inhibition of cyclin-dependent kinase 5 by peptides derived from p25 with molecular dynamics simulations and MM-PBSA
J. Mol. Model.
16
1-8
2010
Homo sapiens
Manually annotated by BRENDA team
Malmstroem, J.; Viklund, J.; Slivo, C.; Costa, A.; Maudet, M.; Sandelin, C.; Hiller, G.; Olsson, L.L.; Aagaard, A.; Geschwindner, S.; Xue, Y.; Vasaenge, M.
Synthesis and structure-activity relationship of 4-(1,3-benzothiazol-2-yl)-thiophene-2-sulfonamides as cyclin-dependent kinase 5 (cdk5)/p25 inhibitors
Bioorg. Med. Chem. Lett.
22
5919-5923
2012
Homo sapiens (Q00535)
Manually annotated by BRENDA team
Aggarwal, P.; Vaites, L.P.; Kim, J.K.; Mellert, H.; Gurung, B.; Nakagawa, H.; Herlyn, M.; Hua, X.; Rustgi, A.K.; McMahon, S.B.; Diehl, J.A.
Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase
Cancer Cell
18
329-340
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Leitch, A.E.; Lucas, C.D.; Marwick, J.A.; Duffin, R.; Haslett, C.; Rossi, A.G.
Cyclin-dependent kinases 7 and 9 specifically regulate neutrophil transcription and their inhibition drives apoptosis to promote resolution of inflammation
Cell Death Differ.
19
1950-1961
2012
Homo sapiens
Manually annotated by BRENDA team
Flores, O.; Wang, Z.; Knudsen, K.E.; Burnstein, K.L.
Nuclear targeting of cyclin-dependent kinase 2 reveals essential roles of cyclin-dependent kinase 2 localization and cyclin E in vitamin D-mediated growth inhibition
Endocrinology
151
896-908
2010
Homo sapiens
Manually annotated by BRENDA team
Ngompaza-Diarra, J.; Bettayeb, K.; Gresh, N.; Meijer, L.; Oumata, N.
Synthesis and biological evaluation of selective and potent cyclin-dependent kinase inhibitors
Eur. J. Med. Chem.
56
210-216
2012
Asteroidea, Homo sapiens
Manually annotated by BRENDA team
Moshe, Y.; Bar-On, O.; Ganoth, D.; Hershko, A.
Regulation of the action of early mitotic inhibitor 1 on the anaphase-promoting complex/cyclosome by cyclin-dependent kinases
J. Biol. Chem.
286
16647-16657
2011
Homo sapiens
Manually annotated by BRENDA team
Cuomo, M.E.; Platt, G.M.; Pearl, L.H.; Mittnacht, S.
Cyclin-cyclin-dependent kinase regulatory response is linked to substrate recognition
J. Biol. Chem.
286
9713-9725
2011
Homo sapiens, Human gammaherpesvirus 8
Manually annotated by BRENDA team
Traquandi, G.; Ciomei, M.; Ballinari, D.; Casale, E.; Colombo, N.; Croci, V.; Fiorentini, F.; Isacchi, A.; Longo, A.; Mercurio, C.; Panzeri, A.; Pastori, W.; Pevarello, P.; Volpi, D.; Roussel, P.; Vulpetti, A.; Brasca, M.G.
Identification of potent pyrazolo[4,3-h]quinazoline-3-carboxamides as multi-cyclin-dependent kinase inhibitors
J. Med. Chem.
53
2171-2187
2010
Homo sapiens
Manually annotated by BRENDA team
Hisanaga, S.; Endo, R.
Regulation and role of cyclin-dependent kinase activity in neuronal survival and death
J. Neurochem.
115
1309-1321
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Rovnak, J.; Brewster, C.D.; Quackenbush, S.L.
Retroviral cyclin enhances cyclin-dependent kinase-8 activity
J. Virol.
86
5742-5751
2012
Homo sapiens
Manually annotated by BRENDA team
Hizli, A.A.; Chi, Y.; Swanger, J.; Carter, J.H.; Liao, Y.; Welcker, M.; Ryazanov, A.G.; Clurman, B.E.
Phosphorylation of eukaryotic elongation factor 2 (eEF2) by cyclin A-cyclin-dependent kinase 2 regulates its inhibition by eEF2 kinase
Mol. Cell. Biol.
33
596-604
2013
Homo sapiens
Manually annotated by BRENDA team
Wang, H.; Xu, Y.; Fang, Z.; Chen, S.; Balk, S.P.; Yuan, X.
Doxycycline regulated induction of AKT in murine prostate drives proliferation independently of p27 cyclin dependent kinase inhibitor downregulation
PLoS ONE
7
e41330
2012
Homo sapiens
Manually annotated by BRENDA team
Liberal, V.; Martinsson-Ahlzen, H.S.; Liberal, J.; Spruck, C.H.; Widschwendter, M.; McGowan, C.H.; Reed, S.I.
Cyclin-dependent kinase subunit (Cks) 1 or Cks2 overexpression overrides the DNA damage response barrier triggered by activated oncoproteins
Proc. Natl. Acad. Sci. USA
109
2754-2759
2012
Homo sapiens
Manually annotated by BRENDA team
Chen, N.; Yang, H.; Niu, J.; Liu, S.
Determination of kinetic parameters and structure-activity relationships of ginsenosides as inhibitors of cyclin-dependent kinase 5/p25 using ultra-pressure liquid chromatography with triple quadrupole tandem mass spectrometry
Rapid Commun. Mass Spectrom.
27
985-992
2013
Homo sapiens
Manually annotated by BRENDA team
Albert, T.K.; Rigault, C.; Eickhoff, J.; Baumgart, K.; Antrecht, C.; Klebl, B.; Mittler, G.; Meisterernst, M.
Characterization of molecular and cellular functions of the cyclin-dependent kinase CDK9 using a novel specific inhibitor
Br. J. Pharmacol.
171
55-68
2014
Homo sapiens
Manually annotated by BRENDA team
Vymetalova, L.; Havlicek, L.; Sturc, A.; Skraskova, Z.; Jorda, R.; Pospisil, T.; Strnad, M.; Krystof, V.
5-Substituted 3-isopropyl-7-[4-(2-pyridyl)benzyl]amino-1(2)H-pyrazolo[4,3-d]pyrimidines with anti-proliferative activity as potent and selective inhibitors of cyclin-dependent kinases
Eur. J. Med. Chem.
110
291-301
2016
Homo sapiens
Manually annotated by BRENDA team
Fujino, A.; Fukushima, K.; Kubota, T.; Kosugi, T.; Takimoto-Kamimura, M.
Crystal structure of human cyclin-dependent kinase-2 complex with MK2 inhibitor TEI-I01800: insight into the selectivity
J. Synchrotron Radiat.
20
905-909
2013
Homo sapiens
Manually annotated by BRENDA team
Liang, K.; Gao, X.; Gilmore, J.M.; Florens, L.; Washburn, M.P.; Smith, E.; Shilatifard, A.
Characterization of human cyclin-dependent kinase 12 (CDK12) and CDK13 complexes in C-terminal domain phosphorylation, gene transcription, and RNA processing
Mol. Cell. Biol.
35
928-938
2015
Homo sapiens (Q14004), Homo sapiens (Q9NYV4), Homo sapiens
Manually annotated by BRENDA team
Petrone, A.; Adamo, M.E.; Cheng, C.; Kettenbach, A.N.
Identification of candidate cyclin-dependent kinase 1 (Cdk1) substrates in mitosis by quantitative phosphoproteomics
Mol. Cell. Proteomics
15
2448-2461
2016
Homo sapiens
Manually annotated by BRENDA team
Talapati, S.; Nataraj, V.; Pothuganti, M.; Gore, S.; Ramachandra, M.; Antony, T.; More, S.; Krishnamurthy, N.
Structure of cyclin-dependent kinase 2 (CDK2) in complex with the specific and potent inhibitor CVT-313
Acta Crystallogr. Sect. F
76
350-356
2020
Homo sapiens (P24941), Homo sapiens
Manually annotated by BRENDA team
Beaujois, R.; Ottoni, E.; Zhang, X.; Gagnon, C.; HSine, S.; Mollet, S.; Viranaicken, W.; DesGroseillers, L.
The M-phase specific hyperphosphorylation of Staufen2 involved the cyclin-dependent kinase CDK1
BMC Cell Biol.
18
25
2017
Homo sapiens (P06493)
Manually annotated by BRENDA team
Naseh, G.; Mohammadifard, M.; Mohammadifard, M.
Upregulation of cyclin-dependent kinase 7 and matrix metalloproteinase-14 expression contribute to metastatic properties of gastric cancer
IUBMB Life
2020
799-805
2016
Homo sapiens (P50613)
Manually annotated by BRENDA team
Mbonye, U.; Wang, B.; Gokulrangan, G.; Shi, W.; Yang, S.; Karn, J.
Cyclin-dependent kinase 7 (CDK7)-mediated phosphorylation of the CDK9 activation loop promotes P-TEFb assembly with Tat and proviral HIV reactivation
J. Biol. Chem.
293
10009-10025
2018
Homo sapiens (P50613)
Manually annotated by BRENDA team