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Family Report for: PPase_methylesterase_euk

PPase_methylesterase_euk



Relationship
Block X
Parent Family : Abhydrolase_6

Comment
PIRSF022950 This group represents protein phosphatase methylesterase, eukaryotic type. Carboxymethylation of proteins is a highly conserved means of regulation in eukaryotic cells. The protein phosphatase 2A (PP2A) catalytic (C) subunit is reversibly methylated at its carboxyl terminus by specific methyltransferase and methylesterase enzymes. Protein phosphatase 2A (PP2A) is an important serine/threonine phosphatase that plays a role in many biological processes. Reversible carboxyl methylation of the PP2A catalytic subunit is an essential regulatory mechanism for its function. Demethylation and negative regulation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to humans. PME-1 directly binds to the active site of PP2A. This interaction results in the activation of PME-1 by rearranging the catalytic triad into an active conformation. Interactions also lead to inactivation of PP2A by evicting the manganese ions required for the phosphatase activity (Xing et al. ). PPME proteins show false positive hits with the prosite PS00120 of lipases

Database
Sequences
Interpro
|
IPR016812 (Protein phosphatase methylesterase, eukaryotic type)
PIRSF
|
Pdoc
|
PFam
|
Prints
|
Prosite
|
no EC number



Peptide in
|Fasta
Nucleotide in
|Fasta
Alignment with Multalin
|Text only/graphic display
Seed alignment with MAFFT
|No colour/coloured with Mview
Alignment with MAFFT
|No colour/coloured with Mview
Dendrogram
|Graphical display, obtained with the dnd file produced by Clustalw

References
    Title: Structural mechanism of demethylation and inactivation of protein phosphatase 2A
    Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y
    Ref: Cell, 133:154, 2008 : PubMed

            

    Title: A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
    Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC
    Ref: Journal of Biological Chemistry, 274:14382, 1999 : PubMed

            

Other Papers


No structure scheme yet for this family

Structures in PPase_methylesterase_euk family (2)

Genes Proteins in PPase_methylesterase_euk family (151)

Fragments of genes in PPase_methylesterase_euk family (10)

No Substrate

Inhibitors of some enzymes in the PPase_methylesterase_euk family (3)



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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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