| IED ID | IndEnz0005000685 |
| Enzyme Type ID | lipase000685 |
| Protein Name |
Protein phosphatase methylesterase 1 PME-1 EC 3.1.1.89 |
| Gene Name | PPME1 PME1 PP2593 PRO0750 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSALEKSMHLGRLPSRPPLPGSGGSQSGAKMRMGPGRKRDFSPVPWSQYFESMEDVEVENETGKDTFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPIMLIGHSMGGAIAVHTASSNLVPSLLGLCMIDVVEGTAMDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNLESARVSMVGQVKQCEGITSPEGSKSIVEGIIEEEEEDEEGSESISKRKKEDDMETKKDHPYTWRIELAKTEKYWDGWFRGLSNLFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKFQMQVLPQCGHAVHEDAPDKVAEAVATFLIRHRFAEPIGGFQCVFPGC |
| Enzyme Length | 386 |
| Uniprot Accession Number | Q9Y570 |
| Absorption | |
| Active Site | ACT_SITE 156; /evidence=ECO:0000269|PubMed:18394995; ACT_SITE 181; /evidence=ECO:0000269|PubMed:18394995; ACT_SITE 349; /evidence=ECO:0000269|PubMed:18394995 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[phosphatase 2A protein]-C-terminal L-leucine methyl ester + H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) + methanol; Xref=Rhea:RHEA:48548, Rhea:RHEA-COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=3.1.1.89; Evidence={ECO:0000269|PubMed:10318862, ECO:0000269|PubMed:18394995}; |
| DNA Binding | |
| EC Number | 3.1.1.89 |
| Enzyme Function | FUNCTION: Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme. {ECO:0000269|PubMed:10318862}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (4); Beta strand (15); Chain (1); Compositional bias (1); Erroneous translation (1); Helix (15); Initiator methionine (1); Modified residue (4); Region (2); Sequence conflict (1) |
| Keywords | 3D-structure;Alternative splicing;Direct protein sequencing;Hydrolase;Methylation;Phosphoprotein;Reference proteome;Serine esterase |
| Interact With | P67775-1 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 15; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 16; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0000250|UniProtKB:Q8BVQ5"; MOD_RES 16; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 42; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" |
| Post Translational Modification | PTM: Phosphorylated by SIK1 following increases in intracellular sodium, leading to dissociation from the protein phosphatase 2A (PP2A) complex and subsequent dephosphorylation of sodium/potassium-transporting ATPase ATP1A1. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3C5V; 3C5W; |
| Mapped Pubmed ID | 15761952; 17803990; 18782753; 19156129; 19293187; 20195357; 20360068; 21398589; 21851590; 22443683; 22732552; 24253382; 24835590; 24841198; 25839665; 26496610; 27048286; 27810903; 27913678; 29577269; 30340029; 31714894; 32071079; 32351291; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,315 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:48548 |
| Cross Reference Brenda | 3.1.1.89; |