Information on EC 2.7.11.21 - polo kinase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.7.11.21
-
RECOMMENDED NAME
GeneOntology No.
polo kinase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + a protein = ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
ATP + a protein = ADP + a phosphoprotein
show the reaction diagram
consensus sequence of Plk1 is D/E-X-S/T-hydrophobic amino acid-X-D/E, X can be any amino acid, with neighbouring phosphorylation sequence L-Q-S-V-L-E being phosphorylated at the serine residue
-
ATP + a protein = ADP + a phosphoprotein
show the reaction diagram
the Plk consensus sequence is D/E-X-S/T-hydrophobic amino acid-X-D/E with X being any amino acid
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (spindle-pole-dependent)
The enzyme associates with the spindle pole during mitosis and is thought to play an important role in the dynamic function of the mitotic spindle during chromosome segregation. The human form of the enzyme, Plk1, does not phosphorylate histone H1, enolase and phosvitin but it can phosphorylate myelin basic protein and microtubule-associated protein MAP-2, although to a lesser extent than casein [2].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
FGF-inducible kinase
-
-
-
-
Proliferation-related kinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
149433-93-2
Polo kinase
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
diverse strains
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Plk3
SwissProt
Manually annotated by BRENDA team
female Wistar rats
SwissProt
Manually annotated by BRENDA team
diverse strains derived from strain W303
-
-
Manually annotated by BRENDA team
strains isogenic to BY4741
-
-
Manually annotated by BRENDA team
Saccharomyces pombe
-
-
-
Manually annotated by BRENDA team
gene plo1, diverse strains and genotypes
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
depletion of PLK1 leads to a delay of cell cycle recovery, and apoptosis
malfunction
-
heterozygosity of Plk4 does not lead to polyploidization and centrosome amplification
malfunction
-
loss of plk-2 inhibits chromosome pairing and licenses synapsis between nonhomologous chromosomes
malfunction
-
partial functional loss leads to chromosome missegregation
physiological function
-
Cdc5 plays multiple roles during the cell cycle, component of the fourteen early anaphase release, FEAR, pathway, degradation of the protein Swe1 is Cdc5 dependent
physiological function
Q5UES2
conserved function in mitotic processes
physiological function
-
conserved function in mitotic processes and cytokinesis
physiological function
-
Plk1 function as a key regulator of mitotic events by phosphorylating substrate proteins of centrosomes, kinetochores, the mitotic spindle, and the midbody
physiological function
-
Plk1 functions in multiple steps of mitosis
physiological function
-
Plk1 is a critical regulator of many stages of mitosis
physiological function
-
Plk1 is a fundamental regulator of mitotic progression
physiological function
-
Plk1 is a key regulator of mitosis
physiological function
-
PLK1 is a key regulator of multiple steps during mitotic progression
physiological function
-
Plk1 is a regulator of interferon induction
physiological function
-
Plk1 is involved in the activation of Cdc2, chromosome segregation, centrosome maturation, bipolar spindle formation and execution of cytokinesis
physiological function
-
PLK1 is the upstream regulator of SYK tyrosine kinase in B-lineage acute lymphoblastic leukemia cells
physiological function
-
PLK1 participates in multiple steps in mitosis
physiological function
-
PLK1 plays a critical role in regulating the cell cycle, PLK inhibition increases gene expression of paramyxovirus
physiological function
-
Plk1 plays an essential role in regulating the many processes involved in mitotic entry and progression
physiological function
-
Plk1 plays several crucial roles in cell cycle progression and cell division
physiological function
-
PLK1 represents the most studied member of this familiy and has known roles throughout mitosis, including mitotic entry, spindle formation, chromosome segregation, and cytokinesis
physiological function
Q00444
PLK4 is a key regulator of centrosome duplication
physiological function
-
Plks are potent regulators of M phase, their roles in mitotic entry, spindle pole functions and cytokinesis are broadly conserved
physiological function
-
promotes adaptation to the DNA damage checkpoint, in addition to its numerous roles in mitotic progression
physiological function
-
responsible for cell cycle progression
physiological function
-
TbPLK regulates cytokinetic initiation
physiological function
-
during meiosis the polo kinases PLK-1 is targeted to the pairing center by ZIM/HIM-8-pairing proteins, during meiosis the polo kinases PLK-2 is targeted to the pairing center by ZIM/HIM-8-pairing proteins. PLK-2 enzyme is required for pairing center-mediated interhomolog interactions and for meiosis-specific phosphorylation of SUN-1 and establishment of dynamic SUN/KASH (SUN-1/ZYG-12) modules that promote homolog pairing
physiological function
-
enzyme Cdc5 is required for spindle integrity during checkpoint bypass, it is not required for meiosis checkpoint activation
physiological function
-
PLK1 plays an important role in DNA damage recovery
physiological function
-
polo-like kinase 4 controls centriole duplication but does not directly regulate cytokinesis
physiological function
-
polo-like kinase 4 plays a key role in initiating centriole duplication. Kinase-mediated, autoregulated instability of Plk4 self-limits Plk4 activity so as to prevent centrosome amplification
physiological function
-
the dynamics of the enzyme at kinetochores control two critical mitotic processes: initially establishing correct kinetochore-microtubule attachments and subsequently silencing the spindle checkpoint
physiological function
-
the enzyme has multiple functions and substrates in mitosis
physiological function
-
the enzyme plays a critical role in cell division
physiological function
-
the enzyme plays a pivotal role in the regulation of cell cycle progression and the orchestration of cell division
physiological function
-
via the formation of the Nedd1-Plk1 complex and subsequent Augmin phosphorylation, Plk1 regulates spindle microtubule-based microtubule nucleation to accomplish normal bipolar spindle formation and mitotic progression
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 20S proteasome
ADP + phosphorylated S20 proteasome
show the reaction diagram
-
phosphorylation by Plk1 enhances the proteolytic activity
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
show the reaction diagram
-
the enzyme creates the 3F3/2 kinase phosphoepitope on mitotic kinetichores, depletion of enzyme in M phase cell extract leads to loss of 3F3/2 kinase activity
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
show the reaction diagram
-
purified recombinant Plk1 or M phase cell extract, phosphoepitope mapping reveals that the 3F3/2 kinase phosphoepitope overlaps the enzyme consensus phosphorylation seqence, overview
-
-
?
ATP + 5FAM-RALMEASFADQAR-NH2
ADP + phosphorylated 5FAM-RALMEASFADQAR-NH2
show the reaction diagram
Q4KMI8
substrate peptide, based on human Cdc25C, used in biochemical activity assay
-
-
?
ATP + 85kDa microtubule-associated protein
ADP + phosphorylated 85kDa microtubule-associated protein
show the reaction diagram
-
protein is released from microtubules after phosphorylation
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
Xenopus laevis, Saccharomyces pombe
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
Q5UES2
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
Q00444
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
Q4FZD7
-
-
-
?
ATP + abnormal spindle pole protein
ADP + phosphorylated abnormal spindle pole protein
show the reaction diagram
-
i.e. abnormal spindle pole protein, activation of abnormal spindle pole protein by phosphorylation
-
-
?
ATP + alpha-casein
ADP + phosphorylated alpha-casein
show the reaction diagram
-
-
-
-
?
ATP + alpha-casein
ADP + phosphorylated alpha-casein
show the reaction diagram
-
-
-
-
?
ATP + alpha-casein
ADP + phosphorylated alpha-casein
show the reaction diagram
-
high activity of wild-type enzyme
-
-
?
ATP + Bcl-xL
ADP + phosphorylated Bcl-xL
show the reaction diagram
-
-
-
-
?
ATP + Bem3
ADP + phosphorylated Bem3
show the reaction diagram
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + beta-casein
ADP + phosphorylated beta-casein
show the reaction diagram
-
-
-
-
?
ATP + beta-tubulin
ADP + phosphorylated beta-tubulin
show the reaction diagram
-
the enzyme is required for beta-tubulin recruitment to the centrosome
-
-
?
ATP + Brd4
ADP + phosphorylated Brd4
show the reaction diagram
-
the E2 binding domain of Brd4 is phosphorylated by Plk1 in vitro
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
show the reaction diagram
-
S676 is an in vivo Plk1 phosphorylation site in BubR1
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
show the reaction diagram
-
BubR1 interacts with Plk1 during prometaphase, binds to the C-terminal, complete polo-box domain of Plk1
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
show the reaction diagram
-
Plk1 is responsible for the hyperphosphorylation of BubR1 during prometaphase
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
show the reaction diagram
-
Plk1-BubR1 interaction is mediated by polo-box domain binding to pT620 of BubR1. S676 is a Plk1-specific phosphorylation site, site is phosphorylated during prometaphase, but dephosphorylated at metaphase upon establishment of tension between sister chromatids. Phosphorylation is not required for spindle checkpoint function but instead is important for the stability of kinetochore-microtubule interactions, timely mitotic progression, and chromosome alignment onto the metaphase plate
-
-
?
ATP + casein
ATP + phosphorylated casein
show the reaction diagram
-
-
-
-
?
ATP + casein
ADP + phosphocasein
show the reaction diagram
P32562
-
-
-
?
ATP + casein
ADP + phosphocasein
show the reaction diagram
-
substrate in biochemical activity assay
-
-
?
ATP + casein
ADP + phosphocasein
show the reaction diagram
Q6DRK7
substrate in biochemical activity assay
-
-
?
ATP + casein
ADP + phosphorylated casein
show the reaction diagram
-
-
-
-
?
ATP + casein
ADP + phosphorylated casein
show the reaction diagram
-
-
-
-
?
ATP + casein
ADP + phosphorylated casein
show the reaction diagram
-
-
-
-
?
ATP + casein
ADP + phosphorylated casein
show the reaction diagram
-
-
-
-
?
ATP + casein
ADP + phosphorylated casein
show the reaction diagram
-
kinase assay
-
-
?
ATP + casein
ADP + a phosphorylated casein
show the reaction diagram
-
activity assay
-
-
?
ATP + Cdc14A
ADP + phosphorylated Cdc14A
show the reaction diagram
-
-
-
-
?
ATP + Cdc25
ADP + phosphorylated Cdc25
show the reaction diagram
-
-
-
-
?
ATP + Cdc25
ADP + phosphorylated Cdc25
show the reaction diagram
-
-
-
-
?
ATP + Cdc25A
ADP + phosphorylated Cdc25A
show the reaction diagram
-
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
show the reaction diagram
-
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
show the reaction diagram
-
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
show the reaction diagram
-
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
show the reaction diagram
-
phosphorylation by Plk1 on Ser198 in a nuclear export signal sequence promoting its nuclear translocation, inhibition of Cdc25 activation resulting in a delay in Cdc2 activation, Plk3 activity in vitro, phosphorylation by Plk1 on Ser198
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
show the reaction diagram
O00444, Q9NYY3
preferentially phosphorylates Ser 198 and 191
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
show the reaction diagram
-
the polo box domain displays a similar affinity for non-phosphorylated and phosphorylated Cdc25C target peptides, full-length Plk1 shows ca. 7fold more affinity for the phosphorylated peptide
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
show the reaction diagram
-
substrate in activity assay
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25
show the reaction diagram
-
-
-
-
?
ATP + Cdh1
ADP + phosphorylated Cdh1
show the reaction diagram
-
-
-
-
?
ATP + centromeric protein PBIP1
ADP + phosphorylated centromeric protein PBIP1
show the reaction diagram
-
Plk1 phosphorylates PBIP1 at T78, GST-PBIPtide is used as in vitro substrate
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
show the reaction diagram
-
-
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
show the reaction diagram
-
phosphorylation at Thr68
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
show the reaction diagram
-
substrate is a protein kinase, phosphorylated by Plk1 at Ser28, Thr68, and Thr26 in vitro
-
-
?
ATP + cJun peptide
ADP + phosphorylated cJun peptide
show the reaction diagram
O00444, Q9NYY3
strong preference of PLK1 versus PLK2 and PLK3
-
-
?
ATP + claspin
ADP + phosphorylated claspin
show the reaction diagram
-
Plx1 is involved in alleviating DNA replication checkpoint response by inactivation of claspin through phosphorylation, checkpoint protein, interaction and phosphorylation at Thr906 and Ser934
-
-
?
ATP + cohesin
ADP + phosphorylated cohesin
show the reaction diagram
-
-
-
-
?
ATP + cohesin
ADP + phosphorylated cohesin
show the reaction diagram
-
phosphorylation by Cdc5 required for removal of cohesin from chromosomes, phosphorylation adjacent to the cleavage site of Scc1 by Cdc5
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
show the reaction diagram
-
-
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
show the reaction diagram
-
-
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
show the reaction diagram
-
phosphorylation at S126, S128, S133, and S147 for nuclear translocation of cyclin B, no phosphorylation of cyclin B1
-
-
?
ATP + cyclin B1
ADP + phosphorylated cyclin B
show the reaction diagram
-
phosphorylation at S101, not at S113 in the cytoplasmic retention sequence
-
-
?
ATP + Ecm25
ADP + phosphorylated Ecm25
show the reaction diagram
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + Ect2
ADP + phosphorylated Ect2
show the reaction diagram
-
-
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
show the reaction diagram
-
CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit, in response to increased free Ca2+ levels CaMKII acts as a priming kinase mediating the interaction between Emi2 and Plx1 polo box domain via phosphorylation at a specific motif, Emi2, i.e. XErp1, is a cytostatic factor, CaMKII specifically directs Plx1 activity toward Emi2 by functioning as a priming kinase, creating a phosphoepitope on Emi2 that recruits the polo box domain of Plx1, allowing subsequent phosphorylation of Emi2s degron and its recognition by SCFbetaTrCP for ubiquitination and destruction
-
-
?
ATP + Fkh2p
ADP + phosphorylated Fkh2p
show the reaction diagram
-
Fkh2p is only poorly phosphorylated by Cdc5p, Fkh2p has a function in nucleating the formation of a Fkh2p-Ndd1p-Cdc5p complex on CLB2 cluster promoters, and the subsequent Cdc5p-dependent phosphorylation of Ndd1p at Ser 85
-
-
?
ATP + gammaBD of IKKbeta
ADP + phosphorylated gammaBD of IKKbeta
show the reaction diagram
-
Plk1 phosphorylates serines 733, 740 and 750 in the IKKgammaNEMO-binding domain, gammaBD, of IKKbeta
-
-
?
ATP + giantin
ADP + phosphorylated giantin
show the reaction diagram
-
-
-
-
?
ATP + Hice1 subunit of Augmin complex
ADP + phosphorylated Hice1 subunit of Augmin complex
show the reaction diagram
-
via the formation of the Nedd1-Plk1 complex and subsequent Augmin phosphorylation, Plk1 regulates spindle microtubule-based microtubule nucleation to accomplish normal bipolar spindle formation and mitotic progression
-
-
?
ATP + histone H1
ADP + phosphorylated histone H1
show the reaction diagram
-
substrate used in kinase assay
-
-
?
ATP + histone H1
ADP + phosphorylated histone H1
show the reaction diagram
-
substrate used in kinase assay
-
-
?
ATP + histone H1 kinase
ADP + phosphorylated histone H1 kinase
show the reaction diagram
-
activation
-
-
?
ATP + HsCdc14A
ADP + phosphorylated HsCdc14A
show the reaction diagram
-
HsCdc14A binds to PLK1 via its C-terminus, phosphorylation partially releases the auto-inhibition of HsCdc14A, PLK1-mediated phospho-regulation promotes HsCdc14A phosphatase activity
-
-
?
ATP + kinesin-like protein 2
ADP + phosphorylated kinesin-like protein 2
show the reaction diagram
-
Plk1, essential for cytokinesis, Plk1
-
-
?
ATP + Mad1
ADP + phosphorylated Mad1
show the reaction diagram
-
the results suggest that Plk1 is influential of Mad1 phosphorylation, Mad1, mitotic arrest deficiency protein 1
-
-
?
