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Information on EC 2.7.11.36 - MASTL-subfamily protein kinase
for references in articles please use BRENDA:EC2.7.11.36
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.11 Protein-serine/threonine kinases
2.7.11.36 MASTL-subfamily protein kinase
IUBMB Comments
Requires Mg2+. Peptide array data suggest that MASTL prefers to phosphorylate Ser over Thr, followed at position +1 by a bulky hydrophobic (Met, Leu, Phe or Tyr) and with an aromatic residue in the -2 position . Its main role in animal systems is in the regulation of mitosis by phosphorylating a conserved site on endosulfine family proteins (ENSA and ARPP-19 in human), causing them to inhibit the protein phosphatase 2A-B55 [protein phosphatase 2A (PP2A) holoenzyme complex containing a B55-family regulatory subunit] .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
show+
[endosulfine family protein]-L-serine
=
+
[endosulfine family protein]-O-phospho-L-serine
+
[endosulfine family protein]-L-threonine
=
+
[endosulfine family protein]-O-phospho-L-threonine
Synonyms
FLJ14813, Great wall kinase, Greatwall, greatwall kinase, gwl, MASTL, MASTL-subfamily-protein-kinase, microtubule associated serine/threonine kinase, microtubule associated serine/threonine like kinase gene, microtubule-associated (MASTL)-subfamily-protein kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Greatwall
greatwall kinase
gwl
MASTL
microtubule-associated (MASTL)-subfamily-protein kinase
-
-
-
-
RIM15
greatwall kinase
-
-
-
-
gwl
-
-
-
-
MASTL
-
-
-
-
RIM15
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [endosulfine family protein]-L-serine = ADP + [endosulfine family protein]-O-phospho-L-serine
(1)
-
-
-
ATP + [endosulfine family protein]-L-threonine = ADP + [endosulfine family protein]-O-phospho-L-threonine
(2)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:[endosulfine family protein] phosphotransferase (Ser/Thr-phosphorylating)
Requires Mg2+. Peptide array data suggest that MASTL prefers to phosphorylate Ser over Thr, followed at position +1 by a bulky hydrophobic (Met, Leu, Phe or Tyr) and with an aromatic residue in the -2 position [4]. Its main role in animal systems is in the regulation of mitosis by phosphorylating a conserved site on endosulfine family proteins (ENSA and ARPP-19 in human), causing them to inhibit the protein phosphatase 2A-B55 [protein phosphatase 2A (PP2A) holoenzyme complex containing a B55-family regulatory subunit] [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [endosulfine family protein]-L-serine
ADP + [endosulfine family protein]-O-phospho-L-serine
ATP + [endosulfine family protein]-L-threonine
ADP + [endosulfine family protein]-O-phospho-L-threonine
additional information
?
-
-
Substrates: the enzyme forms a complex with protein phosphatase 2A/B55 in G2 (interphase) oocytes but dissociates from the phosphatase in progesterone-treated M phase oocytes
Products: -
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ATP + Arpp19
ADP + ?
-
Substrates: the substrate is phosphorylated by this kinase on the serine residue of the KYFDSGDY consensus sequence (DSG motif)
Products: -
Products: -
?
ATP + Arpp19
ADP + ?
-
Substrates: the substrate is phosphorylated at Ser62
Products: -
Products: -
?
ATP + cAMP-regulated phosphoprotein 19
ADP + ?
-
Substrates: -
Products: -
Products: -
?
ATP + cAMP-regulated phosphoprotein 19
ADP + ?
-
Substrates: -
Products: -
Products: -
?
ATP + ENSA
ADP + ?
-
Substrates: the substrate is phosphorylated by this kinase on the serine residue of the KYFDSGDY consensus sequence (DSG motif)
Products: -
Products: -
?
ATP + ENSA
ADP + ?
