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Search results 201 to 217 out of 217 for Ppp1r12a

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Type Details Score
Protein Domain
IPR037981 | PPP1CC
Type: Family
Description: Serine/threonine-protein phosphatase PP1 () is a complex of a catalytic subunit, either PPP1CA, PPP1CB or PPP1CC, with one or more regulatory or targeting subunits. Example targeting subunits are PPP1R12A and PPP1R12C, which mediate binding of PP1 to myosin [, , ]; PPP1R3A, which mediates binding to glycogen in the skeletal muscle []; PPP1R7, []; PPP1R15A, which mediates binding to EIF2S1 []. The phosphatase associates with any one of many other regulatory proteins to form a complex that dephosphorylates a specific target protein. For example, centrosome splitting is regulated by the association of NEK2 with PP1 via the PPP1CA subunit [], binding to ATG16L1 antagonizes casein kinase 2-mediated phosphorylation of ATG16L1 affecting the fate of cadiomyocytes []and association with TNF-a induces phosphorylation of FOXP3 which controls regulatory T cell function []. PP1 is required for the cell cycle [], cell division, glycogen metabolism [], muscle contraction []and protein synthesis. PPP1CA and PPP1CB are components of the PTW/PP1 phosphatase complex [].This entry includes the catalytic subunit gamma (PPP1CC) from mammals, Dis2 from fission yeasts and Glc7 from budding yeasts. Glc7 is also a component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB [].
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Protein Domain
IPR037979 | PPP1CA
Type: Family
Description: Serine/threonine-protein phosphatase PP1 () is a complex of a catalytic subunit, either PPP1CA, PPP1CB or PPP1CC, with one or more regulatory or targeting subunits. Example targeting subunits are PPP1R12A and PPP1R12C, which mediate binding of PP1 to myosin [, , ]; PPP1R3A, which mediates binding to glycogen in the skeletal muscle []; PPP1R7, []; PPP1R15A, which mediates binding to EIF2S1 []. The phosphatase associates with any one of many other regulatory proteins to form a complex that dephosphorylates a specific target protein. For example, centrosome splitting is regulated by the association of NEK2 with PP1 via the PPP1CA subunit [], binding to ATG16L1 antagonizes casein kinase 2-mediated phosphorylation of ATG16L1 affecting the fate of cadiomyocytes []and association with TNF-a induces phosphorylation of FOXP3 which controls regulatory T cell function []. PP1 is required for the cell cycle [], cell division, glycogen metabolism [], muscle contraction []and protein synthesis. PPP1CA and PPP1CB are components of the PTW/PP1 phosphatase complex [].This entry includes the catalytic subunits PP1-alpha (PPP1CA).
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Publication
11399775 | -
First Author: Tan I
Year: 2001
Journal: J Biol Chem
Title: Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton.
Volume: 276
Issue: 24
Pages: 21209-16
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Protein
P62137
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
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Protein
Q3UMT1
Organism: Mus musculus/domesticus
Length: 782  
Fragment?: false
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Protein
P63087
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Protein
Q9DBR7
Organism: Mus musculus/domesticus
Length: 1029  
Fragment?: false
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Protein
Q8BG95
Organism: Mus musculus/domesticus
Length: 976  
Fragment?: false
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Protein
A6H644
Organism: Mus musculus/domesticus
Length: 992  
Fragment?: false
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Protein
Q3U8W0
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
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Protein
Q3U7K1
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Protein
F6XWD4
Organism: Mus musculus/domesticus
Length: 704  
Fragment?: true
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Protein
A0A0G2JFF1
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: true
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Protein
Q3TYF5
Organism: Mus musculus/domesticus
Length: 329  
Fragment?: true
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Protein
A0A0G2JGC1
Organism: Mus musculus/domesticus
Length: 273  
Fragment?: false
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Protein
Q6ZWM8
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Publication
12819204 | -
First Author: Nedea E
Year: 2003
Journal: J Biol Chem
Title: Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends.
Volume: 278
Issue: 35
Pages: 33000-10
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