ATP + Mad3
ADP + phosphorylated Mad3
show the reaction diagram
-
phosphorylation of Mad3 isozymes at 5 serine residues, S222, S380, S466, S504, and especially at S268, during spindle checkpoint activation, Mad3 is an inhibitor of Cdc20/APC ubiquitin ligase, overview, recombinant HA-tagged wild-type and mutant Mad3 substrate proteins, the activity with mutants in which phorylation site Ser is replaced by Ala is highly reduced, Mad3 is a homologue to the human BubR1 protein
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
show the reaction diagram
-
phosphorylation/polo box binding is required for chromosomal dissociation of MEI-S332
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
show the reaction diagram
-
substrate is a protein essential in meiosis for maintaining cohesion at centromers until sister chromatids separate at the metaphase II/anaphase II transition, phosphorylation by polo kinase removes the protein from centromeres and antagonizes the MEI-S332 function, MEI-S332 phosphorylation by polo kinase is essential for viability of the cells
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
show the reaction diagram
-
enzyme requires residues T331 and possibly in combination with S234 for activity, no activity with MEI-S332 protein mutants T331A and S234A/T331A
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
show the reaction diagram
-
enzyme requires residues T331 and possibly in combination with S234 for activity, no activity with MEI-S332 protein mutants T331A and S234A/T331A in S2 cells
-
-
?
ATP + MEX-5
ADP + phosphorylated MEX-5
show the reaction diagram
-
-
-
-
?
ATP + Mid1p
ADP + phosphorylated Mid1p
show the reaction diagram
-
required for positioning of division sites in cytokinesis
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
show the reaction diagram
-
-
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
show the reaction diagram
-
-
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
show the reaction diagram
-
phosphorylation of Myt1 during M phase, i.e. membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase, no activity with a Myt1 mutant in which the 4 C-terminal phosphorylation sites are mutated to alanine
-
-
?
ATP + Ndd1p
ADP + phosphorylated Ndd1p
show the reaction diagram
-
phosphorylation of Ser 85, phosphorylation is required for the normal temporal expression of cell-cycle-regulated genes such as CLB2 and SWI5 in G2/M phase
-
-
?
ATP + Nud1
ADP + phosphorylated Nud1
show the reaction diagram
-
Cdc5 and Cdc28 activities are required for proper phosphorylation of Nud1
-
-
?
ATP + NudC
ADP + phosphorylated kinesin-like protein 2
show the reaction diagram
-
i.e. nuclear distribution protein C, Plk1 phosphorylates Ser274 and Ser326
-
-
?
ATP + p125
ADP + phosphorylated p125
show the reaction diagram
-
peptide fragment of DNA polymerase delta, phosphorylation at Ser60 by Plk3, peptide fragment of DNA polymerase delta, phosphorylation at Ser60 by Plk3, wild-type and mutant GST-tagged or His6-tagged Plk3
-
-
?
ATP + p53
ADP + phosphorylated p53
show the reaction diagram
-
-
Plk3, Plk1 inhibits tumor suppressor p53 transactivating activity in lung carcinoma cells
-
?
ATP + p53
ADP + phosphorylated p53
show the reaction diagram
-
Plk1 binds tumor suppressor p53, dependent on DNA-binding to the specific DNA binding domain within residues 102-292 of p53, and inhibits its transactivation activity, phosphorylation at Ser20
-
-
?
ATP + p53
ADP + phosphorylated p53
show the reaction diagram
-
Plk3 phosphorylates S20 in vitro, Plk1 inhibits p53 by phosphorylation
-
-
?
ATP + p53
ADP + phosphorylated p53
show the reaction diagram
-
Plk1 apparently phosphorylates other residues than Plk3, Plk3 apparently phosphorylates other residues than Plk1
-
-
?
ATP + Pin1
ADP + phosphorylated Pin1
show the reaction diagram
-
Plk1-mediated phosphorylation at Ser65 stabilizes Pin1 by inhibiting its ubiquitination in cells, recombinant isomerase Pin1 expressed in Escherichia coli, phosphorylation at Ser65, wild-type and truncated mutant Pin1 comprising residues 1-70
-
-
?
ATP + Plk1 polo box 1-derived peptide
ADP + phosphorylated Plk1 polo box 1-derived peptide
show the reaction diagram
-
synthetic substrate
-
-
?
ATP + PLKtide
ADP + phosphorylated PLKtide
show the reaction diagram
O00444, Q9NYY3
substrate corresponds to the consensus sequence for positions -7 to +6 supplemented with residues from Cdc25C for positions -23 to -8. PLK1 displays greatly enhanced activity and a strong preference for the residue corresponding to Ser198 in the optimized substrate
-
-
?
ATP + PLKtide
ADP + phosphorylated PLKtide
show the reaction diagram
O00444, Q9NYY3
substrate corresponds to the consensus sequence for positions -7 to +6 supplemented with residues from Cdc25C for positions -23 to -8. PLK2 displays greatly enhanced activity and a strong preference for the residue corresponding to Ser198 in the optimized substrate
-
-
?
ATP + PLKtide
ADP + phosphorylated PLKtide
show the reaction diagram
O00444, Q9NYY3
substrate corresponds to the consensus sequence for positions -7 to +6 supplemented with residues from Cdc25C for positions -23 to -8. PLK3 displays greatly enhanced activity and a strong preference for the residue corresponding to Ser198 in the optimized substrate
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
Q9H4B4
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
Q6DRK7
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
Q4KMI8
-
-
-
?
ATP + protein MAVS
ADP + phosphorylated protein MAVS
show the reaction diagram
-
phosphorylation of the mitochondria-bound adapter protein MAVS, MAVS, mitochondrial antiviral signaling
-
-
?
ATP + protein p110
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + Rom2
ADP + phosphorylated Rom2
show the reaction diagram
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + Sac7
ADP + phosphorylated Sac7
show the reaction diagram
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + SCC1 cohesin
ADP + phosphorylated SCC1 cohesin
show the reaction diagram
-
-
-
-
?
ATP + Slk19
ADP + phosphorylated Slk19
show the reaction diagram
-
Cdc5 and Cdc28 activities are required for proper phosphorylation of Slk19
-
-
?
ATP + Stu2
ADP + phosphorylated Stu2
show the reaction diagram
-
Cdc5 and Cdc28 activities are required for proper phosphorylation of Stu2
-
-
?
ATP + SYK tyrosine kinase
ADP + phosphorylated SYK tyrosine kinase
show the reaction diagram
-
-
-
-
?
ATP + TbCentrin2
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + TPSDSLIYDDGLS
ADP + phosphorylated TPSDSLIYDDGLS
show the reaction diagram
O00444, Q9NYY3
-
-
-
?
ATP + TRF1
ADP + phosphorylated TRF1
show the reaction diagram
-
the cell-cycle-dependent TRF1 recruitment to telomere chromatin is regulated by the enzyme, TRF1 binds the telomere via the telomeric repeats, process overview, endogenous TRF1 associated to telomeres during mitosis, phosphorylation by Plx1 in vitro
-
-
?
ATP + TRF1
ADP + phosphorylated TRF1
show the reaction diagram
-
is phosphorylated by Plx1 upon transition from interphase to M phase, and is recruited to mitotic telomere chromatin
-
-
?
ATP + Tus1
ADP + phosphorylated Tus1
show the reaction diagram
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + viral phosphoprotein P
ADP + phosphorylated viral phosphoprotein P
show the reaction diagram
-
PLK1 directly phosphorylates viral phosphoprotein P of paramyxovirus in vitro
-
-
?
ATP + Wee1
ADP + phosphorylated Wee1
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
no phosphorylation of histone H1
-
-
-
additional information
?
-
-
the enzyme may be involved in the early signaling events required for growth factor-stimulated cell cycle progression
-
-
-
additional information
?
-
-
playing an important role in regulating the onset and/or progression of mitosis in mammalian cells
-
-
-
additional information
?
-
-
the enzyme is involved in regulating M phase functions during the cell cycle. Prk's role in mitosis is at least partly mediated through direct regulation of Cdc25C
-
-
-
additional information
?
-
-
expression appears to be down-regulated in lung carcinomas
-
-
-
additional information
?
-
Q60806
has two functions, one during the entry of cells into the cell cycle and a second during mitosis of cycling cells
-
-
-
additional information
?
-
P34331
required for nuclear envelope breakdown and the completion of meiosis
-
-
-
additional information
?
-
P32562
required for the initiation of chromosomal DNA replication in Saccharomyces cerevisiae and interaction with the CDC7 protein kinase
-
-
-
additional information
?
-
-
normal bipolar spindles with polyploid complements of chromosomes, bipolar spindles in which one pole can be unusually broad, and monopolar spindles
-
-
-
additional information
?
-
Q9R012
the enzyme is regulated dynamically with synaptic plasticity
-
-
-
additional information
?
-
-
mutation in polo leads to a variety of abnormal mitoses in Drosophila larval neuroblasts. These include otherwise normal looking mitotic spindles upon which chromosomes appear overcondensed
-
-
-
additional information
?
-
P53350
expression of PLK mRNA appeared to be strongly correlated with the mitotic activity of cells
-
-
-
additional information
?
-
-
cell cycle- and terminal differentiation-associated regulation
-
-
-
additional information
?
-
Q64702
enzyme is involved in cell proliferation, expression is associated with mitotic and meiotic cell division
-
-
-
additional information
?
-
-
Plk1 is likely to function in cell cycle progression
-
-
-
additional information
?
-
-
the enzyme is required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells
-
-
-
additional information
?
-
-
Cdc5 plays a role in chromosomes segregation during meiosis I, it is required for phosphorylation and removal of cohesin from chromosomes, it is required for sister-kinetochore orientation with associated Mam1 protein, mechanism, overview
-
-
-
additional information
?
-
-
Chk2 phosphorylation at Thr68 is enhanced by overexpression of Plk1 in vivo
-
-
-
additional information
?
-
-
cytokinetic actomyosin ring formation and septation in fission yeast are dependent on the full recruitment of the polo-like kinase PLO1 to the spindle pole body, regulated by Mad2, and a functional spindle assembly checkpoint which requires an intact microtubule cytoskeleton, overview
-
-
-
additional information
?
-
-
physical and functional interactions between polo kinase and the spindle pole component Cut12 regulate mitotic commitment by feedback control of the MPF complex, overview
-
-
-
additional information
?
-
-
Plk1 depletion induces apoptosis in cancer cells and stabilizes p53 tumor-suppressor protein
-
-
-
additional information
?
-
-
Plk1 inhibits Wee1 inactivation resulting in a delay in Cdc2 activation, the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, modeling of major Plk metabolism pathways, spindle checkpoint machinery, overview
-
-
-
additional information
?
-
-
Plk1 is important in activation and regulation of spindle assembly during mitosis
-
-
-
additional information
?
-
-
Plk1 is involved in regulating centrosome maturation, mitotic entry, sister chromatid cohesion, the anaphase-promoting complex/cyclosome, and cytokinesis, as well as in chromosome orientation, detailed overview of physiological functions of the enzyme
-
-
-
additional information
?
-
-
Plk1 is involved in the regulation of M-phase of the cell cycle and might also be involved in tumorigenesis
-
-
-
additional information
?
-
-
Plk3 is involved in regulating Golgi fragmentation during the cell cycle
-
-
-
additional information
?
-
-
polo kinase Cdc5 is involved as part of the FEAR network, i.e. fourteen early anaphase release network, and of MEN network, i.e. mitotic exit network, in controlling protein phosphatase Cdc14 localization and activity, the enzyme induces phosphorylation of Cdc14 and Cfi1/Net1 by activating the networks, overview
-
-
-
additional information
?
-
-
polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores
-
-
-
additional information
?
-
-
polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores, the enzym is required for association of Cdc20 to kinetochores
-
-
-
additional information
?
-
-
the enzyme is a mitotic kinase and is required for centrosome maturation at mitotic M-phase entry in order to recruit the gamma-tubulin ring complex and activate abnormal spindle pole protein, Asp, the enzyme is involved in mitotic networks and cytokinesis, e.g. in spermatogenesis, overview, functional modeling of polo kinase in mitotic phases
-
-
-
additional information
?
-
-
the enzyme is essential for Ca2+-induced meiotic exit of fertilized eggs after arrest in metaphase II before fertilization
-
-
-
additional information
?
-
-
the enzyme is involved in regulation of centriole duplication cycle by protein phosphorylation
-
-
-
additional information
?
-
-
the enzyme is involved in regulation of cytokinesis and microtubule polymerization modulation during oocyte meiotic maturation, fertilization and early embryonic mitosis
-
-
-
additional information
?
-
Q62673
the enzyme is involved in regulation of cytokinesis and microtubule polymerization modulation during oocyte meiotic maturation, fertilization and early embryonic mitosis
-
-
-
additional information
?
-
-
the enzyme is involved in regulation of Nek2-induced centrosome separation after DNA damage
-
-
-
additional information
?
-
-
the enzyme is involved in spindle formation and septation playing an important role in cell cycle regulation
-
-
-
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, Cdc5 is part of mitotic networks, e.g. the fourteen early anaphase release network FEAR for Cdc14 release, overview
-
-
-
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, mechanism
-
-
-
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, Plo1 is involved in cytokinesis
-
-
-
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, regulation of cytokinesis, overview
-
-
-
additional information
?
-
-
the enzyme plays an essential role in promoting mitosis and cytokinesis, the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain, structure analysis
-
-
-
additional information
?
-
-
the enzyme recruitment to the spindle pole body influences the balance between Cdc25 and Wee1 activities on mitosis-promoting factor, MPF
-
-
-
additional information
?
-
-
the polo-loke kinase activates cyclase-dependent hyphal-like growth acting like a switch between yeast and hyphal growth forms, mechanism, overview
-
-
-
additional information
?
-
-
determination of enzyme consensus sequence
-
-
-
additional information
?
-
-
Plk1 interacts with the 20S and the 26S proteasomes, Plk3 interacts with DNA polymerase delta and Plk1 with the Golgi specific protein GRASP65
-
-
-
additional information
?
-
-
the enzyme interacts with diverse proteins via its poloboxes, overview
-
-
-
additional information
?
-
-
the enzyme interacts with DNA polymerase delta
-
-
-
additional information
?
-
-
the protein phosphatase 1 is no substrate of Plk1
-
-
-
additional information
?
-
O00444, Q9NYY3
consensus substrate sequences for PLK2
-
-
-
additional information
?
-
O00444, Q9NYY3
consensus substrate sequences for PLK3
-
-
-
additional information
?
-
O00444, Q9NYY3
consensus substrate sequences for PLK4
-
-
-
additional information
?
-
O00444, Q9NYY3
expanded consensus substrate sequence for PLK1
-
-
-
additional information
?
-
-
no activity against myelin basic protein or histone H1
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 20S proteasome
ADP + phosphorylated S20 proteasome
show the reaction diagram
-
phosphorylation by Plk1 enhances the proteolytic activity
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
show the reaction diagram
-
the enzyme creates the 3F3/2 kinase phosphoepitope on mitotic kinetichores, depletion of enzyme in M phase cell extract leads to loss of 3F3/2 kinase activity
-
-
?
ATP + 85kDa microtubule-associated protein
ADP + phosphorylated 85kDa microtubule-associated protein
show the reaction diagram
-
protein is released from microtubules after phosphorylation
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
Xenopus laevis, Saccharomyces pombe
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
Q5UES2
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
Q00444
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
Q4FZD7
-
-
-
?
ATP + abnormal spindle pole protein
ADP + phosphorylated abnormal spindle pole protein
show the reaction diagram
-
i.e. abnormal spindle pole protein, activation of abnormal spindle pole protein by phosphorylation
-
-
?
ATP + beta-tubulin
ADP + phosphorylated beta-tubulin
show the reaction diagram
-
the enzyme is required for beta-tubulin recruitment to the centrosome
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
show the reaction diagram
-
S676 is an in vivo Plk1 phosphorylation site in BubR1
-
-
?
ATP + casein
ADP + phosphorylated casein
show the reaction diagram
-
kinase assay
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
show the reaction diagram
-
phosphorylation by Plk1 on Ser198 in a nuclear export signal sequence promoting its nuclear translocation, inhibition of Cdc25 activation resulting in a delay in Cdc2 activation
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
show the reaction diagram
-
-
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
show the reaction diagram
-
phosphorylation at Thr68
-
-
?
ATP + claspin
ADP + phosphorylated claspin
show the reaction diagram
-
Plx1 is involved in alleviating DNA replication checkpoint response by inactivation of claspin through phosphorylation
-
-
?
ATP + cohesin
ADP + phosphorylated cohesin
show the reaction diagram
-
phosphorylation by Cdc5 required for removal of cohesin from chromosomes
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
show the reaction diagram
-
phosphorylation at S126, S128, S133, and S147 for nuclear translocation of cyclin B
-
-
?
ATP + cyclin B1
ADP + phosphorylated cyclin B
show the reaction diagram
-
phosphorylation at S101, not at S113 in the cytoplasmic retention sequence
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
show the reaction diagram
-
CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit, in response to increased free Ca2+ levels CaMKII acts as a priming kinase mediating the interaction between Emi2 and Plx1 polo box domain via phosphorylation at a specific motif
-
-
?
ATP + giantin
ADP + phosphorylated giantin
show the reaction diagram
-
-
-
-
?
ATP + Hice1 subunit of Augmin complex
ADP + phosphorylated Hice1 subunit of Augmin complex
show the reaction diagram
-
via the formation of the Nedd1-Plk1 complex and subsequent Augmin phosphorylation, Plk1 regulates spindle microtubule-based microtubule nucleation to accomplish normal bipolar spindle formation and mitotic progression
-
-
?
ATP + kinesin-like protein 2
ADP + phosphorylated kinesin-like protein 2
show the reaction diagram
-
Plk1, essential for cytokinesis
-
-
?
ATP + Mad3
ADP + phosphorylated Mad3
show the reaction diagram
-
phosphorylation of Mad3 isozymes at 5 serine residues, S222, S380, S466, S504, and especially at S268, during spindle checkpoint activation, Mad3 is an inhibitor of Cdc20/APC ubiquitin ligase, overview
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
show the reaction diagram
-
phosphorylation/polo box binding is required for chromosomal dissociation of MEI-S332
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
show the reaction diagram
-
substrate is a protein essential in meiosis for maintaining cohesion at centromers until sister chromatids separate at the metaphase II/anaphase II transition, phosphorylation by polo kinase removes the protein from centromeres and antagonizes the MEI-S332 function, MEI-S332 phosphorylation by polo kinase is essential for viability of the cells
-
-
?
ATP + Mid1p
ADP + phosphorylated Mid1p
show the reaction diagram
-
required for positioning of division sites in cytokinesis
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
show the reaction diagram
-
phosphorylation of Myt1 during M phase
-
-
?
ATP + NudC
ADP + phosphorylated kinesin-like protein 2
show the reaction diagram
-
i.e. nuclear distribution protein C, Plk1 phosphorylates Ser274 and Ser326
-
-
?
ATP + p125
ADP + phosphorylated p125
show the reaction diagram
-
peptide fragment of DNA polymerase delta, phosphorylation at Ser60 by Plk3
-
-
?
ATP + p53
ADP + phosphorylated p53
show the reaction diagram
-
-
Plk3, Plk1 inhibits tumor suppressor p53 transactivating activity in lung carcinoma cells
-
?
ATP + p53
ADP + phosphorylated p53
show the reaction diagram
-
Plk1 binds tumor suppressor p53, dependent on DNA-binding to the specific DNA binding domain within residues 102-292 of p53, and inhibits its transactivation activity
-
-
?
ATP + Pin1
ADP + phosphorylated Pin1
show the reaction diagram
-
Plk1-mediated phosphorylation at Ser65 stabilizes Pin1 by inhibiting its ubiquitination in cells
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
Q9H4B4
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
Q6DRK7
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
Q4KMI8
-
-
-
?
ATP + Rom2
ADP + phosphorylated Rom2
show the reaction diagram
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + TRF1
ADP + phosphorylated TRF1
show the reaction diagram
-
the cell-cycle-dependent TRF1 recruitment to telomere chromatin is regulated by the enzyme, TRF1 binds the telomere via the telomeric repeats, process overview
-
-
?
ATP + Tus1
ADP + phosphorylated Tus1
show the reaction diagram
-
bound by the polo-box domain of Cdc5
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
the enzyme may be involved in the early signaling events required for growth factor-stimulated cell cycle progression
-
-
-
additional information
?
-
-
playing an important role in regulating the onset and/or progression of mitosis in mammalian cells
-
-
-
additional information
?
-
-
the enzyme is involved in regulating M phase functions during the cell cycle. Prk's role in mitosis is at least partly mediated through direct regulation of Cdc25C
-
-
-
additional information
?
-
-
expression appears to be down-regulated in lung carcinomas
-
-
-
additional information
?
-
Q60806
has two functions, one during the entry of cells into the cell cycle and a second during mitosis of cycling cells
-
-
-
additional information
?
-
P34331
required for nuclear envelope breakdown and the completion of meiosis
-
-
-
additional information
?
-
P32562
required for the initiation of chromosomal DNA replication in Saccharomyces cerevisiae and interaction with the CDC7 protein kinase
-
-
-
additional information
?
-
-
normal bipolar spindles with polyploid complements of chromosomes, bipolar spindles in which one pole can be unusually broad, and monopolar spindles
-
-
-
additional information
?
-
Q9R012
the enzyme is regulated dynamically with synaptic plasticity
-
-
-
additional information
?
-
-
mutation in polo leads to a variety of abnormal mitoses in Drosophila larval neuroblasts. These include otherwise normal looking mitotic spindles upon which chromosomes appear overcondensed
-
-
-
additional information
?
-
P53350
expression of PLK mRNA appeared to be strongly correlated with the mitotic activity of cells
-
-
-
additional information
?
-
-
cell cycle- and terminal differentiation-associated regulation
-
-
-
additional information
?
-
Q64702
enzyme is involved in cell proliferation, expression is associated with mitotic and meiotic cell division
-
-
-
additional information
?
-
-
Plk1 is likely to function in cell cycle progression
-
-
-
additional information
?
-
-
the enzyme is required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells
-
-
-
additional information
?
-
-
Cdc5 plays a role in chromosomes segregation during meiosis I, it is required for phosphorylation and removal of cohesin from chromosomes, it is required for sister-kinetochore orientation with associated Mam1 protein, mechanism, overview
-
-
-
additional information
?
-
-
Chk2 phosphorylation at Thr68 is enhanced by overexpression of Plk1 in vivo
-
-
-
additional information
?
-
-
cytokinetic actomyosin ring formation and septation in fission yeast are dependent on the full recruitment of the polo-like kinase PLO1 to the spindle pole body, regulated by Mad2, and a functional spindle assembly checkpoint which requires an intact microtubule cytoskeleton, overview
-
-
-
additional information
?
-
-
physical and functional interactions between polo kinase and the spindle pole component Cut12 regulate mitotic commitment by feedback control of the MPF complex, overview
-
-
-
additional information
?
-
-
Plk1 depletion induces apoptosis in cancer cells and stabilizes p53 tumor-suppressor protein
-
-
-
additional information
?
-
-
Plk1 inhibits Wee1 inactivation resulting in a delay in Cdc2 activation, the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, modeling of major Plk metabolism pathways, spindle checkpoint machinery, overview
-
-
-
additional information
?
-
-
Plk1 is important in activation and regulation of spindle assembly during mitosis
-
-
-
additional information
?
-
-
Plk1 is involved in regulating centrosome maturation, mitotic entry, sister chromatid cohesion, the anaphase-promoting complex/cyclosome, and cytokinesis, as well as in chromosome orientation, detailed overview of physiological functions of the enzyme
-
-
-
additional information
?
-
-
Plk1 is involved in the regulation of M-phase of the cell cycle and might also be involved in tumorigenesis
-
-
-
additional information
?
-
-
Plk3 is involved in regulating Golgi fragmentation during the cell cycle
-
-
-
additional information
?
-
-
polo kinase Cdc5 is involved as part of the FEAR network, i.e. fourteen early anaphase release network, and of MEN network, i.e. mitotic exit network, in controlling protein phosphatase Cdc14 localization and activity, the enzyme induces phosphorylation of Cdc14 and Cfi1/Net1 by activating the networks, overview
-
-
-
additional information
?
-
-
polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores
-
-
-
additional information
?
-
-
polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores, the enzym is required for association of Cdc20 to kinetochores
-
-
-
additional information
?
-
-
the enzyme is a mitotic kinase and is required for centrosome maturation at mitotic M-phase entry in order to recruit the gamma-tubulin ring complex and activate abnormal spindle pole protein, Asp, the enzyme is involved in mitotic networks and cytokinesis, e.g. in spermatogenesis, overview, functional modeling of polo kinase in mitotic phases
-
-
-
additional information
?
-
-
the enzyme is essential for Ca2+-induced meiotic exit of fertilized eggs after arrest in metaphase II before fertilization
-
-
-
additional information
?
-
-
the enzyme is involved in regulation of centriole duplication cycle by protein phosphorylation
-
-
-
additional information
?
-
-
the enzyme is involved in regulation of cytokinesis and microtubule polymerization modulation during oocyte meiotic maturation, fertilization and early embryonic mitosis
-
-
-
additional information
?
-
Q62673
the enzyme is involved in regulation of cytokinesis and microtubule polymerization modulation during oocyte meiotic maturation, fertilization and early embryonic mitosis
-
-
-
additional information
?
-
-
the enzyme is involved in regulation of Nek2-induced centrosome separation after DNA damage
-
-
-
additional information
?
-
-
the enzyme is involved in spindle formation and septation playing an important role in cell cycle regulation
-
-
-
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, Cdc5 is part of mitotic networks, e.g. the fourteen early anaphase release network FEAR for Cdc14 release, overview
-
-
-
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, mechanism
-
-
-
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, Plo1 is involved in cytokinesis
-
-
-
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, regulation of cytokinesis, overview
-
-
-
additional information
?
-
-
the enzyme plays an essential role in promoting mitosis and cytokinesis, the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain, structure analysis
-
-
-
additional information
?
-
-
the enzyme recruitment to the spindle pole body influences the balance between Cdc25 and Wee1 activities on mitosis-promoting factor, MPF
-
-
-
additional information
?
-
-
the polo-loke kinase activates cyclase-dependent hyphal-like growth acting like a switch between yeast and hyphal growth forms, mechanism, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
Emi2 only associates with Plx1 after Ca2+ addition, Ca2+-induced Emi2-Plx1 association in cytostatic factor extract relies mostly on the 192RSST motif, whereas the 333RLST motif contributes only slightly to Plx1 binding
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3-[5-methyl-2-[(3,4,5-trimethoxyphenyl)amino]imidazo[5,1-f][1,2,4]triazin-7-yl]phenyl)(phenyl)methanone
-
-
(7R)-2-[5-(2,4-difluorophenyl)-1H-pyrazol-4-yl]-7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
-
; good selectivity over Plk-1 (193-fold), good permeability and moderate microsomal stability. When dosed orally in rats, the inhibitor demonstrates a 41-45% reduction of pS129-a-synuclein levels in the cerebral cortex
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-5-yl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(oxetan-3-yl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(pyrimidin-5-yl)-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3R)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-5-methyl-8-(1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-5-methyl-8-(tetrahydro-2H-pyran-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-7-ethyl-5-methyl-8-(tetrahydrofuran-3-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
;
(7R)-8-(3,3-difluorocyclobutyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
;
(R)-4-[(8-cyclopentyl-7-ethyl-5,6,7,8-tetrahydro-5-methyl-6-oxo-2-pteridinyl)amino]-3-methoxy-N-(1-methyl-4-piperidinyl)benzamide
-
i.e. BI2536
-
1-(1-methylpiperidin-4-yl)-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-(2-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(2-hydroxyethyl)-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
-
-
1-(2-hydroxyethyl)-5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
-
-
1-(2-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(3,5-dichlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(3,5-dimethylphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(3-bromo-5-chlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(3-chlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(3-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(3-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(4-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(4-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-(5-methyl-2-trifluoro-methyl-furan-3-yl)-3-(5-[2-[6-(1H-[1,2,4]triazol-3-ylamino)-pyrimidin-4-ylamino]-ethyl]-thiazol-2-yl)urea
Q4KMI8
-
1-cyclohexyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
-
high levels of selectivity on a panel of unrelated kinases, as well as against PLK2 and PLK3 isoforms, acceptable oral bioavailability in mice making this inhibitor a suitable candidate for further in vivo activity studies
1-methyl-5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
-
high levels of selectivity on a panel of unrelated kinases, as well as against PLK2 and PLK3 isoforms, acceptable oral bioavailability in mice making this inhibitor a suitable candidate for further in vivo activity studies
1-methyl-5-(2-[[5-(piperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
-
-
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid
-
-
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[(2-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[(2-sulfamoylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-8-[(3-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-8-[(4-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[2-(phenylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-8-[[2-(phenylcarbonyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-8-[[2-(phenylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-8-[[3-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-methyl-8-[[4-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-methyl-N-phenyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
1-phenyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
1-[3-(3-aminopropyl)phenyl]-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-[3-(dimethylamino)phenyl]-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
2'-(2-hydroxyethoxy)-5'-methyl-(1,1':3',1-terphenyl)-4,4''-dinitrile
-
0.3 mM, 11% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
-
2'-(2-hydroxyethoxy)-5'-methyl-(1,1':3':1''-terphenyl)-4''-(1H-tetrazol-5-yl)-4-nitrile
-
0.3 mM, 66% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
-
2'-(2-hydroxyethoxy)-5'-methyl-[1,1':3',1''-terphenyl]-3,3'',5,5''-tetrafluoro-4,4''-diol
-
0.3 mM, 61% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
-
2'-(2-hydroxyethoxy)-5'-methyl-[1,1':3',1''-terphenyl]-4,4''-diacetic acid
-
0.3 mM, 53% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
-
2'-(2-hydroxyethoxy)-5'-methyl-[1,1':3',1''-terphenyl]-4,4''-dicarboxylic acid
-
0.3 mM, 14% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
-
2'-(2-hydroxyethoxy)-5'-methyl-[1,1':3',1''-terphenyl]-4,4''-dipropionic acid
-
0.3 mM, 26% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
-
2'-hydroxy-5'-methyl-[1,1':3',1''-terphenyl]-4,4''-dicarboxylic acid
-
0.3 mM, 36% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
-
2'-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5'-methyl-8'-(propan-2-yl)-5',8'-dihydro-6'H-spiro[cyclobutane-1,7'-pteridin]-6'-one
-
;
2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-(2,2,2-trifluoroethyl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
-
-
2-cyano-3-hydroxy-3-methyl-N-[4-(trifluoromethoxy)phenyl]-propenamide
-
LFM-A12
-
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7,7-trimethyl-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
-
;
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7-(2,2,2-trifluoroethyl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
;
2-[5'-methyl-4,4''-ditetrazol-5-yl-(1,1':3',1''-terphenyl)-2'-oxy]ethanol
-
0.3 mM, 47% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
-
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
;
3-(1-[2-chloro-4-[(3-hydroxypyrrolidin-1-yl)methyl]phenyl]ethoxy)-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-(2-methylcyclohexyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
3-(3,4-dimethoxyphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
3-(3,4-dimethylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
3-(3-chlorophenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)benzonitrile
-
-
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
; >0.01
3-(4-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
3-(4-methylthiophen-3-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
3-benzyl-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
>0.020
