Difference between revisions of "Phosphatase Gene PPM1E"
Line 3: | Line 3: | ||
[[Phosphatase_Gene_PPM1E|PPM1E]] (also known as [http://www.ncbi.nlm.nih.gov/gene/22843 POXP1, PP2CH, caMKN, CaMKP-N]). The encoded protein is localized to the nucleus and dephosphorylates and inactivates multiple substrates including serine/threonine-protein kinase PAK 1, 5'-AMP-activated protein kinase (AMPK) and the multifunctional calcium/calmodulin-dependent protein kinases. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, May 2012] | [[Phosphatase_Gene_PPM1E|PPM1E]] (also known as [http://www.ncbi.nlm.nih.gov/gene/22843 POXP1, PP2CH, caMKN, CaMKP-N]). The encoded protein is localized to the nucleus and dephosphorylates and inactivates multiple substrates including serine/threonine-protein kinase PAK 1, 5'-AMP-activated protein kinase (AMPK) and the multifunctional calcium/calmodulin-dependent protein kinases. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, May 2012] | ||
− | Though PPM1E and another phosphatase of this subfamily [[Phosphatase_Gene_PPM1F|PPM1F]] (also known as [http://www.ncbi.nlm.nih.gov/gene/9647 POXP2, CAMKP, FEM-2, hFEM-2, CaMKPase]) dephosphorylate and regulate multifunctional Ca(2+)/calmodulin-dependent protein kinases, their localizations are different. PPM1E is localized in the nucleus, whereas PPM1F is localized in the cytosol. PPM1E contains two NLSs, NLS1 and NLS2, at the C-terminus. A cluster of basic residues in the NLSs is important for their function. NLS1 and NLS2 function independently, but mutagenesis analysis suggests that these NLSs interact with each other <cite>Takeuchi04</cite>. | + | Though PPM1E and another phosphatase of this subfamily [[Phosphatase_Gene_PPM1F|PPM1F]] (also known as [http://www.ncbi.nlm.nih.gov/gene/9647 POXP2, CAMKP, FEM-2, hFEM-2, CaMKPase]) dephosphorylate and regulate multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaMKs) <cite>Ishida05</cite>, their localizations are different. PPM1E is localized in the nucleus, whereas PPM1F is localized in the cytosol. PPM1E contains two NLSs, NLS1 and NLS2, at the C-terminus. A cluster of basic residues in the NLSs is important for their function. NLS1 and NLS2 function independently, but mutagenesis analysis suggests that these NLSs interact with each other <cite>Takeuchi04</cite>. |
+ | |||
+ | |||
== References == | == References == | ||
<biblio> | <biblio> | ||
+ | #Ishida05 pmid=15680915 | ||
#Takeuchi2014 pmid=15496589 | #Takeuchi2014 pmid=15496589 | ||
</biblio> | </biblio> |
Revision as of 03:55, 6 May 2014
Phosphatase Classification: Superfamily PPM (PP2C): Family PPM (PP2C): Gene PPM1E
PPM1E (also known as POXP1, PP2CH, caMKN, CaMKP-N). The encoded protein is localized to the nucleus and dephosphorylates and inactivates multiple substrates including serine/threonine-protein kinase PAK 1, 5'-AMP-activated protein kinase (AMPK) and the multifunctional calcium/calmodulin-dependent protein kinases. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, May 2012]
Though PPM1E and another phosphatase of this subfamily PPM1F (also known as POXP2, CAMKP, FEM-2, hFEM-2, CaMKPase) dephosphorylate and regulate multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaMKs) [1], their localizations are different. PPM1E is localized in the nucleus, whereas PPM1F is localized in the cytosol. PPM1E contains two NLSs, NLS1 and NLS2, at the C-terminus. A cluster of basic residues in the NLSs is important for their function. NLS1 and NLS2 function independently, but mutagenesis analysis suggests that these NLSs interact with each other [2].
References
- Ishida A, Tada Y, Nimura T, Sueyoshi N, Katoh T, Takeuchi M, Fujisawa H, Taniguchi T, and Kameshita I. Identification of major Ca(2+)/calmodulin-dependent protein kinase phosphatase-binding proteins in brain: biochemical analysis of the interaction. Arch Biochem Biophys. 2005 Mar 1;435(1):134-46. DOI:10.1016/j.abb.2004.11.022 |
- Takeuchi M, Taniguchi T, and Fujisawa H. Identification and characterization of nuclear localization signals of CaMKP-N. J Biochem. 2004 Aug;136(2):183-8. DOI:10.1093/jb/mvh109 |