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The degree of protein phosphorylation is regulated by a balance of protein kinase and phosphatase activities.
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analysis of antibodies generated against the protein phosphatase 1 (zeige PPP1CB Proteine) inhibitor KEPI and characterization of the epitope
PPP1R14C gene encodes a PKC (zeige PRRT2 Proteine)-potentiated inhibitory protein, KEPI, for type-1 Ser/Thr protein phosphatase (zeige PP2A-3 Proteine) (PP1 (zeige PPA1 Proteine)). KEPI mRNA and protein were enriched in brain, heart and skeletal muscle.
the data presented in this manuscript demonstrate a critical function of VPS35 (zeige vps35 Proteine) in regulating PTH1R (zeige PTH1R Proteine) trafficking. This event and VPS35 (zeige vps35 Proteine)-interaction with PPP1R14C appear to be essential for turning off PTH1R's endosomal signaling, and promoting PTH1R (zeige PTH1R Proteine)-mediated catabolic response and bone remodeling.
PPP1R14C gene encodes a PKC-potentiated inhibitory protein, KEPI, for type-1 Ser/Thr protein phosphatase (zeige PP2A-3 Proteine) (PP1 (zeige PPP1CC Proteine)). KEPI mRNA and protein are enriched in brain, heart and skeletal muscle.
The expression patterns point to possible roles for KEPI in regulating protein dephosphorylation by inhibiting PP1 activities in a number of brain pathways.
The degree of protein phosphorylation is regulated by a balance of protein kinase and phosphatase activities. Protein phosphatase-1 (PP1\; see MIM 176875) is a signal-transducing phosphatase that influences neuronal activity, protein synthesis, metabolism, muscle contraction, and cell division. PPP1R14C is an inhibitor of PP1 (Liu et al., 2002
PKC-potentiated PP1 inhibitory protein
, kinase C-enhanced PP1 inhibitor
, kinase-enhanced PP1 inhibitor
, protein phosphatase 1 regulatory subunit 14C
, serologically defined breast cancer antigen NY-BR-81