3-methyl-1-(2-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-(3-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-(4-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-phenyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-[3-(1-methylethyl)phenyl]-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-[3-(methylsulfonyl)phenyl]-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-phenyl-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
3-[(1R)-1-(2-chloro-4-[[(1-methylethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chloro-4-[[(2-hydroxy-1,1-dimethylethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chloro-4-[[(2-hydroxyethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chloro-4-[[(3-hydroxypropyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-(hydroxymethyl)imidazo[1,2-a]pyridin-3-yl]thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
3-[(1R)-1-[2-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(1,1-dioxidothiomorpholin-4-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(3-oxopiperazin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(4-fluoropiperidin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(4-hydroxypiperidin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(4-methylpiperazin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(cyclopentylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(cyclopropylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(dimethylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(ethylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(methylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-(difluoromethoxy)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
tested in rat xenograft model
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-(difluoromethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-chlorophenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-cyclopropylphenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-fluorophenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-methylphenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
3-[(2-chlorobenzyl)oxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[1-(2-chlorophenyl)ethoxy]-5-[7-(hydroxymethyl)imidazo[1,2-a]pyridin-3-yl]thiophene-2-carboxamide
-
-
3-[1-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)piperidin-3-yl]propanamide
Q9H4B4
-
3-[1-[2-chloro-5-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide
-
-
3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanoic acid
-
-
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propan-1-ol
Q9H4B4
-
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
Q9H4B4
;
4-((R)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydro-pteridin-2-ylamino)-3-methoxy-N-(1-methyl-piperidin-4-yl)-benzamide
-
BI 2536
-
4-amino-5-fluoro-3-[6-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl]quinolin-2-ol
-
selectivity profile of PLK2/4 over PLK1/3
4-[(5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-yl)amino]benzenesulfonamide
-
-
4-[7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-6-oxo-6,7-dihydropteridin-8(5H)-yl]benzonitrile
-
;
5-(1-methyl-1H-imidazol-5-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-(1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-(2-amino-1,3-thiazol-5-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-pyrrole-3-carboxamide
-
-
5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-[2-(tetrahydro-2H-pyran-4-yloxy)ethyl]-1H-pyrrole-3-carboxamide
-
-
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
-
-
-
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[2-(trifluoromethyl)-benzyl]oxythiophene-2-carboxamide
-
GW843682X
-
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)-benzyl]oxy]}thiophene-2-carboxamide
-
i.e. GW843682X, inhibition of PLK1 activity abrogates mitotic activation of AMP-activated protein kinasealpha through direct or indirect mechanisms
-
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-(5,6-dimethoxy-1H-benzimidazole-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
-
GW843682X
-
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
5-imidazo[1,2-a]pyridin-3-yl-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-methyl-7-(2-nitrophenyl)-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-7-(3-phenoxyphenyl)-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-7-phenyl-N-(2-pyridin-4-ylethyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
5-methyl-7-phenyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-7-phenyl-N-[3-(trifluoromethyl)phenyl]imidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
5-methyl-7-[3-(trifluoromethyl)phenyl]-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-7-[4-(trifluoromethyl)phenyl]-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-N,7-diphenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-N-(3-morpholin-4-ylpropyl)-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
5-methyl-N-(4-nitrophenyl)-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-pyrazolo[1,5-a]pyridin-3-yl-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-[2-(phenylamino)-1,3-thiazol-5-yl]-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-[2-[(phenylcarbonyl)amino]-1,3-thiazol-5-yl]-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
7-(2-bromophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
7-(2-methoxyphenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
7-(3-bromophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
7-(4-fluorophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7-dimethyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
;
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
-
;
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
;
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(pyridin-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
;
7-ethyl-5-methyl-8-phenyl-2-(2-phenyl-1H-imidazol-1-yl)-7,8-dihydropteridin-6(5H)-one
-
;
7-ethyl-8-(4-fluorophenyl)-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
;
8-(3,3-difluorocyclopentyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
;
8-(biphenyl-2-ylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-(phenylamino)-1-(2,2,2-trifluoroethyl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-(phenylamino)-1-(propan-2-yl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-(phenylamino)-1-[2-(piperidin-1-yl)ethyl]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(2-benzylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-[(2-carbamoylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[(3-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-[(3-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-[(4-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-[(4-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
-
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[[2-acetyl-3-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[[2-acetyl-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
AG-013736
-
selective inhibition of PLK4 relative to PLK1-3
AMPPNP
-
-
ataxia-telangiectasia mutant
-
i.e. ATM, inhibits p53 phosphorylation by Plk1 in vivo
-
BAY 439006
-
selective inhibition of PLK4 relative to PLK1-3
BI 2536
-
; time-dependent inhibition; time-dependent inhibition; time-dependent inhibition of PLK1
BI 2536
-
; potent and selective inhibitor of Plk1, delays prophase and entrance into prometaphase, initiates cyclin A destruction without degrading Emi1, leads to spindle-assembly-checkpoint-induced prometaphase arrest, prevents Plk1s enrichment at kinetochores and centrosomes, in metaphase cells induces detachment of microtubules from kinetochores and leads to spindle collapse, the inhibitor may serve as a powerful tool in mitosis research
BI 2536
-
remarkable potency and selectivity towards Plk1, HeLa cells treated with BI 2536 are first delayed in prophase, after reluctantly entering mitosis, cells become blocked in prometaphase with aberrant monopolar spindles that fail to attach stably to chromosomes
BI 2536
-
-
BI 2536
-
-
BI-2536
-
potential anti-cancer therapeutic agent, shows strong selectivity for Plk1
BI-2536
-
; blocks contractile ring assembly by preventing the localization of Rho and Rho-GEF without affecting the assembly of the central spindle
BI2536
Q5UES2
-
BI6727
-
-
-
BTO-1
-
-
BTO-1
-
; blocks contractile ring assembly by preventing the localization of Rho and Rho-GEF without affecting the assembly of the central spindle
CHIR-258
-
; selectivity profile of PLK2/4 over PLK1/3; selectivity profile of PLK2/4 over PLK1/3
CP 547632
-
selective inhibition of PLK4 relative to PLK1-3
cyclapolin 1
-
-
cyclic (-CH2-CO-Pro-Leu-His-Ser-pThr-Cys-S-)
-
-
cyclic [-CH2-CO-N[2-(1H-indol-3-yl)ethyl]-CH2-CO-Leu-His-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
-
cyclic [-CH2-CO-N[3-[[2-(1H-indol-3-yl)ethyl]amino]-3-oxopropyl]-CH2-CO-Leu-His-Ser-p-Thr-NH-CH[CONH2]-CH2-S-]
-
-
cyclic [-CH2-CO-N[6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl]-CH2-CO-Leu-His-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
-
cyclic [-CH2-CO-N[6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl]-CH2-CO-Leu-His[N3-(8-phenyloctyl)]-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
-
DAP81
-
-
ethyl 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylate
-
-
genistein
-
decreases Plk1 expression
GO 6976
-
; loses PLK1 activity by at least an order of magnitude, relative to staurosporine; loses PLK2 activity by at least an order of magnitude, relative to staurosporine; loses PLK3 activity by at least an order of magnitude, relative to staurosporine
GSK 461364
-
-
GSK461364
-
-
GSK461364A
-
ATP-competitive inhibitor
GSK461364A
-
-
GW843682
-
-
-
GW843682X
-
-
GW843682X
Q5UES2
-
H-1152
-
selective inhibition of PLK4 relative to PLK1-3
HMN-214
-
-
-
imatinib
-
selective inhibition of PLK4 relative to PLK1-3
indirubin
-
decreases Plk1 expression
LY294002
-
selective inhibition of PLK4 relative to PLK1-3
LY294002
-
-
LY294002
Q5UES2
-
Map205
-
Map205 can stabilize Polo and inhibit its cellular activity in vivo
-
matrimony
-
the matrimony protein acts as a negative regulator of polo during the later stages of G2 arrest during meiosis
-
morin
-
-
morin
-
enzymatic inhibitor
N,1-dimethyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-(2-hydroxyethyl)-3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide
-
-
N-(3,4-dimethoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
N-(3-methoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
N-(4-methoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
N-benzyl-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
N-cyclohexyl-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
N-cyclopentyl-1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-cyclopropyl-1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
N-[(1S)-1-phenylethyl]-3-thiophen-2-ylisoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
N-[2-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]-2-phenylacetamide
-
-
N-[4-[(6-chloropyridin-3-yl)methoxy]-3-methoxybenzyl]-2-(3,4-dimethoxyphenyl)ethanamine
-
SBE13
N-[4-[2-(dimethylamino)ethoxy]phenyl]-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
ON-01910
-
-
-
ON01910.Na
-
-
-
ONO1910
-
; does not significantly impacting Plk3 activity in vitro; inhibits Plk1 activity without significantly impacting Plk3 activity in vitro
PHA-680626
-
; selective against Plk1
Purpurogallin
-
polo box inhibitor
quercetin
-
-
quercetin
-
enzymatic inhibitor
RNA
-
RNA interference abrogates centrosome maturation, spindle bipolarization, and silencing of the spindle assembly checkpoint
RNA
-
downregulates PLK, in procyclic forms inhibition of kinetoplast division, in bloodstream form also delayed kinetoplast division, which is further observed to inhibit furrow ingression during cytokinesis
RNAi
-
induces Plk3 depletion, which causes a large fraction of cells to become quiescent, Plk3-depleted cells appear to pass through mitosis normally and complete cell division, but failed to reenter the cell cycle
-
RNAi
-
down-regulation of Plk1 protein level by ca. 90%, abolishes the mobility-shifted, hyperphosphorylated form of BubR1 in the prometaphase-arrested cells
-
RNAi
-
specific down-regulation of Plk1
-
SBE13
-
selective type II Plk1 inhibitor
-
SBE13
-
-
-
scytonemin
-
; strongest inhibitory effect against Plk1 expression in mouse one-cell stage embryos, cleavage rate decreases and phosphorylation level of Tyr15 of Cdc2 increases
scytonemin
-
enzymatic inhibitor
shRNA
-
inhibits G2/M transition, cleavage rate decreases and phosphorylation level of Tyr15 of Cdc2 increases
-
shRNA
-
-
-
silibinin
-
decreases Plk1 expression
siRNA
-
depletion of Plk1, which leads to loss of BubR1 hyperphosphorylation, but has no significant effects on BubR1 localization
-
siRNA
-
; reduces serine phosphorylation of HsCdc14A but not HsCdc14 protein level
-
siRNA
-
-
-
staurosporine
-
specific for PLK4
staurosporine
-
enzymatic inhibitor
SU11248
-
selective inhibition of PLK4 relative to PLK1-3
tert-butyl 1-methyl-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-4-oxo-1,4,6,7-tetrahydro-5H-pyrrolo[3,2-c]pyridine-5-carboxylate
-
-
thymoquinone
-
polo box inhibitor
trichostatin A
-
decreases Plk1 expression
Vanillin
-
decreases Plk1 expression
VX-680
-
selective inhibition of PLK4 relative to PLK1-3
Wortmannin
-
time-dependent irreversible inhibition with PLK1
Wortmannin
Q6DRK7
-
Wortmannin
Q5UES2
-
Wortmannin
-
enzymatic inhibitor
methyl 2-[(3-carbamoyl-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazolin-8-yl)amino]benzoate
-
-
-
additional information
-
Plk1 depletion in HeLa Plk RNAi cells by Aurora B inhibitor hesperadin, enzyme depletion delays entry into mitosis and arrest in prometaphase activating the spindle checkpoint
-
additional information
-
the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain
-
additional information
-
Plk1 expression is decreased during ciplatin-induced apoptosis while p53 is stabilized
-
additional information
-
in vivo inhibition of Plk1 by DNA damage is ATM- or ATR-dependent
-
additional information
-
Plk1 activity is inhibited upon DNA damage involving ATM or ATR, caffeine blocks the inhibition
-
additional information
-
the enzyme activity is inhibited upon DNA damage
-
additional information
-
only simultaneous mutation of both motifs 192RSST195 and 333RLST336 of Emi2 abrogates polo box domain binding of Plx1
-
additional information
-
GO 6976 retains PLK4 activity
-
additional information
-
inhibited by Plk1-specific antibodies
-
additional information
-
1-NM-PP1 and 3-MB-PP1 have little effect on wild-type
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aurora A
-
-
-
aurora A
-
Plk1 activity is increased upon phosphorylation at threonine-210 by Aurora A in conjunction with Bora
-
basic fibroblast growth factor
-
bFGF, extracellular stimuli to induce NS-1 cell differentiation
-
Bora
-
Plk1 activity is increased upon phosphorylation at threonine-210 by Aurora A in conjunction with Bora
-
dibutyryl cAMP
-
dbcAMP, extracellular stimuli to induce NS-1 cell differentiation
forskolin
-
extracellular stimuli to induce NS-1 cell differentiation
nerve growth factor
-
NGF, extracellular stimuli to induce NS-1 cell differentiation
-
nocodazole
-
-
okadaic acid
-
-
pituitary adenylate cyclase-activating polypeptide 38
-
PACAP38, extracellular stimuli to induce NS-1 cell differentiation
-
interleukin-6
-
IL-6, extracellular stimuli to induce NS-1 cell differentiation
additional information
-
Plk2 is activated in vivo near the G1- to S-phase transition of the cell cycle
-
additional information
-
in vivo enzyme activity is dependent on Cut12
-
additional information
-
expression of Plk2 is rapidly induced by X-ray irradiation and is partly mediated by p53
-
additional information
-
substrate binding to Plk1 is supposed to promote its activity
-
additional information
-
activation of Plk1 requires phosphorylation of the conserved threonine residue Thr210
-
additional information
Q5UES2
activation of SmPlk1 requires phosphorylation of the conserved threonine residue Thr182
-
additional information
Q00444
autophosphorylation of serine 305
-
additional information
-
activated by phosphorylation
-
additional information
Q4FZD7
plk5 is a DNA damage inducible gene
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
ATP
-
-
0.0008
ATP
-
-
0.001
ATP
-
-
0.002
ATP
-
PLK2
0.003
ATP
-
apparent Km, T210V mutant, varied substrate ATP, constant substrate Cdc25c; mutant T210V
0.0032
ATP
-
apparent Km, wild-type enzyme, varied substrate ATP, constant substrate Cdc25c; wild-type
0.004
ATP
-
apparent Km, T210D mutant, varied substrate ATP, constant substrate Cdc25c; mutant T210D
0.0055
ATP
-
apparent Km, hPlk1 1-346 T210D
0.0064
ATP
Q6DRK7
apparent Km, zPlk1 1-312 T196D
0.0076
ATP
Q6DRK7
apparent Km, zPlk1 1-312 wild type
0.0006
Cdc25C
-
apparent Km, T210D mutant, varied substrate Cdc25c, constant substrate ATP; mutant T210D
-
0.00066
Cdc25C
-
apparent Km, wild-type enzyme, varied substrate Cdc25c, constant substrate ATP; wild-type
-
0.0008
Cdc25C
-
apparent Km, T210V mutant, varied substrate Cdc25c, constant substrate ATP; mutant T210V
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
ATP
-
mutant T210V; T210V mutant, varied substrate Cdc25c, constant substrate ATP
0.00229
ATP
Q6DRK7
zPlk1 1-312 wild type
0.0041
ATP
-
wild-type; wild-type enzyme, varied substrate ATP, constant substrate Cdc25c
0.01311
ATP
Q6DRK7
zPlk1 1-312 T196D
0.01386
ATP
-
hPlk1 1-346 T210D
0.019
ATP
-
mutant T210D; T210D mutant, varied substrate ATP, constant substrate Cdc25c
0.0049
Cdc25C
-
mutant T210V; T210V mutant, varied substrate ATP, constant substrate Cdc25c
-
0.0094
Cdc25C
-
wild-type; wild-type enzyme, varied substrate Cdc25c, constant substrate ATP
-
0.0376
Cdc25C
-
T210D mutant, varied substrate Cdc25c, constant substrate ATP
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00085
4-amino-5-fluoro-3-[6-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl]quinolin-2-ol
-
-
0.0000042
AG-013736
-
-
0.02
AG-013736
-
-
0.00024
BAY 439006
-
-
0.02
BAY 439006
-
;
0.03
BAY 439006
-
-
0.000001
BI 2536
-
time-dependent inhibition; time-dependent inhibition; time-dependent inhibition
0.02
BI 2536
-
-
0.0014
CHIR-258
-
-
0.02
CHIR-258
-
;
0.00012
CP 547632
-
-
0.02
CP 547632
-
-
0.0000034
GO 6976
-
-
0.008
GO 6976
-
-
0.016
GO 6976
-
-
0.019
GO 6976
-
-
0.0000005
GSK461364A
-
Ki, apparent dissociation constant, less than 0.0000005
0.00012
H-1152
-
-
0.02
H-1152
-
-
0.0022
imatinib
-
-
0.018
imatinib
-
-
0.02
imatinib
-
;
0.0061
LY294002
-
-
0.0075
LY294002
-
-
0.016
LY294002
-
-
0.02
LY294002
-
-
0.02
N-methyl-2-({3-[(E)-2-(pyridin-2-yl)ethenyl]-2H-indazol-6-yl}sulfanyl)benzenecarboximidic acid