-
Substrates: the substrate is phosphorylated at Ser67
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-serine
ADP + [endosulfine family protein]-O-phospho-L-serine
-
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-serine
ADP + [endosulfine family protein]-O-phospho-L-serine
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-serine
ADP + [endosulfine family protein]-O-phospho-L-serine
-
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-threonine
ADP + [endosulfine family protein]-O-phospho-L-threonine
-
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-threonine
ADP + [endosulfine family protein]-O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-threonine
ADP + [endosulfine family protein]-O-phospho-L-threonine
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [endosulfine family protein]-L-serine
ADP + [endosulfine family protein]-O-phospho-L-serine
ATP + [endosulfine family protein]-L-threonine
ADP + [endosulfine family protein]-O-phospho-L-threonine
ATP + Arpp19
ADP + ?
-
Substrates: the substrate is phosphorylated by this kinase on the serine residue of the KYFDSGDY consensus sequence (DSG motif)
Products: -
Products: -
?
ATP + Arpp19
ADP + ?
-
Substrates: the substrate is phosphorylated at Ser62
Products: -
Products: -
?
ATP + cAMP-regulated phosphoprotein 19
ADP + ?
-
Substrates: -
Products: -
Products: -
?
ATP + cAMP-regulated phosphoprotein 19
ADP + ?
-
Substrates: -
Products: -
Products: -
?
ATP + ENSA
ADP + ?
-
Substrates: the substrate is phosphorylated by this kinase on the serine residue of the KYFDSGDY consensus sequence (DSG motif)
Products: -
Products: -
?
ATP + ENSA
ADP + ?
-
Substrates: the substrate is phosphorylated at Ser67
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-serine
ADP + [endosulfine family protein]-O-phospho-L-serine
-
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-serine
ADP + [endosulfine family protein]-O-phospho-L-serine
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-serine
ADP + [endosulfine family protein]-O-phospho-L-serine
-
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-threonine
ADP + [endosulfine family protein]-O-phospho-L-threonine
-
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-threonine
ADP + [endosulfine family protein]-O-phospho-L-threonine
Substrates: -
Products: -
Products: -
?
ATP + [endosulfine family protein]-L-threonine
ADP + [endosulfine family protein]-O-phospho-L-threonine
-
Substrates: -
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R)-3,5,7-trihydroxy-2-[(2R,3S)-7-hydroxy-2-(4-hydroxy-3-methoxyphenyl)-3-hydroxymethyl-2,3-dihydrobenzofuran-5-yl]chroman-4-one
UNPD178438, silychristin
(5R)-1-[4-hydroxy-3-[(6-hydroxy-2-naphthyl)methoxy]phenyl]-5-(methylaminomethoxy)octan-3-one
ZINC85597499
2-[1-[4-(dimethylamino)phenyl]tetrazol-5-yl]sulfanyl-N-(4-propan-2-ylphenyl)acetamide
ZINC01029685; ZINC77292085
2-[4-[(1H-pyrazol-1-yl)methyl]phenyl]-3,5,6,8-tetrahydro-4H-thiopyrano[4',3':4,5]thieno[2,3-d]pyrimidin-4-one
ZINC53845290
3-[2-[5-hydroxy-3-methoxy-4-methyl-2-(3-methylbut-2-enyl)phenyl]ethyl]benzene-1,2-diol
ZINC14679203
4-(3,7-dimethyl-6-hydroxy-2,7-octadienyl)-1,3,5,8-tetrahydroxyxanthone
UNPD218939, garcihombronone B
phenylethenyl-1,4,6,7-tetrahydropyrazolo[4,3-c] pyridin-5-yl]-3-thiophen-2-ylpropan-1-one
ZINC20201746
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme relocalizes in part from nucleus to centrosomes in mitosis, when it is active
brenda
-
the enzyme translocates from the nucleus to the cytoplasm in prophase
brenda
-
the enzyme localizes to the nucleus and disperses into cytoplasm during germinal vesicle breakdown
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
When overexpressed, the enzyme induces activation of Gsk3 kinase which phosphorylates the PHLPP phosphatase involved in the dephosphorylation and inactivation of Akt on its Ser473 activating site
physiological function
malfunction
enzyme depletion from mitotic extracts rapidly lowers maturation promoting factor activity due to the accumulation of inhibitory phosphorylations on Cdc2 kinase. Enzyme depletion similarly prevents cycling extracts from entering M phase
malfunction
-
yeast cells lacking the enzyme are hypersensitive to acetic acid and are even unable to survive with the treatment with 5 g/l acetic acid
malfunction
-
enzyme deletion reverses life span extension associated with deficiencies in Sch9, Tor1, or Ras2
malfunction
-
immunodepletion of the enzyme increases the DNA damage response to damaged DNA
malfunction
-
cells strongly depleted of the enzyme by RNAi delay in G2 phase and reveal slow chromosome condensation. Enzyme RNAi cells that enter and progress through mitosis often fail to completely separate their sister chromatids in anaphase. This causes chromatin to be trapped in the cleavage furrow, which may lead to the formation of 4N G1 cells by cytokinesis failure. Cyclin B1 destruction is incomplete when mitotic cells that are strongly depleted of the enzyme exit mitosis
malfunction
-
enzyme downregulation or overexpression of catalytically-inactive enzyme inhibits partial meiotic maturation of mouse oocytes
malfunction
-
a transient knockdown of the enzyme in zebrafish results in deficiency of circulating thrombocytes, correlating with a decrease in the expression of the thrombopoietin receptor, c-mpl, and the CD41 platelet adhesion protein, GpIIb, but has no effect on essential housekeeping zebrafish gene, EF1alpha
malfunction
-
yeast cells lacking the enzyme are hypersensitive to acetic acid and are even unable to survive with the treatment with 5 g/l acetic acid
-
malfunction
Saccharomyces cerevisiae DBY746
-
enzyme deletion reverses life span extension associated with deficiencies in Sch9, Tor1, or Ras2
-
physiological function
-
the nucleo-cytoplasmic regulation of the enzyme is essential for its functions in vivo. The spatial regulation of the enzyme at mitotic entry contributes to the mitotic switch
physiological function
-
the enzyme is required for proper chromosome condensation. The enzyme helps activate cell cycle regulators that prepare interphase cells for entry into mitosis. The enzyme is needed to establish high cyclin B-CDK activity during mitotic entry
physiological function
-
enzyme-mediated phosphorylation of cAMP-regulated phosphoprotein 19 and alpha-endosulfine turns these proteins into potent inhibitors of protein phosphatase 2A-B55, thereby promoting a correct timing and progression of mitosis. Besides the enzyme's primordial role in mitotic division, it also contributes in a significant extent to tumorigenic processes. The enzyme also participates in the DNA damage checkpoint and/or response
physiological function
-
the enzyme induces oocyte maturation in the absence of progesterone in a protein synthesis-dependent manner. The enzyme induces the phosphorylation of Cdc25 by several mitotic kinases. Active enzyme overrides inhibitory phosphorylations of Cdc25 at Ser287
physiological function
the enzyme participates in an autoregulatory loop that generates and maintains sufficiently high maturation promoting factor activity levels to support mitosis. The enzyme maintains M phase by preventing inhibitory phosphorylations on Cdc2. The enzyme is also required for mitotic entry
physiological function
-
the enzyme is involved in Arpp19/ENSA phosphorylation and subsequent protein phosphatase 2A-B55 inhibition
physiological function
-
the enzyme plays a role in the regulation of mitotic division and is required for DNA checkpoint recovery
physiological function
-
the enzyme functions together with transcriptional factor Yap1 in regulating acetic acid stress-induced genes, which requires enzyme kinase activity. The enzyme improves H2O2 stress tolerance through antioxidant systems
physiological function
-
the enzyme plays a role in the regulation of mitotic division and is required for DNA checkpoint recovery
physiological function
-
the enzyme plays a role in the regulation of mitotic division and is required for DNA checkpoint recovery
physiological function
-
the enzyme plays a role in the regulation of mitotic division and is required for DNA checkpoint recovery
physiological function
-
the enzyme is required for yeast chronological life span extension caused by deficiencies in Ras2, Tor1, and Sch9, and by calorie restriction. The Ras/cAMP/PKA/Rim15/Msn2/4 and the Tor/Sch9/Rim15/Gis1 pathways are major mediators of the calorie restriction-dependent stress resistance and life span extension. The enzyme activates Gis1, a transcription factor that binds to the PDS element (AWAGGGAT), and induces a variety of stress response genes when cells enter stationary phase
