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Search results 201 to 238 out of 238 for Cdc25c

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Type Details Score
Publication
22722334 | J:205471
First Author: Guo L
Year: 2012
Journal: Cell Death Differ
Title: Histone demethylase Kdm4b functions as a co-factor of C/EBPβ to promote mitotic clonal expansion during differentiation of 3T3-L1 preadipocytes.
Volume: 19
Issue: 12
Pages: 1917-27
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Publication
25740542 | J:222105
First Author: Luo YB
Year: 2015
Journal: Biol Reprod
Title: PLK4 is essential for meiotic resumption in mouse oocytes.
Volume: 92
Issue: 4
Pages: 101
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Publication
29024968 | J:245071
First Author: Chen MJ
Year: 2017
Journal: Biol Reprod
Title: Iron suppresses ovarian granulosa cell proliferation and arrests cell cycle through regulating p38 mitogen-activated protein kinase/p53/p21 pathway.
Volume: 97
Issue: 3
Pages: 438-448
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Publication
17681131 | -
First Author: Kleylein-Sohn J
Year: 2007
Journal: Dev Cell
Title: Plk4-induced centriole biogenesis in human cells.
Volume: 13
Issue: 2
Pages: 190-202
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Publication
19223768 | J:180569
First Author: Pirino G
Year: 2009
Journal: Cell Cycle
Title: Protein kinase A regulates resumption of meiosis by phosphorylation of Cdc25B in mammalian oocytes.
Volume: 8
Issue: 4
Pages: 665-70
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Publication
10926775 | J:64024
First Author: Liu D
Year: 2000
Journal: Dev Biol
Title: A role for cyclin A1 in the activation of MPF and G2-M transition during meiosis of male germ cells in mice.
Volume: 224
Issue: 2
Pages: 388-400
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Publication
19748123 | J:155237
First Author: Morse E
Year: 2009
Journal: Mol Immunol
Title: PPARalpha ligands cause lymphocyte depletion and cell cycle block and this is associated with augmented TRB3 and reduced Cyclin B1 expression.
Volume: 46
Issue: 16
Pages: 3454-61
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Publication
12352953 | -
First Author: Leung GC
Year: 2002
Journal: Nat Struct Biol
Title: The Sak polo-box comprises a structural domain sufficient for mitotic subcellular localization.
Volume: 9
Issue: 10
Pages: 719-24
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Protein
F6QIM3
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: true
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Publication
9914175 | -
First Author: Nigg EA
Year: 1998
Journal: Curr Opin Cell Biol
Title: Polo-like kinases: positive regulators of cell division from start to finish.
Volume: 10
Issue: 6
Pages: 776-83
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Publication
1660828 | -
First Author: Llamazares S
Year: 1991
Journal: Genes Dev
Title: polo encodes a protein kinase homolog required for mitosis in Drosophila.
Volume: 5
Issue: 12A
Pages: 2153-65
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Publication
10594031 | -
First Author: Song S
Year: 2000
Journal: Mol Cell Biol
Title: Essential function of the polo box of Cdc5 in subcellular localization and induction of cytokinetic structures.
Volume: 20
Issue: 1
Pages: 286-98
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Publication
12615979 | -
First Author: Reynolds N
Year: 2003
Journal: J Cell Sci
Title: Polo boxes form a single functional domain that mediates interactions with multiple proteins in fission yeast polo kinase.
Volume: 116
Issue: Pt 7
Pages: 1377-87
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Publication
22018922 | -
First Author: Harper NC
Year: 2011
Journal: Dev Cell
Title: Pairing centers recruit a Polo-like kinase to orchestrate meiotic chromosome dynamics in C. elegans.
Volume: 21
Issue: 5
Pages: 934-47
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Protein Domain
IPR000959 | POLO_box_dom
Type: Domain
Description: A subgroup of serine/threonine protein kinases, Polo or Polo-like kinases play multiple roles during the cell cycle. Polo kinases are required at several key points through mitosis, starting from control of the G2/M transition through phosphorylation of Cdc25C and mitotic cyclins. They are also involved in meiosis I as regulators of kinetochore function [, ]. Polo kinases are characterised by an amino terminal catalytic domain, and a carboxy terminal non-catalytic domain consisting of three blocks of conservedsequences known as polo boxes which form one single functional domain []. The domain is named after its founding member encoded by the polo gene of Drosophila melanogaster []. This domain of around 70 amino acids has been found in species ranging from yeast to mammals. Polo boxes appear to mediate interaction with multiple proteins through protein:protein interactions; some but not all of these proteins are substrates for the kinase domain of the molecule [].The crystal structure of the polo domain of the murine protein, Sak, is dimeric, consisting of two α-helices and two six-stranded β-sheets []. The topology of one polypeptide subunit of the dimer consists of, from its N- to C terminus, an extended strand segment, five β-strands, one α-helix (A) and C-terminal β-strand. β-strands from one subunit form a contiguous antiparallel β-sheet with β-strands from the second subunit. The two β-sheets pack with crossing angle of 110 degrees, orienting the hydrophobic surfaces inward and the hydrophilic surfaces outward. Helix A, which is colinear with β-strand 6 of the same polypeptide, buries a large portion of the non-overlapping hydrophobic β-sheet surfaces. Interactions involving helices A comprise a majority of the hydrophobic core structure and also the dimer interface.Point mutations in the Polo box of the budding yeast Cdc5 protein abolish the ability of overexpressed Cdc5 to interact with the spindle poles and to organise cytokinetic structures [].
