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Information on EC 2.7.11.21 - polo kinase

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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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UNIPROT: Q00444
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
polo-like kinase 1, polo-like kinase, plk-1, polo-like kinase-1, tbplk, plk1 kinase, cdc5p, polo-like kinase 4, polo-like kinase 2, polo-like kinase cdc5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FGF-inducible kinase
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-
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Proliferation-related kinase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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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
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-
-
?
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
Q00444
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
autophosphorylation of serine 305
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
kinase assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
PLK4 is a key regulator of centrosome duplication
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
HXC5_HUMAN
222
0
24976
Swiss-Prot
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
autophosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PLK4_1-285
fragment, kinase domain only
PLK4_1-367_K41M
N-terminal fragment that possesses a mutation within the catalytic domain
S285A
mutant
S305A
mutation of the autophosphorylation site
S305E
mutation of the autophosphorylation site
T289A
mutant
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
the vector pSUMO is used, an EGFP-PLK4 construct is used
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sillibourne, J.E.; Tack, F.; Vloemans, N.; Boeckx, A.; Thambirajah, S.; Bonnet, P.; Ramaekers, F.C.; Bornens, M.; Grand-Perret, T.
Autophosphorylation of polo-like kinase 4 and its role in centriole duplication
Mol. Biol. Cell
21
547-561
2010
Homo sapiens (Q00444)
Manually annotated by BRENDA team
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