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Literature summary extracted from

  • Shields, D.J.; Lehner, R.; Agellon, L.B.; Vance, D.E.
    Membrane topography of human phosphatidylethanolamine N-methyltransferase (2003), J. Biol. Chem., 278, 2956-2962.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.17 endoplasmic reticulum
-
 Homo sapiens 5783
-
2.1.1.17 membrane
-
 Homo sapiens 16020
-
2.1.1.17 membrane topographical model: 4 transmembrane regions span the membrane such that both the N and C termini of the enzyme are localized external to the ER. Two hydrophilic connecting loops protrude into the luminal face of the microsomes whereas a corresponding loop protrudes on the cytosolic side remains proximate to the membrane Homo sapiens 16020
-
2.1.1.17 membrane mitochondria-associated membrane Homo sapiens 16020
-
2.1.1.17 mitochondrion
-
 Homo sapiens 5739
-
2.1.1.17 mitochondrion mitochondria associated membrane Homo sapiens 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.17 22000
-
 x * 22000, SDS-PAGE, epitope-tagged protein Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.17 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.17 liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.17 S-adenosyl-L-methionine + phosphatidylethanolamine
-
 Homo sapiens S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.17 ? x * 22000, SDS-PAGE, epitope-tagged protein Homo sapiens
2.1.1.17 More membrane protein, four transmembrane regions, topographical model Homo sapiens