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Protein

Phosphatidylethanolamine N-methyltransferase

Gene

PEMT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the three sequential steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME), PMME to phosphatidyldimethylethanolamine (PDME), and PDME to phosphatidylcholine (PC).UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine.UniRule annotation
S-adenosyl-L-methionine + phosphatidyl-N-dimethylethanolamine = S-adenosyl-L-homocysteine + phosphatidylcholine.UniRule annotation
S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.UniRule annotation

Enzyme regulationi

The first methylation is rate-limiting.

Pathwayi: phosphatidylcholine biosynthesis

This protein is involved in the pathway phosphatidylcholine biosynthesis, which is part of Phospholipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciZFISH:HS05721-MONOMER.
BRENDAi2.1.1.17. 2681.
ReactomeiR-HSA-1483191. Synthesis of PC.
UniPathwayiUPA00753.

Chemistry databases

SwissLipidsiSLP:000001199. [Q9UBM1-1]

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylethanolamine N-methyltransferaseUniRule annotation (EC:2.1.1.17UniRule annotation, EC:2.1.1.71UniRule annotation)
Short name:
PEAMTUniRule annotation
Short name:
PEMTUniRule annotation
Alternative name(s):
PEMT2
Phospholipid methyltransferaseUniRule annotation
Short name:
PLMTUniRule annotation
Gene namesi
Name:PEMTUniRule annotation
Synonyms:PEMPT, PNMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:8830. PEMT.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 12LumenalUniRule annotation1 PublicationAdd BLAST11
Intramembranei13 – 33HelicalUniRule annotation1 PublicationAdd BLAST21
Topological domaini34 – 45LumenalUniRule annotation1 Publication1 PublicationAdd BLAST12
Transmembranei46 – 66HelicalUniRule annotationAdd BLAST21
Topological domaini67 – 93CytoplasmicUniRule annotation1 PublicationAdd BLAST27
Transmembranei94 – 114HelicalUniRule annotationAdd BLAST21
Topological domaini115 – 157LumenalUniRule annotation1 Publication1 PublicationAdd BLAST43
Transmembranei158 – 178HelicalUniRule annotationAdd BLAST21
Topological domaini179 – 199CytoplasmicUniRule annotation1 Publication1 PublicationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi98G → E: Impairs binding to S-adenosyl-L-methionine. 1 Publication1
Mutagenesisi100G → D: Abolishes binding to S-adenosyl-L-methionine. 1 Publication1
Mutagenesisi180E → D: Abolishes binding to S-adenosyl-L-methionine. 1 Publication1
Mutagenesisi181E → D: Impairs binding to S-adenosyl-L-methionine. 1 Publication1

Organism-specific databases

DisGeNETi10400.
OpenTargetsiENSG00000133027.
PharmGKBiPA33175.

Polymorphism and mutation databases

BioMutaiPEMT.
DMDMi148887406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001939202 – 199Phosphatidylethanolamine N-methyltransferaseAdd BLAST198

Post-translational modificationi

Isoform 2 is N-glycosylated with high-mannose oligosaccharides.1 Publication

Proteomic databases

PaxDbiQ9UBM1.
PeptideAtlasiQ9UBM1.
PRIDEiQ9UBM1.
TopDownProteomicsiQ9UBM1-1. [Q9UBM1-1]

Expressioni

Gene expression databases

BgeeiENSG00000133027.
CleanExiHS_PEMT.
HS_PNMT.
ExpressionAtlasiQ9UBM1. baseline and differential.
GenevisibleiQ9UBM1. HS.

Organism-specific databases

HPAiHPA042375.

Interactioni

Protein-protein interaction databases

BioGridi115672. 1 interactor.
STRINGi9606.ENSP00000255389.

Structurei

3D structure databases

ProteinModelPortaliQ9UBM1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 100S-adenosyl-L-methionine bindingUniRule annotation1 Publication3
Regioni180 – 181S-adenosyl-L-methionine bindingUniRule annotation1 Publication2

Sequence similaritiesi

Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4142. Eukaryota.
ENOG4111HY0. LUCA.
GeneTreeiENSGT00390000007041.
HOGENOMiHOG000208789.
HOVERGENiHBG000990.
InParanoidiQ9UBM1.
KOiK00551.
OMAiTSTWALG.
OrthoDBiEOG091G0IQ4.
PhylomeDBiQ9UBM1.
TreeFamiTF300198.

