Aliases for PPP2R2D Gene
- Protein Phosphatase 2, Regulatory Subunit B, Delta 2 3
- PP2A Subunit B Isoform Delta 2 3 4
- Protein Phosphatase 2, Regulatory Subunit B, Delta Isoform 2 3
- PP2A Subunit B Isoform PR55-Delta 3 4
- PP2A Subunit B Isoform B55-Delta 3 4
- PP2A Subunit B Isoform R2-Delta 3 4
- Serine/Threonine-Protein Phosphatase 2A 55 KDa Regulatory Subunit B Delta Isoform 3
- KIAA1541 4
- MDS026 3
External Ids for PPP2R2D Gene
Previous GeneCards Identifiers for PPP2R2D Gene
GeneCards Summary for PPP2R2D Gene
PPP2R2D (Protein Phosphatase 2, Regulatory Subunit B, Delta) is a Protein Coding gene. Among its related pathways are PI3K-Akt signaling pathway and Cell Cycle, Mitotic. GO annotations related to this gene include protein phosphatase type 2A regulator activity. An important paralog of this gene is PPP2R2C.
UniProtKB/Swiss-Prot for PPP2R2D Gene
B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55-delta) fluctuate during the cell cycle: the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and also may direct the localization of the catalytic enzyme to a particular subcellular compartment (By similarity).
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.