Aliases for PPP2R1B Gene
- Protein Phosphatase 2 Regulatory Subunit A, Beta 2 3 5
- Protein Phosphatase 2 (Formerly 2A), Regulatory Subunit A, Beta Isoform 2 3
- Protein Phosphatase 2, Regulatory Subunit A, Beta 2 3
- Protein Phosphatase 2 (Formerly 2A), Regulatory Subunit A (PR 65), Beta Isoform 2
- Protein Phosphatase 2, Structural/Regulatory Subunit A, Beta 3
- PP2A, Subunit A, PR65-Beta Isoform 3
- PP2A, Subunit A, R1-Beta Isoform 3
- PP2A Subunit A Isoform PR65-Beta 4
External Ids for PPP2R1B Gene
Previous GeneCards Identifiers for PPP2R1B Gene
This gene encodes a constant regulatory subunit of protein phosphatase 2. Protein phosphatase 2 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. The constant regulatory subunit A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. This gene encodes a beta isoform of the constant regulatory subunit A. Mutations in this gene have been associated with some lung and colon cancers. Alternatively spliced transcript variants have been described. [provided by RefSeq, Apr 2010]
GeneCards Summary for PPP2R1B Gene
PPP2R1B (Protein Phosphatase 2 Regulatory Subunit A, Beta) is a Protein Coding gene. Diseases associated with PPP2R1B include lung cancer and hereditary wilms' tumor. Among its related pathways are Platelet activation, signaling and aggregation and Gene Expression. GO annotations related to this gene include binding. An important paralog of this gene is PPP2R1A.
UniProtKB/Swiss-Prot for PPP2R1B Gene
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.
Protein Ser/Thr phosphatases are a group of enzymes that catalyze the removal of phosphate groups from serine and/or threonine residues by hydrolysis of phosphoric acid monoesters. They oppose the action of kinases and phosphorylases and are involved in signal transduction.