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Information on EC 2.7.11.21 - polo kinase and Organism(s) Mus musculus and UniProt Accession Q60806

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     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.11 Protein-serine/threonine kinases
                2.7.11.21 polo kinase
IUBMB Comments
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 .
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Mus musculus
UNIPROT: Q60806
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
polo-like kinase 1, polo-like kinase, plk-1, polo kinase, polo-like kinase 4, polo-like kinase-1, tbplk, plk1 kinase, cdc5p, polo-like kinase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytokine-inducible serine/threonine-protein kinase
-
FGF-inducible kinase
-
-
-
-
polo related kinase
-
Polo-like kinase 1
-
-
polo-like kinase 2
-
polo-like kinase 4
-
polo-like kinase 5
-
Proliferation-related kinase
-
-
-
-
serine/threonine-protein kinase PLK
-
serine/threonine-protein kinase SNK
-
SMK/PLK-AKIN kinase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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].
CAS REGISTRY NUMBER
COMMENTARY hide
149433-93-2
Polo kinase
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
ATP + BubR1
ADP + phosphorylated BubR1
show the reaction diagram
-
Plk1 is responsible for the hyperphosphorylation of BubR1 during prometaphase
-
-
?
ATP + casein
ADP + phosphorylated casein
show the reaction diagram
-
-
-
-
?
ATP + Cdc25
ADP + phosphorylated Cdc25
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 + cohesin
ADP + phosphorylated cohesin
show the reaction diagram
-
-
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
show the reaction diagram
-
-
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
show the reaction diagram
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + Wee1
ADP + phosphorylated Wee1
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
ATP + protein
ADP + phosphoprotein
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
BI 2536
-
-
RNAi
-
specific down-regulation of Plk1
-
scytonemin
shRNA
-
inhibits G2/M transition, cleavage rate decreases and phosphorylation level of Tyr15 of Cdc2 increases
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
basic fibroblast growth factor
bFGF, extracellular stimuli to induce NS-1 cell differentiation
-
dibutyryl cAMP
dbcAMP, extracellular stimuli to induce NS-1 cell differentiation
forskolin
extracellular stimuli to induce NS-1 cell differentiation
interleukin-6
IL-6, extracellular stimuli to induce NS-1 cell differentiation
nerve growth factor
NGF, extracellular stimuli to induce NS-1 cell differentiation
-
pituitary adenylate cyclase-activating polypeptide 38
PACAP38, extracellular stimuli to induce NS-1 cell differentiation
-
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
scytonemin
Mus musculus
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
activity assay
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
heterozygosity of Plk4 does not lead to polyploidization and centrosome amplification
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLK3_MOUSE
631
0
70012
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
-
determined by SDS-PAGE and Western Blot analysis
72000
determined by SDS-PAGE and Western Blot analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D154A
kinase-inactive mutant enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
kinase-active Plk4 is inherently unstable and targeted for degradation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nucleoli are prepared from NIH3T3 cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the vector pEGFP-C1 for transfection of NIH3T3 and HEK-293 cells
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Plk is over-expressed in tumors of diverse origins
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chase, D.; Feng, Y.; Hanshew, B.; Winkles, J.A.; Longo, D.L.; Ferris, D.K.
Expression and phosphorylation of fibroblast-growth-factor-inducible kinase (Fnk) during cell-cycle progression
Biochem. J.
333
655-660
1998
Mus musculus (Q60806)
-
Manually annotated by BRENDA team
Donohue, P.J.; Alberts, G.F.; Guo, Y.; Winkles, J.A.
Identification by targeted differential display of an immediate early gene encoding a putative serine/threonine kinase
J. Biol. Chem.
270
10351-10357
1995
Mus musculus (Q60806), Mus musculus
Manually annotated by BRENDA team
Hamanaka, R.; Maloid, S.; Smith, M.R.; O'Connell, C.D.; Longo, D.L.; Ferris, D.K.
Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase
Cell Growth Differ.
5
249-257
1994
Homo sapiens (P53350), Homo sapiens, Mus musculus (Q07832), Mus musculus
Manually annotated by BRENDA team
Lake, R.J.; Jelinek, W.R.
Cell cycle- and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase
Mol. Cell. Biol.
13
7793-7801
1993
Homo sapiens (P53350), Mus musculus (Q07832)
Manually annotated by BRENDA team
Simmons, D.L.; Neel, B.G.; Stevens, R.; Evett, G.; Erikson, R.L.
Identification of an early-growth-response gene encoding a novel putative protein kinase
Mol. Cell. Biol.
12
4164-4169
1992
Mus musculus (P53351)
Manually annotated by BRENDA team
Clay, F.J.; McEwen, S.J.; Bertoncello, I.; Wilks, A.F.; Dunn, A.R.
Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila
Proc. Natl. Acad. Sci. USA
90
4882-4886
1993
Mus musculus (Q07832)
Manually annotated by BRENDA team
Fode, C.; Motro, B.; Yousefi, S.; Heffernan, M.; Dennis, J.W.
Sak, a murine protein-serine/threonine kinase that is related to the Drosophila polo kinase and involved in cell proliferation
Proc. Natl. Acad. Sci. USA
91
6388-6392
1994
Mus musculus (Q64702), Mus musculus
Manually annotated by BRENDA team
Plyte, S.; Musacchio, A.
PLK1 inhibitors: setting the mitotic death trap
Curr. Biol.
17
R280-R283
2007
Mus musculus, Homo sapiens (P53350), Homo sapiens
Manually annotated by BRENDA team
Matsumura, S.; Toyoshima, F.; Nishida, E.
Polo-like kinase 1 facilitates chromosome alignment during prometaphase through BubR1
J. Biol. Chem.
282
15217-15227
2007
Mus musculus, Homo sapiens (P53350)
Manually annotated by BRENDA team
Zhang, Z.; Su, W.H.; Feng, C.; Yu, D.H.; Cui, C.; Xu, X.Y.; Yu, B.Z.
Polo-like kinase 1 may regulate G2/M transition of mouse fertilized eggs by means of inhibiting the phosphorylation of Tyr 15 of Cdc2
Mol. Reprod. Dev.
74
1247-1254
2007
Mus musculus
Manually annotated by BRENDA team
Lu, L.Y.; Wood, J.L.; Minter-Dykhouse, K.; Ye, L.; Saunders, T.L.; Yu, X.; Chen, J.
Polo-like kinase 1 is essential for early embryonic development and tumor suppression
Mol. Cell. Biol.
28
6870-6876
2008
Mus musculus
Manually annotated by BRENDA team
Draghetti, C.; Salvat, C.; Zanoguera, F.; Curchod, M.L.; Vignaud, C.; Peixoto, H.; Di Cara, A.; Fischer, D.; Dhanabal, M.; Andreas, G.; Abderrahim, H.; Rommel, C.; Camps, M.
Functional whole-genome analysis identifies polo-like kinase 2 and poliovirus receptor as essential for neuronal differentiation upstream of the negative regulator alphaB-crystallin
J. Biol. Chem.
284
32053-32065
2009
Mus musculus (P53351)
Manually annotated by BRENDA team
Andrysik, Z.; Bernstein, W.Z.; Deng, L.; Myer, D.L.; Li, Y.Q.; Tischfield, J.A.; Stambrook, P.J.; Bahassi, E.M.
The novel mouse Polo-like kinase 5 responds to DNA damage and localizes in the nucleolus
Nucleic Acids Res.
38
2931-2943
2010
Homo sapiens, Mus musculus (Q4FZD7), Mus musculus
Manually annotated by BRENDA team
Park, J.E.; Li, L.; Park, J.; Knecht, R.; Strebhardt, K.; Yuspa, S.H.; Lee, K.S.
Direct quantification of polo-like kinase 1 activity in cells and tissues using a highly sensitive and specific ELISA assay
Proc. Natl. Acad. Sci. USA
106
1725-1730
2009
Mus musculus, Homo sapiens (P53350), Homo sapiens
Manually annotated by BRENDA team
Holland, A.J.; Lan, W.; Niessen, S.; Hoover, H.; Cleveland, D.W.
Polo-like kinase 4 kinase activity limits centrosome overduplication by autoregulating its own stability
J. Cell Biol.
188
191-198
2010
Mus musculus (Q64702)
Manually annotated by BRENDA team
Holland, A.J.; Fachinetti, D.; Da Cruz, S.; Zhu, Q.; Vitre, B.; Lince-Faria, M.; Chen, D.; Parish, N.; Verma, I.M.; Bettencourt-Dias, M.; Cleveland, D.W.
Polo-like kinase 4 controls centriole duplication but does not directly regulate cytokinesis
Mol. Biol. Cell
23
1838-1845
2012
Homo sapiens (O00444), Homo sapiens, Mus musculus (Q64702), Mus musculus
Manually annotated by BRENDA team