Aliases for PPP2CB Gene
- Protein Phosphatase 2, Catalytic Subunit, Beta Isozyme 2 3
- Protein Phosphatase 2 (Formerly 2A), Catalytic Subunit, Beta Isoform 2 3
- EC 188.8.131.52 4 63
- PP2A-Beta 3 4
- Serine/Threonine Protein Phosphatase 2A, Catalytic Subunit, Beta Isoform 3
- Serine/Threonine-Protein Phosphatase 2A Catalytic Subunit Beta Isoform 3
- Protein Phosphatase 2, Catalytic Subunit, Beta Isoform 3
External Ids for PPP2CB Gene
Previous GeneCards Identifiers for PPP2CB Gene
This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. This gene encodes a beta isoform of the catalytic subunit. [provided by RefSeq, Mar 2010]
GeneCards Summary for PPP2CB Gene
PPP2CB (Protein Phosphatase 2, Catalytic Subunit, Beta Isozyme) is a Protein Coding gene. Among its related pathways are PI3K-Akt signaling pathway and Signaling by FGFR. GO annotations related to this gene include protein C-terminus binding and protein serine/threonine phosphatase activity. An important paralog of this gene is PPP4C.
UniProtKB/Swiss-Prot for PPP2CB Gene
PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.
Protein ser/thr phosphatases are a group of enzymes that catalyze the removal of phosphate groups from serine and/or threonine residues by the hydrolysis of phosphoric acid monoesters. They directly oppose the actions of kinases and phosphorylases and therefore play an integral role in many signal transduction pathways. There are two groups of serine/threonine phosphatases; phosphoprotein phosphatases (e.g. PP1, calcineurin), which are sensitive to okadaic acid and metallo-phosphatases (e.g. PP2C), which require a divalent cation, commonly Mg2+, for catalytic activity. Dephosphorylation, depending on the residue that the phosphate group is removed from, can have a stimulatory or inhibitory effect on the target molecule. This makes protein Ser/Thr phosphatases essential for many signal transduction pathways. Protein Ser/Thr phosphatase are regulated by their subcellular localization and by inhibitor proteins, which are subtype-specific.