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Protein Domain
IPR036947 | POLO_box_dom_sf
Type: Homologous_superfamily
Description: A subgroup of serine/threonine protein kinases, Polo or Polo-like kinases play multiple roles during the cell cycle. Polo kinases are required at several key points through mitosis, starting from control of the G2/M transition through phosphorylation of Cdc25C and mitotic cyclins. They are also involved in meiosis I as regulators of kinetochore function [, ]. Polo kinases are characterised by an amino terminal catalytic domain, and a carboxy terminal non-catalytic domain consisting of three blocks of conservedsequences known as polo boxes which form one single functional domain []. The domain is named after its founding member encoded by the polo gene of Drosophila melanogaster []. This domain of around 70 amino acids has been found in species ranging from yeast to mammals. Polo boxes appear to mediate interaction with multiple proteins through protein:protein interactions; some but not all of these proteins are substrates for the kinase domain of the molecule [].The crystal structure of the polo domain of the murine protein, Sak, is dimeric, consisting of two α-helices and two six-stranded β-sheets []. The topology of one polypeptide subunit of the dimer consists of, from its N- to C terminus, an extended strand segment, five β-strands, one α-helix (A) and C-terminal β-strand. β-strands from one subunit form a contiguous antiparallel β-sheet with β-strands from the second subunit. The two β-sheets pack with crossing angle of 110 degrees, orienting the hydrophobic surfaces inward and the hydrophilic surfaces outward. Helix A, which is colinear with β-strand 6 of the same polypeptide, buries a large portion of the non-overlapping hydrophobic β-sheet surfaces. Interactions involving helices A comprise a majority of the hydrophobic core structure and also the dimer interface.Point mutations in the Polo box of the budding yeast Cdc5 protein abolish the ability of overexpressed Cdc5 to interact with the spindle poles and to organise cytokinetic structures [].
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Publication
25533956 | J:216866
First Author: Kim J
Year: 2015
Journal: Nature
Title: Meikin is a conserved regulator of meiosis-I-specific kinetochore function.
Volume: 517
Issue: 7535
Pages: 466-71
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Protein
Q3TV29
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: true
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Protein
Q4FZD7
Organism: Mus musculus/domesticus
Length: 595  
Fragment?: false
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Protein
G3X967
Organism: Mus musculus/domesticus
Length: 599  
Fragment?: false
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Protein
A0A0N4SWB8
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: false
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Protein
E9Q4W7
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Protein
Q64702
Organism: Mus musculus/domesticus
Length: 925  
Fragment?: false
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Protein
P53351
Organism: Mus musculus/domesticus
Length: 682  
Fragment?: false
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Protein
Q60806
Organism: Mus musculus/domesticus
Length: 631  
Fragment?: false
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Protein
Q07832
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
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Protein
Q3UG81
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
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Protein
Q548A9
Organism: Mus musculus/domesticus
Length: 682  
Fragment?: false
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Protein
F6V5S5
Organism: Mus musculus/domesticus
Length: 610  
Fragment?: true
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Protein
I6L9A2
Organism: Mus musculus/domesticus
Length: 504  
Fragment?: false
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Protein
Q3U0L5
Organism: Mus musculus/domesticus
Length: 648  
Fragment?: false
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Protein
E9PVH4
Organism: Mus musculus/domesticus
Length: 922  
Fragment?: false
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Protein
Q8K226
Organism: Mus musculus/domesticus
Length: 682  
Fragment?: false
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Protein
Q3TPZ2
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
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Protein
Q6P571
Organism: Mus musculus/domesticus
Length: 648  
Fragment?: false
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Protein
Q3V382
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: false
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Protein
P68254
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
A3KML3
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom