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Search results 101 to 131 out of 131 for Ppp1cb

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Type Details Score
Publication
First Author: Lee JH
Year: 2010
Journal: J Biol Chem
Title: Identification and characterization of a novel human PP1 phosphatase complex.
Volume: 285
Issue: 32
Pages: 24466-76
Publication
First Author: Ito M
Year: 2004
Journal: Mol Cell Biochem
Title: Myosin phosphatase: structure, regulation and function.
Volume: 259
Issue: 1-2
Pages: 197-209
Publication
First Author: Zagórska A
Year: 2010
Journal: Sci Signal
Title: New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion.
Volume: 3
Issue: 115
Pages: ra25
Publication
First Author: Tang PM
Year: 1991
Journal: J Biol Chem
Title: Molecular cloning and expression of the regulatory (RG1) subunit of the glycogen-associated protein phosphatase.
Volume: 266
Issue: 24
Pages: 15782-9
Publication
First Author: Ceulemans H
Year: 2002
Journal: J Biol Chem
Title: Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1.
Volume: 277
Issue: 49
Pages: 47331-7
Publication
First Author: Connor JH
Year: 2001
Journal: Mol Cell Biol
Title: Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1.
Volume: 21
Issue: 20
Pages: 6841-50
Publication
First Author: Mi J
Year: 2007
Journal: Cancer Res
Title: Protein phosphatase-1alpha regulates centrosome splitting through Nek2.
Volume: 67
Issue: 3
Pages: 1082-9
Publication
First Author: Song H
Year: 2015
Journal: Autophagy
Title: ATG16L1 phosphorylation is oppositely regulated by CSNK2/casein kinase 2 and PPP1/protein phosphatase 1 which determines the fate of cardiomyocytes during hypoxia/reoxygenation.
Volume: 11
Issue: 8
Pages: 1308-25
Publication
First Author: Nie H
Year: 2013
Journal: Nat Med
Title: Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-α in rheumatoid arthritis.
Volume: 19
Issue: 3
Pages: 322-8
Publication
First Author: Yao Z
Year: 2023
Journal: Nat Metab
Title: Upregulation of WDR6 drives hepatic de novo lipogenesis in insulin resistance in mice.
Volume: 5
Issue: 10
Pages: 1706-1725
Protein Domain
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 [].
Protein Domain
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).
Publication
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
Publication  
First Author: Liu R
Year: 2015
Journal: J Mol Cell Cardiol
Title: Cardiac-specific deletion of protein phosphatase 1β promotes increased myofilament protein phosphorylation and contractile alterations.
Volume: 87
Pages: 204-13
Publication  
First Author: Gu Q
Year: 2023
Journal: Int J Mol Sci
Title: Expression Levels of the Tnni3k Gene in the Heart Are Highly Associated with Cardiac and Glucose Metabolism-Related Phenotypes and Functional Pathways.
Volume: 24
Issue: 16
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 329  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 273  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
Publication
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
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory