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MGP004226

UniProt Annotations

Entry Information
Gene Namephosphatidylethanolamine N-methyltransferase
Protein EntryPEMT_HUMAN
UniProt IDQ9UBM1
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; Synonyms=PEMT-S; IsoId=Q9UBM1-1; Sequence=Displayed; Name=2; Synonyms=PEMT-L; IsoId=Q9UBM1-2; Sequence=VSP_037311; Note=Much lower enzymatic activity than isoform 1. Variant in position: 11:V->A. {ECO:0000269|PubMed:20860552}; Name=3; IsoId=Q9UBM1-3; Sequence=VSP_037311, VSP_046034; Note=No experimental confirmation available. Ref.5 (BAG63603) sequence is in conflict in position: 222:S->N. {ECO:0000305};
Catalytic ActivityS-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine. {ECO:0000255|PROSITE- ProRule:PRU00931}.
Catalytic ActivityS-adenosyl-L-methionine + phosphatidyl-N- dimethylethanolamine = S-adenosyl-L-homocysteine + phosphatidylcholine. {ECO:0000255|PROSITE-ProRule:PRU00931}.
Catalytic ActivityS-adenosyl-L-methionine + phosphatidyl-N- methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N- dimethylethanolamine. {ECO:0000255|PROSITE-ProRule:PRU00931}.
Enzyme RegulationThe first methylation is rate-limiting.
FunctionCatalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC).
PathwayPhospholipid metabolism; phosphatidylcholine biosynthesis. {ECO:0000255|PROSITE-ProRule:PRU00931}.
PtmIsoform 2 is N-glycosylated with high-mannose oligosaccharides. {ECO:0000269|PubMed:20860552}.
Sequence CautionSequence=AAF14867.1; Type=Erroneous initiation; Evidence={ECO:0000305};
SimilarityBelongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00931}.
Subcellular LocationIsoform 1: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20860552}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria. {ECO:0000250}.
Subcellular LocationIsoform 2: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20860552}; Multi-pass membrane protein {ECO:0000305}.
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/pemt/";
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