-
;
0.000011
N-[4-({4-[(Z)-(5-methyl-1,2-dihydro-3H-pyrazol-3-ylidene)amino]-6-(4-methylpiperazin-1-yl)pyrimidin-2-yl}sulfanyl)phenyl]cyclopropanecarboxamide
-
-
0.00079
PP1
-
-
0.02
PP1
-
-
0.0000026
staurosporine
-
-
0.00015
staurosporine
-
-
0.00079
staurosporine
-
-
0.0012
staurosporine
-
-
0.0003
SU11248
-
-
0.0093
SU11248
-
-
0.02
SU11248
-
;
0.02
VX-680
-
-
0.0015
Wortmannin
-
time-dependent irreversible inhibition
0.0028
Wortmannin
-
-
0.003
Wortmannin
-
-
0.02
Wortmannin
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00041
(3-[5-methyl-2-[(3,4,5-trimethoxyphenyl)amino]imidazo[5,1-f][1,2,4]triazin-7-yl]phenyl)(phenyl)methanone
-
-
0.000103
(7R)-2-[5-(2,4-difluorophenyl)-1H-pyrazol-4-yl]-7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00126
(7R)-2-[5-(2,4-difluorophenyl)-1H-pyrazol-4-yl]-7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000007
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00135
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000021
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00327
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000532
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-5-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.0288
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-5-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000012
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00867
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000042
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00355
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00104
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(oxetan-3-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000033
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00753
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000009
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00025
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000025
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00087
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000044
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(pyrimidin-5-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00776
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(pyrimidin-5-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000021
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3R)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00048
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3R)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000008
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00038
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000092
(7R)-7-ethyl-5-methyl-8-(1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00303
(7R)-7-ethyl-5-methyl-8-(1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000036
(7R)-7-ethyl-5-methyl-8-(tetrahydro-2H-pyran-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00025
(7R)-7-ethyl-5-methyl-8-(tetrahydro-2H-pyran-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000039
(7R)-7-ethyl-5-methyl-8-(tetrahydrofuran-3-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00141
(7R)-7-ethyl-5-methyl-8-(tetrahydrofuran-3-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000012
(7R)-8-(3,3-difluorocyclobutyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00939
(7R)-8-(3,3-difluorocyclobutyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.01
1-(1-methylpiperidin-4-yl)-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010, pH 7.9, 25C
-
0.004516
1-(2-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000102
1-(2-hydroxyethyl)-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
-
pH and temperature not specified in the publication
0.000151
1-(2-hydroxyethyl)-5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
-
pH and temperature not specified in the publication
0.01445
1-(2-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000641
1-(3,5-dichlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000149
1-(3,5-dimethylphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000274
1-(3-bromo-5-chlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000121
1-(3-chlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000464
1-(3-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.005928
1-(3-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.003241
1-(4-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000703
1-(4-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000143
1-cyclohexyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000009
1-methyl-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
-
pH and temperature not specified in the publication
0.000015
1-methyl-5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
-
pH and temperature not specified in the publication
0.000018
1-methyl-5-(2-[[5-(piperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
-
pH and temperature not specified in the publication
0.000009
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000014
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000068
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.00011
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid
-
pH 7.9, 25C
0.000002
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000006
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000015
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000488
1-methyl-8-[(2-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000051
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000278
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.002666
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.003733
1-methyl-8-[(2-sulfamoylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.01
1-methyl-8-[(3-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide, 1-methyl-8-[(4-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010, pH 7.9, 25C
-
0.000011
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000012
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.00011
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000014
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000016
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000097
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000949
1-methyl-8-[[2-(phenylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.001969
1-methyl-8-[[2-(phenylcarbonyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.002033
1-methyl-8-[[2-(phenylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000146
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000365
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000509
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000095
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000109
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000432
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000051
1-methyl-8-[[3-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000872
1-methyl-8-[[4-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.01
1-methyl-N-phenyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010, pH 7.9, 25C
0.01
1-phenyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010, pH 7.9, 25C
-
0.000059
1-[3-(3-aminopropyl)phenyl]-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000977
1-[3-(dimethylamino)phenyl]-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.00115
2'-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5'-methyl-8'-(propan-2-yl)-5',8'-dihydro-6'H-spiro[cyclobutane-1,7'-pteridin]-6'-one
-
22C, pH not specified in the publication
0.0253
2'-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5'-methyl-8'-(propan-2-yl)-5',8'-dihydro-6'H-spiro[cyclobutane-1,7'-pteridin]-6'-one
-
22C, pH not specified in the publication
0.000028
2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-(2,2,2-trifluoroethyl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
-
pH and temperature not specified in the publication
0.00271
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7,7-trimethyl-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00012
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7-(2,2,2-trifluoroethyl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00348
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7-(2,2,2-trifluoroethyl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000004
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.000024
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.000214
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.00002
3-(1-[2-chloro-4-[(3-hydroxypyrrolidin-1-yl)methyl]phenyl]ethoxy)-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.005689
3-(2-methylcyclohexyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.004927
3-(3,4-dimethoxyphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.00033
3-(3,4-dimethylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.000625
3-(3-chlorophenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.000412
3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)benzonitrile
-
-
0.000549
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.001449
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.01
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
>0.01
0.00117
3-(4-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.000779
3-(4-methylthiophen-3-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.02
3-benzyl-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
>0.020
0.007685
3-methyl-1-(2-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000474
3-methyl-1-(3-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.004528
3-methyl-1-(4-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.001301
3-methyl-1-phenyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.001476
3-methyl-1-[3-(1-methylethyl)phenyl]-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.000225
3-methyl-1-[3-(methylsulfonyl)phenyl]-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
0.001616
3-phenyl-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.000028
3-[(1R)-1-(2-chloro-4-[[(1-methylethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000023
3-[(1R)-1-(2-chloro-4-[[(2-hydroxy-1,1-dimethylethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000021
3-[(1R)-1-(2-chloro-4-[[(2-hydroxyethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000019
3-[(1R)-1-(2-chloro-4-[[(3-hydroxypropyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.0000008
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000006
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000025
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
HCT-116 cell
0.000001
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000035
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000321
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
HCT-116 cell
0.000001
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000061
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000073
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
HCT-116 cell
0.000003
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000045
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
HCT-116 cell
0.00061
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000004
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000013
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
HCT-116 cell
0.00025
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000003
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000017
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
HCT-116 cell
0.00024
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000007
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.0000073
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-(hydroxymethyl)imidazo[1,2-a]pyridin-3-yl]thiophene-2-carboxamide
-
-
0.000006
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
0.000034
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
HCT-116 cell
0.0011
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
0.000002
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
0.000003
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
HT-29 cell
0.000005
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
Colo-205 cell
0.000009
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
MX-1 cell
0.000011
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
A-549 cell; HCT-116 cell; SKOV-3 cell
0.00063
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
0.000004
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
0.000032
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
HCT-116 cell
0.00046
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
-
0.000088
3-[(1R)-1-[2-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.0000049
3-[(1R)-1-[2-chloro-4-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000016
3-[(1R)-1-[2-chloro-4-[(1,1-dioxidothiomorpholin-4-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000012
3-[(1R)-1-[2-chloro-4-[(3-oxopiperazin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000013
3-[(1R)-1-[2-chloro-4-[(4-fluoropiperidin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000027
3-[(1R)-1-[2-chloro-4-[(4-hydroxypiperidin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000017
3-[(1R)-1-[2-chloro-4-[(4-methylpiperazin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000025
3-[(1R)-1-[2-chloro-4-[(cyclopentylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000012
3-[(1R)-1-[2-chloro-4-[(cyclopropylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000022
3-[(1R)-1-[2-chloro-4-[(dimethylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000021
3-[(1R)-1-[2-chloro-4-[(ethylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000016
3-[(1R)-1-[2-chloro-4-[(methylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.0000098
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-(difluoromethoxy)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.00002
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-(difluoromethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000021
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-chlorophenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.00021
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-cyclopropylphenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000046
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-fluorophenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.00015
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-methylphenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.00003
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000044
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000994
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
HCT-116 cell
0.0003
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000002
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.000009
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
-
0.00114
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
HCT-116 cell
0.000035
3-[(2-chlorobenzyl)oxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000092
3-[1-(2-chlorophenyl)ethoxy]-5-[7-(hydroxymethyl)imidazo[1,2-a]pyridin-3-yl]thiophene-2-carboxamide
-
-
0.007479
3-[1-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)piperidin-3-yl]propanamide
Q9H4B4
-
0.000039
3-[1-[2-chloro-5-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
0.000032
3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide
-
-
0.000021
3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanoic acid
-
-
0.000099
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propan-1-ol
Q9H4B4
-
0.000051
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
Q9H4B4
-
0.000172
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
Q9H4B4
-
0.001382
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
Q9H4B4
-
0.00000083
4-((R)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydro-pteridin-2-ylamino)-3-methoxy-N-(1-methyl-piperidin-4-yl)-benzamide
-
-
-
0.00274
4-[(5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-yl)amino]benzenesulfonamide
-
-
0.000031
4-[7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-6-oxo-6,7-dihydropteridin-8(5H)-yl]benzonitrile
-
22C, pH not specified in the publication
0.00376
4-[7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-6-oxo-6,7-dihydropteridin-8(5H)-yl]benzonitrile
-
22C, pH not specified in the publication
0.00043
5-(1-methyl-1H-imidazol-5-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
0.000035
5-(1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
0.003
5-(2-amino-1,3-thiazol-5-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
larger than 0.003
0.0000018
5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-pyrrole-3-carboxamide
-
pH and temperature not specified in the publication
0.000272
5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-[2-(tetrahydro-2H-pyran-4-yloxy)ethyl]-1H-pyrrole-3-carboxamide
-
pH and temperature not specified in the publication
0.000002
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
0.000009
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
0.0000022
5-(5,6-dimethoxy-1H-benzimidazole-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
-
-
-
0.0013
5-(5,6-dimethoxy-1H-benzimidazole-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
-
Escherichia coli-expressed recombinant GST-tagged TbPLK
-
0.000003
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
0.000041
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
0.000476
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
HCT-116 cell
0.000022
5-imidazo[1,2-a]pyridin-3-yl-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
0.00198
5-methyl-7-(2-nitrophenyl)-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.0005
5-methyl-7-(3-phenoxyphenyl)-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.01
5-methyl-7-phenyl-N-(2-pyridin-4-ylethyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
0.00004
5-methyl-7-phenyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.01
5-methyl-7-phenyl-N-[3-(trifluoromethyl)phenyl]imidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
0.01
5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
0.00003
5-methyl-7-[3-(trifluoromethyl)phenyl]-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.00106
5-methyl-7-[4-(trifluoromethyl)phenyl]-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.0012
5-methyl-N,7-diphenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.01
5-methyl-N-(3-morpholin-4-ylpropyl)-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
0.00281