Family and domain databases

HAMAPiMF_03216. PLMT. 1 hit.
InterProiIPR024960. PEMT/MFAP.
IPR007318. Phopholipid_MeTrfase.
[Graphical view]
PANTHERiPTHR15458. PTHR15458. 1 hit.
PfamiPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF005444. PEMT. 1 hit.
PROSITEiPS51599. SAM_PEMT_PEM2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBM1-1) [UniParc]FASTAAdd to basket
Also known as: PEMT-S

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTRLLGYVDP LDPSFVAAVI TITFNPLYWN VVARWEHKTR KLSRAFGSPY
60 70 80 90 100
LACYSLSVTI LLLNFLRSHC FTQAMLSQPR MESLDTPAAY SLGLALLGLG
110 120 130 140 150
VVLVLSSFFA LGFAGTFLGD YFGILKEARV TVFPFNILDN PMYWGSTANY
160 170 180 190
LGWAIMHASP TGLLLTVLVA LTYIVALLYE EPFTAEIYRQ KASGSHKRS
Length:199
Mass (Da):22,134
Last modified:June 12, 2007 - v4
Checksum:i98C07AB54B3B4E6A
GO
Isoform 2 (identifier: Q9UBM1-2) [UniParc]FASTAAdd to basket
Also known as: PEMT-L

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKRSGNPGAEVTNSSVAGPDCCGGLGNIDFRQADFCVM

Note: Much lower enzymatic activity than isoform 1.1 Publication
Show »
Length:236
Mass (Da):25,890
Checksum:i024AEDF227E93FEE
GO
Isoform 3 (identifier: Q9UBM1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKRSGNPGAEVTNSSVAGPDCCGGLGNIDFRQADFCVM
     156-199: MHASPTGLLL...QKASGSHKRS → IPAPAGAVGS...GSPIRRALHR

Note: No experimental confirmation available.Curated
Show »
Length:232
Mass (Da):24,967
Checksum:iACB01FB93D481894
GO

Sequence cautioni

The sequence AAF14867 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 3 (identifier: Q9UBM1-3)
Sequence conflicti222S → N in BAG63603 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0553723R → W.Corresponds to variant rs70959686dbSNPEnsembl.1
Natural variantiVAR_03277158V → I.4 PublicationsCorresponds to variant rs897453dbSNPEnsembl.1
Natural variantiVAR_06008358V → L.Corresponds to variant rs897453dbSNPEnsembl.1
Natural variantiVAR_016093175V → M.6 PublicationsCorresponds to variant rs7946dbSNPEnsembl.1
Natural variantiVAR_055373194G → R.Corresponds to variant rs70965427dbSNPEnsembl.1
Isoform 2 (identifier: Q9UBM1-2)
Natural varianti11V → A.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0373111M → MKRSGNPGAEVTNSSVAGPD CCGGLGNIDFRQADFCVM in isoform 2 and isoform 3. 2 Publications1
Alternative sequenceiVSP_046034156 – 199MHASP…SHKRS → IPAPAGAVGSEARQPHGPAP DGAGGPHLHSGSPIRRALHR in isoform 3. 1 PublicationAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176807 mRNA. Translation: AAD53292.1.
AF176806 mRNA. Translation: AAD53291.1.
AF294468
, AF294463, AF294464, AF294465, AF294466, AF294467 Genomic DNA. Translation: AAK19172.1.
AB029821 mRNA. Translation: BAA82407.1.
AF113126 mRNA. Translation: AAF14867.1. Different initiation.
AK302251 mRNA. Translation: BAG63603.1.
CR457099 mRNA. Translation: CAG33380.1.
EU574003 Genomic DNA. Translation: ACB21050.1.
AC020558 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55701.1.
CH471196 Genomic DNA. Translation: EAW55702.1.
BC000557 mRNA. Translation: AAH00557.1.
BC050593 mRNA. Translation: AAH50593.1.
CCDSiCCDS11186.1. [Q9UBM1-2]
CCDS11187.1. [Q9UBM1-1]
CCDS58520.1. [Q9UBM1-3]
RefSeqiNP_001254480.1. NM_001267551.1.
NP_001254481.1. NM_001267552.1. [Q9UBM1-3]
NP_009100.2. NM_007169.2. [Q9UBM1-1]
NP_680477.1. NM_148172.2. [Q9UBM1-2]
NP_680478.1. NM_148173.1. [Q9UBM1-1]
UniGeneiHs.714193.

Genome annotation databases

EnsembliENST00000255389; ENSP00000255389; ENSG00000133027. [Q9UBM1-2]
ENST00000395781; ENSP00000379127; ENSG00000133027. [Q9UBM1-3]
ENST00000395782; ENSP00000379128; ENSG00000133027. [Q9UBM1-1]
ENST00000395783; ENSP00000379129; ENSG00000133027. [Q9UBM1-1]
GeneIDi10400.
KEGGihsa:10400.
UCSCiuc002grj.3. human. [Q9UBM1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF176807 mRNA. Translation: AAD53292.1.
AF176806 mRNA. Translation: AAD53291.1.
AF294468
, AF294463, AF294464, AF294465, AF294466, AF294467 Genomic DNA. Translation: AAK19172.1.
AB029821 mRNA. Translation: BAA82407.1.
AF113126 mRNA. Translation: AAF14867.1. Different initiation.
AK302251 mRNA. Translation: BAG63603.1.
CR457099 mRNA. Translation: CAG33380.1.
EU574003 Genomic DNA. Translation: ACB21050.1.
AC020558 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55701.1.
CH471196 Genomic DNA. Translation: EAW55702.1.
BC000557 mRNA. Translation: AAH00557.1.
BC050593 mRNA. Translation: AAH50593.1.
CCDSiCCDS11186.1. [Q9UBM1-2]
CCDS11187.1. [Q9UBM1-1]
CCDS58520.1. [Q9UBM1-3]
RefSeqiNP_001254480.1. NM_001267551.1.
NP_001254481.1. NM_001267552.1. [Q9UBM1-3]
NP_009100.2. NM_007169.2. [Q9UBM1-1]
NP_680477.1. NM_148172.2. [Q9UBM1-2]
NP_680478.1. NM_148173.1. [Q9UBM1-1]
UniGeneiHs.714193.

3D structure databases

ProteinModelPortaliQ9UBM1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115672. 1 interactor.
STRINGi9606.ENSP00000255389.

Chemistry databases

SwissLipidsiSLP:000001199. [Q9UBM1-1]

Polymorphism and mutation databases

BioMutaiPEMT.
DMDMi148887406.

Proteomic databases

PaxDbiQ9UBM1.
PeptideAtlasiQ9UBM1.
PRIDEiQ9UBM1.
TopDownProteomicsiQ9UBM1-1. [Q9UBM1-1]

Protocols and materials databases

DNASUi10400.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255389; ENSP00000255389; ENSG00000133027. [Q9UBM1-2]
ENST00000395781; ENSP00000379127; ENSG00000133027. [Q9UBM1-3]
ENST00000395782; ENSP00000379128; ENSG00000133027. [Q9UBM1-1]
ENST00000395783; ENSP00000379129; ENSG00000133027. [Q9UBM1-1]
GeneIDi10400.
KEGGihsa:10400.
UCSCiuc002grj.3. human. [Q9UBM1-1]

Organism-specific databases

CTDi10400.
DisGeNETi10400.
GeneCardsiPEMT.
HGNCiHGNC:8830. PEMT.
HPAiHPA042375.
MIMi602391. gene.
neXtProtiNX_Q9UBM1.
OpenTargetsiENSG00000133027.
PharmGKBiPA33175.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4142. Eukaryota.
ENOG4111HY0. LUCA.
GeneTreeiENSGT00390000007041.
HOGENOMiHOG000208789.
HOVERGENiHBG000990.
InParanoidiQ9UBM1.
KOiK00551.
OMAiTSTWALG.
OrthoDBiEOG091G0IQ4.
PhylomeDBiQ9UBM1.
TreeFamiTF300198.

Enzyme and pathway databases

UniPathwayiUPA00753.
BioCyciZFISH:HS05721-MONOMER.
BRENDAi2.1.1.17. 2681.
ReactomeiR-HSA-1483191. Synthesis of PC.

Miscellaneous databases

ChiTaRSiPEMT. human.
GeneWikiiPhosphatidyl_ethanolamine_methyltransferase.
GenomeRNAii10400.
PROiQ9UBM1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000133027.
CleanExiHS_PEMT.
HS_PNMT.
ExpressionAtlasiQ9UBM1. baseline and differential.
GenevisibleiQ9UBM1. HS.

Family and domain databases

HAMAPiMF_03216. PLMT. 1 hit.
InterProiIPR024960. PEMT/MFAP.
IPR007318. Phopholipid_MeTrfase.
[Graphical view]
PANTHERiPTHR15458. PTHR15458. 1 hit.
PfamiPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF005444. PEMT. 1 hit.
PROSITEiPS51599. SAM_PEMT_PEM2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPEMT_HUMAN
AccessioniPrimary (citable) accession number: Q9UBM1
Secondary accession number(s): A8MZ66
, B4DY41, D3DXC3, Q6IAQ5, Q86VL3, Q9BW86, Q9UHY6, Q9Y6V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 12, 2007
Last modified: November 30, 2016
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.