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Literature summary for 3.1.1.89 extracted from

  • Longin, S.; Zwaenepoel, K.; Martens, E.; Louis, J.; Rondelez, E.; Goris, J.; Janssens, V.
    Spatial control of protein phosphatase 2A (de)methylation (2008), Exp. Cell Res., 314, 68-81.
    View publication on PubMed
Search for more literature for 3.1.1.89

Protein Variants

Protein Variants Comment Organism
K38A mutation does not abolish nuclear localization of enzyme Homo sapiens
additional information construction of deletion mutants and expression in HeLa cells. Domain 1 of the enzyme extends from amino acids 1 to 233, domain 2 from amino acids 234 to 284 and domain 3 includes amino acids 285 to 378. Domain 1 of PME-1 does not migrate into the nucleus and domain 3 shows a speckled cytoplasmic distribution, whereas domain 2 is targeted to the nucleus Homo sapiens
R271A mutation abolishes nuclear localization of enzyme Homo sapiens
R37A mutation does not abolish nuclear localization of enzyme Homo sapiens
R39A mutation does not abolish nuclear localization of enzyme Homo sapiens
S156A mutation abolishes the methylesterase activity, residue S156 is a functional active site serine Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus enzyme is predominantly localized in the nucleus and harbors a functional nuclear localization signal. This is in good correlation with the methylation status of its substrate protein phosphates PP2AC, demethylated PP2AC being substantially nuclear Homo sapiens 5634
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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General Information

General Information Comment Organism
physiological function overexpression of enzyme PME-1, but not of an inactive mutant, results in increased demethylation of substrate protein phosphatase PP2AC in the nucleus, whereas overexpression of a cytoplasmic PME-1 mutant lacking the nuclear localization signal results in increased demethylation in the cytoplasm, albeit without any obvious functional consequences. PME-1 associates with an inactive PP2A population, regardless of its esterase activity or localization. RNAi-mediated knock-down of PME-1 in HeLa cellsdoes not result in changes in substrate PP2AC methylation levels Homo sapiens