5-methyl-N-(4-nitrophenyl)-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.00013
5-pyrazolo[1,5-a]pyridin-3-yl-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
0.003
5-[2-(phenylamino)-1,3-thiazol-5-yl]-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
larger than 0.003
0.0021
5-[2-[(phenylcarbonyl)amino]-1,3-thiazol-5-yl]-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
0.000003
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
0.000015
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
HCT-116 cell
0.00035
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
0.000007
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
0.00003
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
HCT-116 cell
0.00055
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
0.000002
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
0.000003
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
HT-29 cell
0.000005
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
Colo-205 cell
0.00001
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
MX-1 cell
0.000012
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
HCT-116 cell
0.000014
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
A-549 cell
0.000032
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
SKOV-3 cell
0.00027
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
-
0.00267
7-(2-bromophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.00566
7-(2-methoxyphenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.00007
7-(3-bromophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.00008
7-(4-fluorophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.00003
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7-dimethyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00716
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7-dimethyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000009
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00342
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00013
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00182
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000168
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(pyridin-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00182
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(pyridin-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000017
7-ethyl-5-methyl-8-phenyl-2-(2-phenyl-1H-imidazol-1-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00283
7-ethyl-5-methyl-8-phenyl-2-(2-phenyl-1H-imidazol-1-yl)-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000015
7-ethyl-8-(4-fluorophenyl)-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00234
7-ethyl-8-(4-fluorophenyl)-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.000013
8-(3,3-difluorocyclopentyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.00032
8-(3,3-difluorocyclopentyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
22C, pH not specified in the publication
0.001565
8-(biphenyl-2-ylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000006
8-(phenylamino)-1-(2,2,2-trifluoroethyl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.00043
8-(phenylamino)-1-(propan-2-yl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.01
8-(phenylamino)-1-[2-(piperidin-1-yl)ethyl]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010, pH 7.9, 25C
-
0.000248
8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000103
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000261
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000346
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000012
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000013
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.00015
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000943
8-[(2-benzylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.002076
8-[(2-carbamoylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000027
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000037
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000125
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000013
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000024
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000042
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.0001
8-[(3-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000135
8-[(3-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000197
8-[(4-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000256
8-[(4-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
-
0.000049
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.002104
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.002523
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.002051
8-[[2-acetyl-3-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.01
8-[[2-acetyl-3-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010; larger than 0.010
0.000464
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.002292
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.01
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010
0.000109
8-[[2-acetyl-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.01
8-[[2-acetyl-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010; larger than 0.010
0.00004
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000066
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000082
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.000007
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000238
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.00045
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
-
0.14
AMPPNP
-
mutant T210D
0.155
AMPPNP
-
mutant T210V
0.166
AMPPNP
-
wild-type
0.00000083
BI 2536
-
-
0.0008
BI-2536
-
-
0.0000008
BI2536
-
-
0.00000087
BI6727
-
-
-
0.008
BTO-1
-
-
0.0098
cyclic (-CH2-CO-Pro-Leu-His-Ser-pThr-Cys-S-)
-
25C, pH not specified in the publication
0.0085
cyclic [-CH2-CO-N[2-(1H-indol-3-yl)ethyl]-CH2-CO-Leu-His-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
25C, pH not specified in the publication
0.0048
cyclic [-CH2-CO-N[3-[[2-(1H-indol-3-yl)ethyl]amino]-3-oxopropyl]-CH2-CO-Leu-His-Ser-p-Thr-NH-CH[CONH2]-CH2-S-]
-
25C, pH not specified in the publication
0.0026
cyclic [-CH2-CO-N[6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl]-CH2-CO-Leu-His-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
25C, pH not specified in the publication
0.0011
cyclic [-CH2-CO-N[6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl]-CH2-CO-Leu-His[N3-(8-phenyloctyl)]-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
25C, pH not specified in the publication
0.01
ethyl 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylate
-
larger than 0.010, pH7.9, 25C
0.00000005
GSK461364A
-
less than 50 nM
0.00525
LY294002
-
-
0.001117
methyl 2-[(3-carbamoyl-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazolin-8-yl)amino]benzoate
-
pH 7.9, 25C
-
0.0126
morin
-
-
0.0126
morin
-
-
0.004215
N,1-dimethyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
pH 7.9, 25C
0.000048
N-(2-hydroxyethyl)-3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide
-
-
0.00009
N-(3,4-dimethoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.0003
N-(3-methoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.00068
N-(4-methoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.0015
N-benzyl-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.01
N-cyclohexyl-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
0.01
N-cyclopentyl-1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010, pH 7.9, 25C
0.01
N-cyclopropyl-1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
larger than 0.010, pH 7.9, 25C
0.003007
N-[(1S)-1-phenylethyl]-3-thiophen-2-ylisoxazolo[5,4-c]pyridin-5-amine
Q9H4B4
-
0.000207
N-[2-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]-2-phenylacetamide
-
-
0.0000002
N-[4-[(6-chloropyridin-3-yl)methoxy]-3-methoxybenzyl]-2-(3,4-dimethoxyphenyl)ethanamine
-
-
0.00038
N-[4-[2-(dimethylamino)ethoxy]phenyl]-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
0.000009
ONO1910
-
-
0.00026
ONO1910
-
Plk2
0.01
ONO1910
-
-
0.00034
PHA-680626
-
mutant T210D
0.00044
PHA-680626
-
mutant T210V
0.00053
PHA-680626
-
; wild-type
0.064
quercetin
-
-
0.064
quercetin
-
-
0.0000002
SBE13
-
immunoprecipitated Plk1 from HeLa cells
-
0.002
scytonemin
-
-
0.002
scytonemin
-
-
0.002
scytonemin
-
-
0.0008
staurosporine
-
-
0.000817
tert-butyl 1-methyl-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-4-oxo-1,4,6,7-tetrahydro-5H-pyrrolo[3,2-c]pyridine-5-carboxylate
-
pH and temperature not specified in the publication
0.000024
Wortmannin
-
-
0.000024
Wortmannin
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity of wild-type and mutant GST-tagged or His6-tagged Plk3 with p125
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
-
activity assay
7.2
-
activity assay
7.2
-
Plk scintillation proximity assay
7.4
-
assay at
7.4
-
; assay at
7.4
-
activity assay
7.4
-
kinase assay
7.4
-
activity assay
7.4
-
kinase assay
7.5
-
assay at
7.5
-
assay at
7.5
-
kinase assay
7.5
-
kinase assay
7.5
-
assay at
7.6
-
in vitro kinase assay
7.9
-
kinase assay; kinase assay; kinase assay
8
-
in vitro kinase assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
kinase assay at room temperature
22
-
Plk scintillation proximity assay at room temperature
22
Q00444
kinase assay
22
-
kinase assay at room temperature
23
-
kinase assay
25
-
kinase assay; kinase assay; kinase assay
30
-
assay at
30
-
; assay at
30
-
activity assay
30
-
in vitro kinase assay
30
-
kinase assay
30
-
activity assay
30
-
kinase assay
30
-
assay at
37
-
assay at
37
-
kinase assay
37
-
kinase assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.13
Q5UES2
theoretical
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
anaplastic thyroid carcinoma cell line
Manually annotated by BRENDA team
-
squamous A-253 cell
Manually annotated by BRENDA team
-
squamous A-431 cell
Manually annotated by BRENDA team
-
NSCLC line A549
Manually annotated by BRENDA team
-
anaplastic thyroid carcinoma cell line
Manually annotated by BRENDA team
-
anaplastic thyroid carcinoma cell line
Manually annotated by BRENDA team
-
increased requirement for Plk1 in comparison to normal cells
Manually annotated by BRENDA team
-
one-cell stage embryos, both the protein and the mRNA of Plk1 are uniformly distributed, but the kinase activity of Plk1 increases at G2/M phase and decreases at the end of M phase
Manually annotated by BRENDA team
-
skin epidermis
Manually annotated by BRENDA team
-
is highly expressed, on average 2.7-fold higher mRNA expression levels than in normal organs excluding testis, promoter activity 18.9 higher than in normal lung and renal cells
Manually annotated by BRENDA team
Q5UES2
germinal cell of schistosome
Manually annotated by BRENDA team
-
osteoblast cell
Manually annotated by BRENDA team
-
osteoblast cell
Manually annotated by BRENDA team
-
leukemic cell line
Manually annotated by BRENDA team
-
osteosarcoma cell line
Manually annotated by BRENDA team
-
expression appears to be down-regulated in lung carcinomas
Manually annotated by BRENDA team
-
peripheral T cell lymphoma
Manually annotated by BRENDA team
-
transition of monocytes from peripheral blood to matrix bound macrophages is accompanied by increasing levels of Fnk with time in culture
Manually annotated by BRENDA team
-
Plk3 accumulates by serum starvation, at a point in the cell cycle commonly referred to as G0
Manually annotated by BRENDA team
-
screening of a lambdagt 10 library, full-length construct
Manually annotated by BRENDA team
-
osteoblast cell
Manually annotated by BRENDA team
-
anaplastic thyroid carcinoma cell line
Manually annotated by BRENDA team
Q62673
maturing, after activation
Manually annotated by BRENDA team
-
osteosarcoma cell line
Manually annotated by BRENDA team
-
during embryonic development, the mRNA is expressed in all tissues examined, whereas in adult tissues, expression is limited to thymus and ovaries
Manually annotated by BRENDA team
-
osteosarcoma cell line
Manually annotated by BRENDA team
-
neuroblastoma cell
Manually annotated by BRENDA team
-
cDNA library screen, polo-box domain
Manually annotated by BRENDA team
-
anaplastic thyroid carcinoma cell line
Manually annotated by BRENDA team
-
primary, when activated by phytohemagglutinin, a high level of PLK transcripts results within 2-3 days. In some cases, addition of interleukin 2 to these cells increases the expression of PLK mRNA further
Manually annotated by BRENDA team
-
is highly expressed
Manually annotated by BRENDA team
-
during embryonic development, the mRNA is expressed in all tissues examined, whereas in adult tissues, expression is limited to thymus and ovaries
Manually annotated by BRENDA team
-
osteosarcoma cell line
Manually annotated by BRENDA team
-
Plk1 abundance and kinase activity are strongly upregulated at the G2/M transition, reach a peak during mitosis, and are downregulated by the subsequent G1 phase, albeit with slower kinetics than Cdk1/cyclin B activity, which falls acutely at anaphase onset
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
during embryonic development, the mRNA is expressed in all tissues examined, whereas in adult tissues, expression is limited to thymus and ovaries
Manually annotated by BRENDA team
additional information
-
no PLK transcripts are found in normal adult lung, brain, heart, liver, kidney, skeletal muscle, and pancreas, resting peripheral lymphocytes do not express the gene at all. Primary cultures of human peripheral macrophages, which are not dividing under the culture conditions applied, showed very little or no PLK mRN
Manually annotated by BRENDA team
additional information
-
enzyme quantity is stable during meiotic maturation
Manually annotated by BRENDA team
additional information
Q62673
enzyme quantity is stable during meiotic maturation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated with Hsp90
Manually annotated by BRENDA team
-
Plk2 interaction with the centrosome is independent on enzyme kinase activity
Manually annotated by BRENDA team
-
primarily, during interphase
Manually annotated by BRENDA team
-
after transfection into PC3 cells, HeLa cells and NIH 3T3 cells, Plk1 localization is controlled not only by the polo box domain, the kinase domain is also involved in Plk1 targeting mechanism to the centrosome
Manually annotated by BRENDA team
-
co-distributes with HsCdc14A to the centrosomes from prophase to metaphase
Manually annotated by BRENDA team
-
Plk1 expressed during G2 and mitosis
Manually annotated by BRENDA team
-
Plk1s accumulation depends on its own activity, activity is required for maintaining centrosome function
Manually annotated by BRENDA team
-
Plk4 enzyme is localized exclusively to the centrosome, with none accumulated in the spindle midbody
Manually annotated by BRENDA team
-
polo kinase undergoes cell cycle-dependent changes in its distribution. It is predominantly cytoplasmic during interphase, it becomes associated with condensed chromosomes toward the end of prophase, and it remains associated with chromosomes until telophase, whereupon it becomes cytoplasmic
Manually annotated by BRENDA team
-
polo kinase undergoes cell cycle-dependent changes in its distribution. It is predominantly cytoplasmic during interphase, it becomes associated with condensed chromosomes toward the end of prophase, and it remains associated with chromosomes until telophase, whereupon it becomes cytoplasmic
Manually annotated by BRENDA team
Q62673
in fertilized eggs between female and male pronuclei at microtubules
Manually annotated by BRENDA team
-
TbPLK trans-localizes from the flagellum attachment zone to the cytoplasm during anaphase
Manually annotated by BRENDA team
-
TbPLK trans-localizes from the flagellum attachment zone to the cytoplasm during anaphase
-
Manually annotated by BRENDA team
-
the enzyme is enriched at the anterior tip of the flagellum attachment zone
-
Manually annotated by BRENDA team
-
accumulation of Plk1 in germinal vesicle stage oocytes
Manually annotated by BRENDA team
Q62673
accumulation of Plk1 in germinal vesicle stage oocytes
Manually annotated by BRENDA team
-
localization of Plk3 with Golgi fragments during mitosis, overview
Manually annotated by BRENDA team
-
Plk1, Plk3 during interphase, binding via phosphorylated Nir2
Manually annotated by BRENDA team
-
BubR1 colocalizes with Plk1 at kinetochores of unaligned chromosomes
Manually annotated by BRENDA team
-
kinetochore localization of BubR1 and Plk1 is important for BubR1 hyperphosphorylation
Manually annotated by BRENDA team
-
localizes to kinetochores during prophase and metaphase
Manually annotated by BRENDA team
-
Plk1 expressed during G2 and mitosis
Manually annotated by BRENDA team
-
Plk1s accumulation depends on its own activity, activity is required for maintaining kinetochore function
Manually annotated by BRENDA team
-
rapidly accumulates at kinetochores, appears to be partially released once all chromosomes are properly congressed at the metaphase plate
Manually annotated by BRENDA team
-
the enzyme localizes to prometaphase kinetochores and is reduced at metaphase kinetochores
Manually annotated by BRENDA team
Q62673
enzyme is located at and required for microtubule assembly
Manually annotated by BRENDA team
-
at anaphase onset, Plk1 redistributes onto equatorial microtubule bundles that define the spindle midzone or central spindle, and remain tightly associated with these microtubules during midbody formation and completion of cytokinesis
Manually annotated by BRENDA team
-
meiotic chromosome pairing centers localize PLK-2 to the nuclear envelope
Manually annotated by BRENDA team
-
Plk3, as long as the nucleolus is intact, and is undetectable during mitosis
Manually annotated by BRENDA team
-
nucleocytoplasmic space of mitotic cells
Manually annotated by BRENDA team
-
the nuclear localization sequence is 48RSRRRYVRGR57
Manually annotated by BRENDA team
-
speckled domains inside the nucleus
Manually annotated by BRENDA team
-
after fertilization, female and male
Manually annotated by BRENDA team
-
co-localization at the central spindle with Pavarotti, a kinesin-related motor protein
Manually annotated by BRENDA team
-
mid zone of the central spindle
Manually annotated by BRENDA team
-
middle region, at anaphase-telophase I and anaphase-telophase II stages
Manually annotated by BRENDA team
Q62673
middle region, at anaphase-telophase I and anaphase-telophase II stages
Manually annotated by BRENDA team
-
by anaphase, PLK1 relocates from the centrosome to the central spindle while HsCdc14A is still at centrosome
Manually annotated by BRENDA team
-
localizes to spindle poles during prophase and metaphase
Manually annotated by BRENDA team
-
Plk1 is expressed during G2 and mitosis at the spindle pole and spindle midzone
Manually annotated by BRENDA team
-
rapidly accumulates at spindle poles
Manually annotated by BRENDA team
-
after germinal vesicle breakdown, at metaphase I stage, and in MII spindle pole
Manually annotated by BRENDA team
Q62673
after germinal vesicle breakdown, at metaphase I stage, and in MII spindle pole
Manually annotated by BRENDA team
additional information
-
intracellular localization of wild-type and mutant enzymes, overview
-
Manually annotated by BRENDA team
additional information
-
localization changes with embryonal development, colchicine inhibits spindle pole localization of the enzyme, taxol treatment leads to localization in the cytoplasm
-
Manually annotated by BRENDA team
additional information
Q62673
localization changes with embryonal development, e.g. throughout the division plane during cytokinesis, subcellular localization analysis, overview, colchicine inhibits spindle pole localization of the enzyme, taxol treatment leads to localization in the cytoplasm
-
Manually annotated by BRENDA team
additional information
-
localization of the enzyme is dependent on cell cycle stage
-
Manually annotated by BRENDA team
additional information
-
the enzyme co-localizes with the protein kinase Chk2
-
Manually annotated by BRENDA team
additional information
-
the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain
-
Manually annotated by BRENDA team
additional information
-
at telophase, PLK1 localization is only at the mid-body where HsCdc14A is also apparent
-
Manually annotated by BRENDA team
additional information
-
no localization to the nucleus, kinetoplast, basal bodies or to the flagellum
-
Manually annotated by BRENDA team
additional information
-
Plk1 is expressed during G2 and mitosis at the midbody
-
Manually annotated by BRENDA team
additional information
-
translocates to the midbody during telophase, RhoA is also enriched at the midbody region during telophase and colocalizes with Plk1
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
-
recombinant human Plk1 polo-box domain
677343
34000
-
determined by SDS-PAGE and Western Blot analysis
705986
34390
Q4KMI8
expected molecular weight of the protein with the N-terminal Gly-Pro-Leu-Gly-Ser linker residues and a T196D substitution
690267
35920
Q6DRK7
expected molecular weight of the protein with the N-terminal Gly-Pro-Leu-Gly-Ser linker residues that separate the GST protein from Plk1 KD
690239
35930
Q6DRK7
expected molecular weight of the protein with the additional T196D substitution
690239
39050
-
expected molecular weight of the protein with the N-terminal Gly-Pro-Leu-Gly-Ser linker residues that separate the GST protein from Plk1 KD
690239
39060
-
expected molecular weight of the protein with the additional T210D substitution
690239
62000
-
determined by SDS-PAGE and Western Blot analysis
704521
67000
-
determined by SDS-PAGE and Western Blot analysis
702943
68000
-
determined by SDS-PAGE and Western Blot analysis
682039
70500
Q5UES2
theoretical
704101
72000
Q4FZD7
determined by SDS-PAGE and Western Blot analysis
705986
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 70000, about, SDS-PAGE
additional information
-
Plo1 is a component of the spindle pole body, assembly at spindle checkpoint, mechanism, recruitment of Plo1 to the complex is inhibited by Mad2, overview
additional information
-
the enzyme contains 3 different polo box motifs in the non-catalytic region that are involved in protein protein interactions in the mitotic spindle formation process
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
-
phosphoprotein
-
the enzyme is phosphorylated by Chk2
phosphoprotein
Q00444
autophosphorylation
phosphoprotein
-
phosphorylated by Aurora A
phosphoprotein
-
-
phosphoprotein
-
self-phosphorylation at multiple sites is required for Plk4 instability, indicating a requirement for a threshold level of Plk4 kinase activity to promote its own destruction
phosphoprotein
Saccharomyces cerevisiae, Saccharomyces pombe
-
-
phosphoprotein
Q5UES2
-
phosphoprotein
-
Plo1 is phosphorylated at Ser402 in the stress response pathway, mechanism, phosphorylation is required for recruitment to the interphase spindle pole body and mitotic entry for cell tip growth and cell division, Plo1 phosphorylation is increased at elevated temperature
phosphoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the structure of zPlk1 KD in complex with the inhibitor is solved to 2.85 A resolution
Q4KMI8
the structures of wild-type zPlk KD, mutant T196D, wild-type zPlk KD in complex with ADP and the mutant T196D in complex with wortmannin are determined at resolutions of 2.8, 2.4, 2.6 and 2.6 A, respectively
Q6DRK7
zPlk1 is crystallized in complex with compound38
-
crystal structures of the PBD in complex with nonphysiological and control target peptides Cdc25C and Cdc25C-P, to 1.95 A, 2.10 A, and 2.80 A resolution, Trp-414 is fundamental in substrate recognition regardless of its phosphorylation status; the crystal structures of the polo box domain and its complexes with Cdc25C-P and Cdc25C peptides are solved by nuclear replacement and refined to 1.95, 2.10, and 2.80 A resolution
-
crystal structures of the T210V mutant of the kinase domain of human Plk1 complexed with adenylylimidodiphosphate or the pyrrolo-pyrazole inhibitor PHA-680626 are determined at 2.4 and 2.1 A resolution, respectively; wild-type, to ca. 3 A resolution, T210V mutant complexed with the nonhydrolyzable ATP analogue AMP-PNP or the pyrrolo-pyrazole inhibitor PHA-680626 at 2.4 and 2.1 A resolution, respectively, by the hanging drop method, typical kinase fold with the unphosphorylated (mutant T210V) activation loop in an extended conformation, stabilized by a crystal contact, presence of a phenylalanine at the bottom of the ATP pocket, combined with a cysteine in the roof of the binding site, a pocket created by Leu132 in the hinge region, and a cluster of positively charged residues in the solvent-exposed area outside of the adenine pocket adjacent to the hinge region
-
crystal-packing analysis
-
Plk1 polo-box domain in complex with unphosphorylated and phosphorylated Cdc25C, to 2.1 and 2.85 A resolution, respectively, by the sitting-drop method, crystals of the polo-box domain in complex with the phosphorylated peptide belong to the orthorhombic space group P212121, with unit-cell parameters a = 38.23, b = 67.35, c = 88.25 A, alpha = gamma = beta = 90, and contain one molecule per asymmetric unit. Crystals of the polo-box domain in complex with the unphosphorylated peptide belong to the monoclinic space group P21, with unit-cell parameters a = 40.18, b = 49.17, c = 56.23 A, alpha = gamma = 90, beta = 109.48, and contain one molecule per asymmetric unit
-
purified untagged recombinant selenomethionine-labeled enzyme comprising residues 367-603, cleavage through subtilisin, sitting drop vapour diffusion method, 4C, 0.001 ml of protein solution containing 10 mg/ml protein is mixed with 0.001 ml mother liquor containing 5-10% v/v PEG 4000, 0.1 M sodium citrate, pH 6.0, and 0.1 M ammonium acetate, formation of needle-like crystals that do not diffract, co-crystallization with the synthesized phosphopeptide MQSpTPL is suitable for crystallization giving crystals within 2-3 days by sitting drop vapour diffusion from 1-10% PEG 20000, 0.1 M MES, pH 6.5, at room temperature, X-ray diffraction structure determination and analysis at 2.2-2.3 A resolution, complex formation between enzyme and phosphopeptide via residues W414, L490, H538, and K540
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
association with Hsp90 at the centrosome stabilizes the enzyme
-
kinase-active Plk4 is inherently unstable and targeted for degradation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 50 mM HEPES buffer, pH 7.5, 5 mM TCEP
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q4KMI8
using a glutathione-Sepharose and a Q-Sepharose column
Q6DRK7
protein A-affinity purification is performed
-
affinity purified; on Ni2+ resin
-
by gel filtration
-
by gel filtration; using glutathione-agarose
-
by Ni2+ chromatography and gel-filtration; the protein is purified in a Ni2+ column and by gel filtration chromatography
-
hexahistidine-tagged Plk1 is purified using HIS-select nickel affinity agarose
-
on nickel affinity column and by gel filtration; using a HiTrap nickel chelating affinity column and a gel filtration column, the His-tag is removed by PreScission protease treatment
-
Plk1, aa 36-345, is expressed in H5 insect cells as GST fusion protein, the tag is removed and the ptotein is purified on an ion exchange column
-
purified Plk1 is obtained from HeLa cell extracts using a Q-Sepharose FF, a Heparin FF, a CM Sepharose FF, a poly(U) Sepharose 4B, and a substrate affinity column
-
recombinant GST-tagged Plk1 from Spodoptera frugiperda Sf9 cells
-
recombinant HA-tagged Plk from HeLa cells by immunoprecipitation
-
recombinant His6-tagged wild-type and mutant Plk3 from HeLa cells
-
recombinant selenomethionine-labeled GST-tagged Plk1 from Escherichia coli by glutathione affinity chromatography, the GST-tag is cleaved off, recombinant His-tagged Plk1 from Sf9 insect cells by nickel affinity chromatography
-
SYK and PLK1 immune complexes immunoprecipitated from whole cell lysates of NALM-6 and BT-20 cell lines
-
using a glutathione-Sepharose and a Q-Sepharose column
-
nucleoli are prepared from NIH3T3 cells
Q4FZD7
by glutathione-Sepharose 4B purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for a yeast two-hybrid screen
-
full-length zPlk1 cDNA and the zPlk1 kinase domain sequence, encompassing residues 17-312, are cloned, the expression plasmid pGEX6P-1 is used
Q4KMI8
full-length zPlk1 cDNA is inserted into the pME18S-FL3 plasmid and subcloned into pGEX6P-1, the zPlk1 kinase domain sequences for crystallography and activity constructs encompassing amino acids 1-312 or 17-312
Q6DRK7
developmental expression analysis of the highly conserved enzyme
-
expression of GST-tagged Plx1 in S2 cells, co-expression with GFP-tagged MEI-S332
-
into the pDONR221lambda entry vector, the gene is recombined in different destination vectors for expression in fusion with GFP or protein A
-
the polo fragment is cloned into pBluescript and subcloned into the pUASP vector to generate transgenic flies
-
a full-length Myc-PLK1 plasmid is used, full-length PLK1, cloned into pDON207, is inserted into a pCINeo vector, pFLAG-PLK1-PBD and pEGFP-PLK1-PBD constructs are generated
-
determination of nucleotide sequence of cDNA
-
DNA sequence determination, transient expression of FLAG-tagged wild-type and mutant enzymes in 293T cells, co-expression witg GFP, overexpression induces wild-type protein kinase Chk2 phosphorylation, but does not increase phosphorylation of Chk2 mutant T68A
-
expressed in Escherichia coli BL21(DE3) pLysS as a GST fusion protein, 293T cells co-transfected with FLAG-PLK1 and GFPHsCdc14A, GST-tagged PLK1 kinase expressed in insect, HeLa cells transiently transfected to express GFP-HsCdc14A and FLAG-PLK1; into the pGEX-6P vector for expression in Escherichia coli BL21DE3 cells, furthermore an insect expression construct is used, and in fusion with a FLAG-tag for transfection of HEK-293T cells
-
expressed in sf21 cells; into pFastBac1 for expression in Spodoptera frugiperda insect cells
-
expressed through the baculoviral vector system
-
expression in Escherichia coli
-
expression in U2OS cells
-
expression of FLAG-tagged Plk1 in COS-7 cells, co-expression of Plk1 and p53 in p53-deficient lung carcinoma H1299 cells greatly decreases the p53-mediated recombinant transcription, this effect does not appear with co-expression of kinase-defective K82M Plk1
-
expression of GFP-tagged enzyme in HeLa cells and LLCPK cells
-
expression of GST-tagged Plk1 in Escherichia coli strain B834(DE3) strain as selenomethionine-labeled enzyme, expression of His-tagged Plk1 in Spodoptera frugiperda Sf9 cells using the baculovirus system
-
expression of HA-tagged Plk in HeLa cells, co-expression of His-tagged Plk with wild-type and mutant Myt1
-
expression of His6-tagged wild-type and mutant Plk3 in HeLa cells
-
expression of Plk1 in HeLa cells, DU145 cells, T98G cells, and in GM05849 cells
-
expression of wild-type and K111R mutant enzyme in CHO cells, overexpression of HA-tagged wild-type and mutant Plk2 in U2OS cells
-
expression of wild-type and mutant GST-tagged or His6-tagged Plk3
-
FLAG-tagged PLK1 is constructed
-
Fnk as fusion protein with GFP expressed in COS cells
-
full-length hPlk1 cDNA is inserted into a pCMV plasmid and subcloned into pGEX6P-1, the hPlk1 kinase domain sequences for crystallography and activity constructs encompassing amino acids 1-346
-
GST-tagged PLK1 (1-331) expressed in SF9 cells; His-tagged PLK4 (1-269) expressed in Escherichia coli
-
human full-length Plk1 cDNA or FLAG-Plk1 cDNA is subcloned into the pZeoSV2+ vector
-
into the pCAGGS vector
-
into the vector pBluescript II KS+, subsequently into pET15b+ for expression in Escherichia coli BL21DE3 cells, and into pEGFP-C1
-
into the vector pCMV6-XL5 for transfection
-
into the vector pRcCMV for transfection of lung fibroblasts, the plasmid YCplac111-GAL1-HA-EGFP-PLK is used for the transformation of Saccharomyces cerevisiae cells
-
Plk1 cDNAs are subcloned into pEGFP-C1
-
Plk1 cloned into vector pFastBac, the polo box domain cDNA sequence (residues 367-603) cloned into vector pGEX-6P-2. PC3 cells, HeLa cells and NIH 3T3 cells transfected with either EGFP-Plk1 or EGFP-Plk1 H538A/K540M; the Plk cDNA sequence is cloned into a pFastBac vector to generate a recombinant baculovirus, the polo box domain cDNA sequence, residues 367-603, is cloned into vector pGEX-6P-2
-
Plk1 polo-box domain cloned into vector pGEX-6P-2, overexpressed as a GST fusion protein in Escherichia coli BL21(DE3) plys strain
-
siRNA targeted against Plk1 gene is cloned into pEGFP-H1
-
stable expression of Plk1 and transfection with hairpin shRNA in HeLa cells, expression of GST-tagged Plk1 in Spodoptera frugiperda Sf9 cells
-
the plasmids pBluescript, pBS-FLAG, pRC-beta actin and pRC-CMV are used
-
the Plk1 3'-UTR region is amplified and cloned downstream of the luciferase gene into the pMIRREPORT luciferase vector
-
the vector pSUMO is used, an EGFP-PLK4 construct is used
Q00444
transduction of PLK1flox/delta cells with retroviruses expressing either wild-type Plk1 or the equivalent double mutant C67V/L130G, as EGFP fusions
-
into the vector pEGFP-C1 for transfection of NIH3T3 and HEK-293 cells
Q4FZD7
isolation of cDNA
-
synchronized HeLa GFP-histone H2B cells transfected with HA-tagged mouse Plk1
-
the plasmids of pU6-Plk1 shRNA and pU6-Plk1 scramble shRNA are constructed
-
wild-type and kinase-inactive (D154A) mutant enzyme are stably expressed in a human cell line (DLD-1) in which accurate chromosome segregation maintains a pseudodiploid karyotype
-
a GST-fusion protein is generated
-
EGFP-tagged Cdc5 protein is expressed by high copy plasmid pRS424, 425 or 426 under control of authentic promoter
-
expression of CDC5 fused to the Met3 promoter intergrated in the LEU2 locus of a yeast strain carrying a null allele of CDC5
-
GAL-HA3-cdc5, GAL-HA3-cdc5-K110A, and GAL-HA3-cdc5-ad are integrated into the plasmids pDM164, pDM173, and pDM191, respectively
-
HA-epitope-tagged Cdc5p expressed in FKH2 and fkh2delta strains
-
the plasmids pRS316, YEp351 and YCplac111 are used
-
into the pDrive cloning vector for sequencing, into the pCR2.1-TOPO and V5His-tagged pcDNA3.1 expression vectors
Q5UES2
overexpression of mutant K69R in a checkpoint-defective mad2-deletion strain, two-hybrid expression of wild-type and mutant enzymes with diverse protein partners for interaction study, overview
-
a DNA fragment encoding the N-terminus of the TbPLK gene product is cloned into the tetracycline-inducible RNAi vector pZJM for knockdown of TbPLK expression, for tagging proteins TbPLK is cloned into the pC-EYFP-Bla vector, a plasmid for expressing glutathione S-transferase-TbPLK is constructed by cloning a DNA fragment containing full-length TbPLK into the vector pET41a
-
overexpression of TY1-epitope-tagged PLK and a kinase-dead variant, results in the accumulation of cells that have divided their nucleus but not their kinetoplast (2N1K cells), kinetoplast is mainly found at the posterior end of the cell
-
the Trypanosoma brucei EYFP-tagged enzyme is ectopically expressed in HeLa cells. It is predominantly nuclear in interphase cells, whereas in mitotic cells it is localized throughout the cytoplasm. It is unable to be targeted to spindle poles, the central spindle or the midbody in HeLa cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
inhibition of BCR/ABL by imatinib or nilotinib leads to decreased expression of PLK1 protein in CML cells
-
Plk expression is regulated by the microRNAs miR-100 and miR-142-5p
-
overexpressed in many tumor types
-
overexpressed in various tumors
-
overexpression is often associated with oncogenesis
-
overexpression of Plk1 is commonly observed in many human malignancies, Plk expression is regulated by the microRNAs miR-100 and miR-142-5p
-
Plk is over-expressed in approximately 80% of human tumors of diverse origins
-
PLK1 is highly expressed in anaplastic thyroid carcinoma, ATC
-
PLK1 is highly expressed in sarcoma cell lines and in osteosarcoma tissues
-
Plk1 is overexpressed in tumors
-
Plk1 overexpression is strongly associated with cancer
-
significantly over-expressed in basal cell carcinoma and squamous cell carcinoma
-
up-regulated in many cancers
-
up-regulated in many tumors
-
decline upon mitotic exit into G1
-
PLK1 is overexpressed in many clinical cancer samples
-
Plk1 mRNA, protein and activity levels begin to rise in S-phase, peaking at the G2/M transition, over-expressed in a variety of cancers
-
Plk is over-expressed in tumors of diverse origins
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T196D
-
variant containing an activating substitution
V396A
-
mutant for interaction studies with Map205
W395F
-
mutant for interaction studies with Map205
C67V/L130G
-
localizes to centrosomes and kinetochores in mitotic cells like the wild-type, is ca. 12fold less active than wild-type in the presence of ATP, both 1-NM-PP1 and 3-MB-PP1 inhibit rapidly, selectively, and reversibly its growth in a dose-dependent manner. Acute treatment during anaphase prevents recruitment of both Plk1 itself and the Rho guanine nucleotide exchange factor Ect2 to the central spindle, abolishes RhoA GTPase localization to the equatorial cortex, and suppresses cleavage furrow formation and cell division. 3-MB-PP1 elicits a more penetrant phenotype that is virtually identical to PLK1 deletion
DELTAKD
-
kinase domain deleted Plk1, residues 307-603
DELTAPlk1
-
polo box deleted Plk1, residues 1-400
EGFP-Plk1D176N
-
construct used in FRAP experiments, expressed in U2OS cells, kinase-dead mutant
EGFP-Plk1PBD
-
construct used in FRAP experiments, expressed in U2OS cells, only C-terminal PBD domain
EGFP-Plk1T210A
-
construct used in FRAP experiments, expressed in U2OS cells, nonphosphorylatable T-loop form of Plk1
EGFP-Plk1T210D
-
construct used in FRAP experiments, expressed in U2OS cells, constitutively active mutant
H538A/K540M
-
localizes at the centrosome, when wild-type Plk1 and H538A/K540M are fused to EGFP. After photobleaching recovers its signal at the centrosome following very similar kinetics as the wild-type, double mutant, no differences in centrosomal localization compared to the wild-type protein are detected
K111R
-
site-directed mutagenesis, kinase inactive mutant, overexpression blocks the centriole duplication and arrests the cells in S-phase
K52R
-
site-directed mutagenesis, kinase-defective mutant
K82M
-
mutant
K82M
-
site-directed mutagenesis, kinase-defective mutant
K82M
-
site-directed mutagenesis, kinase-defective Plk1 mutant
K82M
-
kinase defective mutant
K82M
-
Plk1 kinase-dead mutant
K82M
-
kinase-deficient PLK1
PBD
-
polo box domain, residues 401-603
PLK1-C
-
construct comprising amino acids 305-603
PLK1-N
-
construct comprising amino acids 1-300
PLK1-PBD H538A/K540M
-
PLK1 polo box domain double mutant, constructed for the determination of the specifity of the association of PLK1 with MAVS
PLK1-PBD W414F/H538A/K540M
-
PLK1 polo box domain triple mutant, constructed for the determination of the specifity of the association of PLK1 with MAVS
PLK4_1-285
Q00444
fragment, kinase domain only
PLK4_1-367_K41M
Q00444
N-terminal fragment that possesses a mutation within the catalytic domain
S137D
-
constitutively active mutant
S285A
Q00444
mutant
S305A
Q00444
mutation of the autophosphorylation site
S305E
Q00444
mutation of the autophosphorylation site
T210D
-
site-directed mutagenesis, constitutively active mutant, overrides the irradiation-induced DNA damage and inhibition of centrosome separation in contrast to the wild-type enzyme
T210D
-
site-directed mutagenesis, hyperactive Plk1 mutant, shows reduced activity with truncated Pin1 compared to the wild-tpe Plk1
T210D
-
expression at low levels, no crystals obtained
T210D
-
constitutively active mutant
T210D
-
variant containing an activating substitution
T210D
-
hyperactive mutant
T210D
-
mutation in sequence of full-lenght construct
T210V
-
mutant, crystals obtained
T210V
-
mutation in sequence of full-lenght construct
T289A
Q00444
mutant
T82A
-
site-directed mutagenesis
W414F
-
abolishes molecular recognition and diminishes centrosomal localization, mutation abolishes polo box domain target peptide binding and reduces EGFP-Plk1 centrosomal localization
N209A
-
Cdc5KD, kinase-dead mutant
W565R
-
single point mutation within the PB1 motif of the highly conserved polo box domain, mutant exhibits a temperature-sensitive growth defect
SmPlk1DK
Q5UES2
dead kinase version of SmPlk1, obtained by replacing the D166FG168 active motif by a D166NA168 inactive motif
SmPlk1T182D
Q5UES2
constitutively active mutant
SmPlk1T182D-DK
Q5UES2
double mutant
SmPlk1T182V
Q5UES2
inactive mutant
D181N
-
site-directed mutagenesis, mutation of the kinase domain, no complementation by plo1
D181R
-
site-directed mutagenesis, mutation of the kinase domain, no complementation by plo1
D623A/H624A/K625A
-
site-directed mutagenesis, mutation of polo box 3, mutant strain shows reduced mitotic activity, no complementation by plo1
E139K
-
site-directed mutagenesis, mutation in the kinase domain, mutant enzyme is fully active with histone H1 kinase
E193V
-
site-directed mutagenesis, mutation of the kinase domain, no complementation by plo1
F518A/N519A
-
site-directed mutagenesis, mutation of polo box 1, mutant strain shows reduced mitotic activity
G505A
-
site-directed mutagenesis, mutation of polo box 1, mutant strain shows reduced mitotic activity
K69R
-
site-directed mutagenesis, mutation of the kinase domain, mutant is catalytically inactive, no complementation by plo1
S402A
-
site-directed mutagenesis, no phosphorylation of the mutant by the stress response machinery, leading to delay in cell tip growth and cell division
T197V
-
site-directed mutagenesis, mutation of the kinase domain, no complementation by plo1
W49F
-
site-directed mutagenesis, mutation of polo box 1, mutant strain shows reduced mitotic activity
Y506A/Q507A/L508A
-
site-directed mutagenesis, mutation of polo box 1, mutant strain shows reduced mitotic activity, no complementation by plo1
F561A
-
mutation does not affect kinase activity, the mutant enzyme is correctly localized to the anterior tip of the new flagellum attachment zone
H710A
-
mutation does not affect kinase activity, the mutant enzyme is correctly localized to the anterior tip of the new flagellum attachment zone
K70R
-
no kinase activity
N169A
-
abrogates kinase activity, after PLK depletion the single kinetoplast is predominantly located between the two divided nuclei
T198A
-
mutation disrupts the ability to phosphorylate the in vitro substrate TbCentrin2
T198D
-
kinase activity of the mutant enzyme is several-fold higher than that of wild-type enzyme
T201A
-
mutation disrupts the ability to phosphorylate the in vitro substrate TbCentrin2
T201D
-
kinase activity of the mutant enzyme is several-fold higher than that of wild-type enzyme
W557F
-
mutation does not affect kinase activity, the mutant enzyme is correctly localized to the anterior tip of the new flagellum attachment zone
N166A
-
kinase dead mutant
additional information
-
constructed mutant cells deficient in Cdc5p are blocked early in nuclear division with very short spindles and unseparated chromatin, the cell cycle defective mutants show also formation of hyphal-like filaments under yeast growth conditions
L408A
-
mutant for interaction studies with Map205
additional information
-
male homozygous polo mutant flies die in the third instar larval stage, heterozygous mutants show affected centromer dissociation of MEI-S332, but not association resulting in chromosome segragation defects
additional information
-
mutant phenotype analysis
K82R
-
myc-tagged kinase inactive mutant
additional information
-
construction of an kinase-active deletion mutant lacking 32 amino acids of te N-terminus
additional information
-
construction of Plk1 deletion mutants comprising residues 1-480, 1-330, or 1-408, deletion mutant 1-330 shows no kinase activity
additional information
-
down-regulation of Plk1 by expression of hairpin shRNA results in increased Pin1 ubiquitination and to down-regulation of pin 1 levels during mitosis
additional information
-
enzyme depletion using the vector-based small interfering RNA technique, Plk1 depletion leads to highly inhibited cell proliferation, decreased viability, and results in cell-cycle arrest with 4 n DNA content, formation of dumbbell-like chromatin structure due to impaired sister chromatin separation, induction of apoptosis, the apoptotic effect is reversible by co-transfection of murine Plk1
additional information
-
enzyme inhibition by expression of siRNA or inhibition of enzyme expression in HeLa cells reducing the the level of 3F3/2 phosphoepitope and inhibiting normal kinetochore association, overview
additional information
-
inhibition of p53 phosphorylation by Plk3 via siRNA transfection
additional information
-
overexpression of dominant negative Plk2 mtant results in abolished centriole duplication in fibroblasts and in U2OS2 cells
additional information
-
Plk1 depletion by siRNA transfection combined with Nek2 overexpression in U2OS cells
additional information
-
both copies of the PLK1 locus deleted in telomerase-immortalized human retinal pigment epithelial cells, more than 90% knockdown of Plk1 does not cause any cell cycle impairment, PLK1-null cells arrest in mitosis with immature centrosomes and monopolar spindles. Plk1 function and cell viability can be reconstituted by expressing either wildtype Plk1 or an analog-sensitive variant, the analog-sensitive variant is inhibited by 3-MB-PP1
additional information
-
EGFP-Plk1 delta400-603 mutant, lacks the polo box domain, localizes to the centrosome and displays a similar fluorescence intensity to the W414F mutant
additional information
-
homozygous deletion of PLK1 fully abrogates its function in vivo, PLK1delta/delta cells have monopolar or disorganized bipolar spindles with adjacent and immature centrosomes
additional information
-
polo-box domain mutant in which residues His 538 and Lys 540, critical for ligand binding, are changed to alanine, do not pull down BubR1 from mitotic cell lysates
additional information
-
human full-length Plk1 with the mutation T210D in the active-site loop of kinase domain
D154A
-
kinase-inactive mutant enzyme
additional information
-
in mutant cells in which the Cdc5 promoter is exchanged for the Clb2 promoter, the enzyme is degradated during G1 phase and is absent in meiosis, Cdc5-depleted cells progress through premeiotic S phase and enter metaphase I but arrest in metaphase I, mechanism
additional information
-
overexpression of Cdc5 leads to Cdc14 release from the nucleolus in S-phase-arrested cells
additional information
-
overexpression of mutant or wild-type Cdc5 results in multinucleated cells, Cdc5 overexpression overrides checkpoint-induced cell cycle arrest, Cdc5-defective mutant protein suppresses a Rad53 checkpoint defect
additional information
-
mutants lacking Cdc5, contractile actin ring assembly is impaired
additional information
-
several yeast Cdc5-mutant strains are used
L577A
-
site-directed mutagenesis, mutation of polo box 2, mutant strain shows reduced mitotic activity
additional information
-
construction of C-terminal deletions, the deletion mutants comprise residues 1-633, 1-583, and 1-483, no complementation of the mutants by plo1
additional information
-
generation of temperature-sensitive mutants of Plo1 which are inactivated at 35C for 4 h, Plo1 activity is abolished in Cut12 loss-of-function mutant cells, but is increased in Cut12 gain-of-function mutant cells
additional information
-
overexpression of Plo1 results in formation of multiple septa without nuclear division
K712A
-
mutation does not affect kinase activity, the mutant enzyme is correctly localized to the anterior tip of the new flagellum attachment zone
additional information
-
deletion of the C-terminal polo-box domain abolishes localization of polo-like kinase
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the development of an ELISA-based Plk1 assay is described that employs a principle to rapidly and accurately quantify the Plk1 activity with high sensitivity and specificity
drug development
-
promoter of PLK is an esophageal tumor-specific promoter and may serve as useful tool in the establishment of a transcriptional targeting strategy for esophageal cancer gene therapy
drug development
-
roles of Plk1 in cell cycle progression and in mitosis, role for Plk1 in the activation of the CDK1-Cyclin B complex. Plk1 is required not only to obtain, but also to maintain, chromosome bi-orientation on the mitotic spindle, use of BI 2536, a small-molecule inhibitor of Plk1, as an analytical tool and potential cancer therapeutic
medicine
-
correlation between Plk1 overexpression in tumors and poor patient prognosis, Plk1 acts at multiple discrete steps throughout late G2 phase, mitosis, and cytokinesis, triggers activation of the Ect2-RhoA network
medicine
-
in the study Plk1 is detected in 63.6% of Non-Hodgkin's Lymphoma cases and overexpression is positively linked to systemic symptom, elevated LDH level and higher IDI scores, Plk1 may be a new target in NHL therapy
medicine
-
Plk1 is a target for the development of anticancer therapeutics
medicine
-
Plks are targets for the development of anticancer therapeutics
medicine
-
GSK461364A is broadly antiproliferative for tumor cell lines in vitro and efficacious in multiple in vivo tumor models
medicine
-
it is possible that targeting PLK1 will enhance host innate immune responsees, leading to a novel strategy of clearing paramyxovirus infections quickly
medicine
-
knockdown of plk1 results in sensitization of multidrug resistant cells to doxorubicin, and this combination of gene silencing and small drug delivery may prove useful to achieve potent therapeutic effects
medicine
-
Plk1 attracts great attention in the field of cancer therapy because it exhibits generally elevated activity in cancer cells and is a negative prognostic factor for cancer patients
medicine
-
PLK1 can be a potential therapeutic target for the treatment of osteosarcoma
medicine
-
PLK1 is a promising target for the molecular therapy of anaplastic thyroid carcinoma, ATC
medicine
-
Plk1 is a promising therapeutic target for the treatmment of cancer
medicine
-
Plk1 is recognized as an attractive therapeutic target in the treatment of proliferative diseases
medicine
-
Plk1 represents a target for anticancer therapy
medicine
-
polo-like kinase may represent a novel drug target in imatinib-sensitive and imatinib-resistant chronic myeloid leukemia
medicine
-
polo-like kinases represent an attractive target for cancer treatment through interference with the cell cycle
medicine
-
targeting Plk1 might be a promising approach for cancer therapy
medicine
-
targeting Plk1 will cause mitotic catastrophe, with significant cytotoxicity both in vitro and in vivo, underscoring the important therapeutic opportunity of Plk1 in nasopharyngeal cancer
medicine
-
the data demonstrate the function of Plk1 as a regulator of interferon induction and provide the basis for the development of inhibitors preventing the PLK1/MAVS association to sustain innate immunity
medicine
-
the skin is an attractive tissue for Plk1 based cancer chemoprevention and chemotherapeutic applications
medicine
-
good target in tumor therapy
medicine
-
overexpression of Plk1 is strongly correlated with aggressiveness and prognosis of many cancers, so Plk1 is a potential target for anticancer therapy
medicine
-
Plk1 is a target for the development of anticancer therapeutics
medicine
-
inhibition of PLK1 activity in cancer cells causes mitotic arrest and finally induces strong cell-killing effect
medicine
-
Plk1 may be a useful target for cancer chemoprevention
analysis
-
the development of an ELISA-based Plk1 assay is described that employs a principle to rapidly and accurately quantify the Plk1 activity with high sensitivity and specificity
medicine
-
Plk1 is a target for the development of anticancer therapeutics
additional information
-
only one polo kinase found, is a master mitotic regulator, involved in the regulation of mitotic entry, the metaphase to anaphase transition, mitotic exit and cytokinesis
medicine
-
therapeutic target for Parkinson's disease
additional information
-
late mitotic function of Plk1, kinase activity of Plk1 is needed for an early event in cytokinesis, acts upstream of RhoA, Plk1 activity is required for the equatorial localization of RhoA and its effectors during anaphase
additional information
-
Plk1 controls both spindle elongation and cytokinesis, coordinates chromosome segregation with cytokinesis through its dual control of anaphase B and contractile ring assembly
additional information
-
Plk1 facilitates chromosome alignment during prometaphase through BubR1, Plk1 is necessary for not only proper spindle assembly but also the formation of functional kinetochore-microtubule attachments
additional information
-
Plk1 functions during mitosis and cytokinesis
additional information
-
Plk1 has specific functions in Emi1 degradation, activation of Cdk1-cyclin B, cohesin release, centrosome function, and regulation of microtubule-kinetochore attachments, Plk1 is not required for prophase entry, but is required for timely entry into prometaphase
additional information
-
Plk1 is responsible for causing mitotic BubR1 upshift, and attribute a kinetochore-specific function to the hyperphosphorylated form of BubR1 in the stabilization of kinetochore-microtubule interactions
additional information
-
Plk2 is expressed earlier in the cell cycle, Plk3 is expressed earlier in the cell cycle, regulates entry into S phase, attenuates cyclin E expression through a post transcriptional mechanism, it must be a critical regulator of G1 events
additional information
-
RhoA and Plk1 physically interact, their interaction appears to be enhanced during mitosis, Plk1 may alter activation of RhoA during mitotic cytokinesis
additional information
-
temporal control of HsCdc14A phosphatase activity by PLK1 is essential for chromosome segregation in mitosis
additional information
-
with respect to both substrate and ATP-site specificity, highest similarity is between PLK2 and PLK3, PLK1 is next most similar, and PLK4 is least similar
drug development
-
BI 2536 is well tolerated
additional information
-
Plk1 may regulate cell cycle progression of mouse fertilized eggs by means of inhibiting the phosphorylation of Tyr15 of Cdc2
additional information
-
Cdc5 is required to establish contractile actin ring assembly and to maintain it. Cdc5 controls the targeting and activation of Rho1 at the division site via Rho1 guanine nucleotide exchange factors Tus1 and Rom2
additional information
-
Cdc5p is required for the production of key mitotic regulators
additional information
-
only one polo kinase found, is a master mitotic regulator, involved in the regulation of mitotic entry, the metaphase to anaphase transition, mitotic exit and cytokinesis
medicine
Q5UES2
potential new target against schistosomiasis
additional information
-
role for PLK kinase activity in basal body and kinetoplast migration, PLK is essential for cytokinesis furrow ingression in bloodstream-form Trypanosoma brucei
additional information
-
is an essential factor for Ca2+-induced meiotic exit
additional information
-
Plx1 is required for M phase specific telomere binding of TRF1, is required for efficient loading of TRF1 to mitotic chromatin