physiological function
-
the enzyme is required to enter into and maintain mitosis. The enzyme is involved in cancer processes and DNA damage recovery. Activated enzyme phosphorylates both Arpp19 and ENSA, which associate and inhibit protein phosphatase 2A-B55. The enzyme-Arpp19/ENSA-protein phosphatase 2A-B55 pathway is essential to achieve an efficient division of cells and to maintain genomic stability
physiological function
-
the enzyme activity is essential for mitotic entry and progression. The enzyme plays a role in the upregulation of the Wnt/beta-catenin pathway and is an activator of cell contractility via the positive modulation of myocardin-related transcription factor A/serum response factor signaling
physiological function
-
the enzyme upregulates ribophagy, while it downregulates non-selective degradation of ribosomes
physiological function
-
the enzyme is a key element in the G2/M transition and helps maintain M phase through inhibition of PP2A/B55delta, the principal phosphatase for Cdk-phosphorylated substrates. The enzyme also promotes recovery from DNA damage and is itself directly inhibited by the DNA damage response. The enzyme is a regulator of DNA damage response, which plays an important role in recovery from DNA damage
physiological function
-
the enzyme enhances cyclin B1-Cdk1-dependent mitotic phosphorylation events, directing mitotic entry, anaphase and cytokinesis in human cells
physiological function
-
the enzyme is required for meiosis resumption in mouse oocytes and acts in a pathway with protein phosphatase 2A which is essential for prophase I exit and metaphase I microtubule assembly
physiological function
-
the enzyme plays a specific role in the development of hematopoietic cells
physiological function
-
the enzyme is involved in cancer processes and DNA damage recovery. The enzyme-Arpp19/ENSA-PP2A-B55 pathway is essential to achieve an efficient division of cells and to maintain genomic stability. The enzyme phosphorylates Arpp19/ENSA inhibitors and thereby blocks PP2A-B55 activity. The enzyme is essential for entry into metaphase II or for its maintenance
physiological function
-
the enzyme functions together with transcriptional factor Yap1 in regulating acetic acid stress-induced genes, which requires enzyme kinase activity. The enzyme improves H2O2 stress tolerance through antioxidant systems
-
physiological function
Saccharomyces cerevisiae DBY746
-
the enzyme is required for yeast chronological life span extension caused by deficiencies in Ras2, Tor1, and Sch9, and by calorie restriction. The Ras/cAMP/PKA/Rim15/Msn2/4 and the Tor/Sch9/Rim15/Gis1 pathways are major mediators of the calorie restriction-dependent stress resistance and life span extension. The enzyme activates Gis1, a transcription factor that binds to the PDS element (AWAGGGAT), and induces a variety of stress response genes when cells enter stationary phase
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GWL_XENLA
887
0
98683
Swiss-Prot
other Location (Reliability: 3)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
the Polo kinase associates with and phosphorylates the enzyme, promoting its binding to 14-3-3epsilon and its localization to the cytoplasm in prophase
phosphoprotein
-
the enzyme is phosphorylated at T193, T206 and S861. Phosphorylation of enzyme C-tail turn motif (S861) is dispensable for kinase function in cellulo
phosphoprotein
-
the enzyme is activated by phosphorylation. Several phosphatases such as PP1, PP2A-B55 and FCP1 are required to control the dephosphorylation and inactivation of the enzyme and a properly regulated mitotic exit
phosphoprotein
-
only the phosphorylation of the tail/linker site, located outside the putative T loop, is essential for enzyme activation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F863A
-
the mutation decreases the enzyme activity by 71% compared to the wild type enzyme
G44S
-
the mutation decreases the enzyme activity by 95% compared to the wild type enzyme
G825A
-
the mutation does not change either kinase activity or the capacity to maintain mitosis
K39A
-
the mutation decreases the enzyme activity by 17% compared to the wild type enzyme
K48A
-
the mutation decreases the enzyme activity by 47% compared to the wild type enzyme
K48A/K62A
-
the mutation decreases the enzyme activity by 82% compared to the wild type enzyme
K48A/K65A
-
the mutations decrease the enzyme activity by more than 80% compared to the wild type enzyme
K62A
-
the mutation decreases the enzyme activity by 92% compared to the wild type enzyme
K65A
K71M
-
the cognate Scant Greatwall mutation K71M has sufficient constitutive kinase activity to promote M phase in Xenopus oocytes. M phase induction by Scant Greatwall requires protein synthesis but is not associated with altered binding or release of PP2A/B55 as compared to wild type enzyme
K830A
-
the mutation does not change either kinase activity or the capacity to maintain mitosis
P849A
-
the mutation decreases the enzyme activity by 34% compared to the wild type enzyme
P849A/P852A
-
the mutation decreases the enzyme activity by about 90% compared to the wild type enzyme
P852A
-
the mutation decreases the enzyme activity by 76% compared to the wild type enzyme
T741A
-
the mutation decreases the enzyme activity by 78% compared to the wild type enzyme
W840A
-
the mutation decreases the enzyme activity by 57% compared to the wild type enzyme
K65A
-
the mutation decreases the enzyme activity by 7% compared to the wild type enzyme
K65A
-
the mutation decreases the enzyme activity by about 10% compared to the wild type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Sf9 insect cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is expressed at a constant level during the prophase I to metaphase II transition and becomes hyperphosphorylated at the time of Cdc2-cyclin B activation
-
the enzyme is upregulated in epatocarcinoma, neuroblastoma, head and neck squamous cell carcinoma, as well as breast, gastric, and colorectal cancers
-
the enzyme is upregulated in various cancers including breast, prostate and oral cancers
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
the enzyme is a therapeutic target for several cancers, such as acute myeloid leukemia, head and neck squamous cell carcinoma, and thyroid carcinoma
medicine
the enzyme's association with poor patient survival establishes it as an important drug target in cancer therapy
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, X.Q.; Yuan, B.; Zhang, F.L.; Liu, C.G.; Auesukaree, C.; Zhao, X.Q.
Novel roles of the greatwall kinase Rim15 in yeast oxidative stress tolerance through mediating antioxidant systems and transcriptional regulation
Antioxidants (Basel)
13
260
2024
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Goguet-Rubio, P.; Amin, P.; Awal, S.; Vigneron, S.; Charrasse, S.; Mechali, F.; Labbe, J.; Lorca, T.; Castro, A.
PP2A-B55 holoenzyme regulation and cancer
Biomolecules
10
1586
2020
Homo sapiens
brenda
Waliullah, T.M.; Yeasmin, A.M.; Kaneko, A.; Koike, N.; Terasawa, M.; Totsuka, T.; Ushimaru, T.
Rim15 and Sch9 kinases are involved in induction of autophagic degradation of ribosomes in budding yeast
Biosci. Biotechnol. Biochem.
81
307-310
2017
Saccharomyces cerevisiae
brenda
Voets, E.; Wolthuis, R.M.
MASTL is the human orthologue of Greatwall kinase that facilitates mitotic entry, anaphase and cytokinesis
Cell Cycle
9
3591-3601
2010
Homo sapiens
brenda
Peng, A.; Yamamoto, T.M.; Goldberg, M.L.; Maller, J.L.
A novel role for greatwall kinase in recovery from DNA damage
Cell Cycle
9
4364-4369
2010
Xenopus laevis
brenda
Velmurugan Ilavarasi, A.; Mohanty, S.; Katike, U.; Patidar, I.; Venkatesan, A.; Ampasala, D.
Structure-based virtual screening for the identification of novel Greatwall kinase inhibitors
Comput. Methods Drug Discov. Repurpos. Cancer Ther.
2023
101-116
2023
Homo sapiens (Q96GX5)
-
brenda
Zhao, X.; Yu, D.; Feng, C.; Deng, X.; Wu, D.; Jin, M.; Wang, E.; Wang, X.; Yu, B.
Role of Greatwall kinase in release of mouse oocytes from diplotene arrest
Dev. Growth Differ.
56
669-678
2014
Mus musculus
brenda
Johnson, H.J.; Gandhi, M.J.; Shafizadeh, E.; Langer, N.B.; Pierce, E.L.; Paw, B.H.; Gilligan, D.M.; Drachman, J.G.
In vivo inactivation of MASTL kinase results in thrombocytopenia
Exp. Hematol.
