Aliases for PPP1CB Gene
- Protein Phosphatase 1, Catalytic Subunit, Beta Isozyme 2 3
- Protein Phosphatase 1, Catalytic Subunit, Beta Isoform 2 3
- EC 188.8.131.52 4 64
- PPP1CD 3 4
- PP-1B 3 4
- Serine/Threonine Protein Phosphatase PP1-Beta Catalytic Subunit 3
- Serine/Threonine-Protein Phosphatase PP1-Beta Catalytic Subunit 3
- Protein Phosphatase 1, Catalytic Subunit, Delta Isoform 3
External Ids for PPP1CB Gene
The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Mouse studies suggest that PP1 functions as a suppressor of learning and memory. Two alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]
GeneCards Summary for PPP1CB Gene
PPP1CB (Protein Phosphatase 1, Catalytic Subunit, Beta Isozyme) is a Protein Coding gene. Diseases associated with PPP1CB include hiv-1 and cardiac conduction defect. Among its related pathways are Signaling by GPCR and Proteoglycans in cancer. GO annotations related to this gene include protein kinase binding and myosin-light-chain-phosphatase activity. An important paralog of this gene is PPP1CC.
UniProtKB/Swiss-Prot for PPP1CB Gene
Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the Ser-418 residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).
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.