PPM1B

The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase has been shown to dephosphorylate cyclin-dependent kinases (CDKs), and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to cause cell-growth arrest or cell death. Alternative splicing results in multiple transcript variants encoding different isoforms. Additional transcript variants have been described, but currently do not represent full-length sequences. [provided by RefSeq]

protein phosphatase 1B (formerly 2C), magnesium-dependent, beta isoform

Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.

N-terminal protein myristoylationISS:UniProtKB
Negative regulation of defense response to virusManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of I-kappaB kinase/NF-kappaB signalingManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of interferon-beta productionManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of NIK/NF-kappaB signalingManual Assertion Based On ExperimentIMP:UniProtKB
Peptidyl-threonine dephosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of canonical Wnt signaling pathwayManual Assertion Based On ExperimentIBA:GO_Central
Protein dephosphorylationManual Assertion Based On ExperimentIMP:UniProtKB

Cytoplasm, cytosol
Membrane
Weakly associates at the membrane and N-myristoylation mediates the membrane localization.

Isgylation negatively regulates its activity.
N-myristoylation is essential for the recognition of its substrates for dephosphorylation.