PPase_methylesterase_euk

Relationship

Family: PPase_methylesterase_euk

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

Interpro : IPR016812 Protein phosphatase methylesterase, eukaryotic type

PIRSF : PIRSF022950 protein phosphatase methylesterase, eukaryotic type

Pdoc : No Pdoc

Pfam : No Pfam

Prints : No Print

EC Number : No EC Number

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

References (2)

Title : Structural mechanism of demethylation and inactivation of protein phosphatase 2A - Xing_2008_Cell_133_154
Author(s) : Xing Y , Li Z , Chen Y , Stock JB , Jeffrey PD , Shi Y
Ref : Cell , 133 :154 , 2008
Abstract : Xing_2008_Cell_133_154
ESTHER : Xing_2008_Cell_133_154
PubMedSearch : Xing_2008_Cell_133_154
PubMedID: 18394995
Gene_locus related to this paper: human-PPME1

Title : A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A - Ogris_1999_J.Biol.Chem_274_14382
Author(s) : Ogris E , Du X , Nelson KC , Mak EK , Yu XX , Lane WS , Pallas DC
Ref : Journal of Biological Chemistry , 274 :14382 , 1999
Abstract : Ogris_1999_J.Biol.Chem_274_14382
ESTHER : Ogris_1999_J.Biol.Chem_274_14382
PubMedSearch : Ogris_1999_J.Biol.Chem_274_14382
PubMedID: 10318862
Gene_locus related to this paper: human-PPME1 , mouse-PPME1

Structures (2)

Genes Proteins in PPase_methylesterase_euk family (151)

Fragments of genes in PPase_methylesterase_euk family (10)

Structures in PPase_methylesterase_euk family (2)

No substrate

Inhibitors in PPase_methylesterase_euk family (4)