37
901-908
2009
Danio rerio
brenda
Vigneron, S.; Robert, P.; Hached, K.; Sundermann, L.; Charrasse, S.; Labbe, J.C.; Castro, A.; Lorca, T.
The master Greatwall kinase, a critical regulator of mitosis and meiosis
Int. J. Dev. Biol.
60
245-254
2016
Mus musculus
brenda
Erguven, M.; Kilic, S.; Karaca, E.; Diril, M.K.
Genetic complementation screening and molecular docking give new insight on phosphorylation-dependent Mastl kinase activation
J. Biomol. Struct. Dyn.
41
8241-8253
2023
Mus musculus
brenda
Yu, J.; Fleming, S.L.; Williams, B.; Williams, E.V.; Li, Z.; Somma, P.; Rieder, C.L.; Goldberg, M.L.
Greatwall kinase a nuclear protein required for proper chromosome condensation and mitotic progression in Drosophila
J. Cell Biol.
164
487-492
2004
Drosophila melanogaster
brenda
Wang, P.; Galan, J.A.; Normandin, K.; Bonneil, E.; Hickson, G.R.; Roux, P.P.; Thibault, P.; Archambault, V.
Cell cycle regulation of Greatwall kinase nuclear localization facilitates mitotic progression
J. Cell Biol.
202
277-293
2013
Drosophila melanogaster
brenda
Castro, A.; Lorca, T.
Greatwall kinase at a glance
J. Cell Sci.
131
jcs222364
2018
Homo sapiens
brenda
Zhao, Y.; Haccard, O.; Wang, R.; Yu, J.; Kuang, J.; Jessus, C.; Goldberg, M.L.
Roles of Greatwall kinase in the regulation of Cdc25 phosphatase
Mol. Biol. Cell
19
1317-1327
2008
Xenopus laevis
brenda
Yamamoto, T.M.; Blake-Hodek, K.; Williams, B.C.; Lewellyn, A.L.; Goldberg, M.L.; Maller, J.L.
Regulation of Greatwall kinase during Xenopus oocyte maturation
Mol. Biol. Cell
22
2157-2164
2011
Xenopus laevis
brenda
Vigneron, S.; Gharbi-Ayachi, A.; Raymond, A.A.; Burgess, A.; Labbe, J.C.; Labesse, G.; Monsarrat, B.; Lorca, T.; Castro, A.
Characterization of the mechanisms controlling Greatwall activity
Mol. Cell. Biol.
31
2262-2275
2011
Xenopus laevis
brenda
Yu, J.; Zhao, Y.; Li, Z.; Galas, S.; Goldberg, M.L.
Greatwall kinase participates in the Cdc2 autoregulatory loop in Xenopus egg extracts
Mol. Cell
22
83-91
2006
Xenopus laevis (Q6NTJ3)
brenda
Lorca, T.; Castro, A.
The Greatwall kinase a new pathway in the control of the cell cycle
Oncogene
32
537-543
2013
Drosophila melanogaster, Homo sapiens, Saccharomyces cerevisiae, Xenopus laevis
brenda
Amin, P.; Awal, S.; Vigneron, S.; Roque, S.; Mechali, F.; Labbe, J.C.; Lorca, T.; Castro, A.
PP2A-B55 substrates and regulators in the control of cellular functions
Oncogene
41
1-14
2022
Homo sapiens
brenda
Wei, M.; Fabrizio, P.; Hu, J.; Ge, H.; Cheng, C.; Li, L.; Longo, V.D.
Life span extension by calorie restriction depends on Rim15 and transcription factors downstream of Ras/PKA, Tor, and Sch9
PLoS Genet.
4
e13
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae DBY746
brenda
Ammarah, U.; Kumar, A.; Pal, R.; Bal, N.C.; Misra, G.
Identification of new inhibitors against human Great wall kinase using in silico approaches
Sci. Rep.
8
4894
2018
Homo sapiens (Q96GX5)
brenda
Gharbi-Ayachi, A.; Labbe, J.C.; Burgess, A.; Vigneron, S.; Strub, J.M.; Brioudes, E.; Van-Dorsselaer, A.; Castro, A.; Lorca, T.
The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A
Science
330
1673-1677
2010
Homo sapiens
brenda
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