Q9UBM1 (PEMT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylethanolamine N-methyltransferase
Short name=PEAMT
Short name=PEMT
EC=2.1.1.17
EC=2.1.1.71

Alternative name(s):
PEMT2

Gene names

Name:	PEMT
Synonyms:	PEMPT, PNMT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes three sequential methylation reactions of phosphatidylethanolamine (PE) by AdoMet, thereby producing phosphatidylcholine (PC).
Catalytic activity	S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine. S-adenosyl-L-methionine + phosphatidyl-N-dimethylethanolamine = S-adenosyl-L-homocysteine + phosphatidylcholine. S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.
Enzyme regulation	The first methylation is rate-limiting.
Pathway	Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Potential. Mitochondrion membrane; Multi-pass membrane protein Potential. Note: Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria By similarity.
Sequence similarities	Belongs to the PEMT/PEM2 methyltransferase family.
Sequence caution	The sequence AAF14867.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Endoplasmic reticulum Membrane Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Traceable author statement Ref.1. Source: ProtInc phosphatidylcholine biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphatidyl-N-dimethylethanolamine N-methyltransferase activity Inferred from electronic annotation. Source: EC phosphatidyl-N-methylethanolamine N-methyltransferase activity Inferred from electronic annotation. Source: EC phosphatidylethanolamine N-methyltransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UBM1-1)

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.

Isoform 2 (identifier: Q9UBM1-2)

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

Isoform 3 (identifier: Q9UBM1-3)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 199	198	Phosphatidylethanolamine N-methyltransferase		PRO_0000193920
Regions
	Transmembrane	13 – 33	21	Helical; Potential
	Transmembrane	46 – 66	21	Helical; Potential
	Transmembrane	94 – 114	21	Helical; Potential
	Transmembrane	158 – 178	21	Helical; Potential
Natural variations
	Alternative sequence	1	1	M → MKRSGNPGAEVTNSSVAGPD CCGGLGNIDFRQADFCVM in isoform 2 and isoform 3.		VSP_037311
	Alternative sequence	156 – 199	44	MHASP…SHKRS → IPAPAGAVGSEARQPHGPAP DGAGGPHLHSGSPIRRALHR in isoform 3.		VSP_046034
	Natural variant	3	1	R → W. Ref.7		VAR_055372
	Natural variant	58	1	V → I. Ref.3 Ref.5 Ref.6 Ref.7 Ref.10 Corresponds to variant rs897453 [ dbSNP | Ensembl ].		VAR_032771
	Natural variant	58	1	V → L. Corresponds to variant rs897453 [ dbSNP | Ensembl ].		VAR_060083
	Natural variant	175	1	V → M. Ref.1 Ref.2 Ref.3 Ref.6 Ref.7 Ref.9 Ref.10 Corresponds to variant rs7946 [ dbSNP | Ensembl ].		VAR_016093
	Natural variant	194	1	G → R. Ref.7		VAR_055373
Isoform 2:
	Natural variant	11	1	V → A.
Experimental info
Isoform 3:
	Sequence conflict	222	1	S → N in BAG63603. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 12, 2007. Version 4. Checksum: 98C07AB54B3B4E6A	FASTA	199	22,134
	10 20 30 40 50 60 MTRLLGYVDP LDPSFVAAVI TITFNPLYWN VVARWEHKTR KLSRAFGSPY LACYSLSVTI 70 80 90 100 110 120 LLLNFLRSHC FTQAMLSQPR MESLDTPAAY SLGLALLGLG VVLVLSSFFA LGFAGTFLGD 130 140 150 160 170 180 YFGILKEARV TVFPFNILDN PMYWGSTANY LGWAIMHASP TGLLLTVLVA LTYIVALLYE 190 EPFTAEIYRQ KASGSHKRS
	Isoform 2 [UniParc]. Checksum: 024AEDF227E93FEE	FASTA	236	25,890
	10 20 30 40 50 60 MKRSGNPGAE VTNSSVAGPD CCGGLGNIDF RQADFCVMTR LLGYVDPLDP SFVAAVITIT 70 80 90 100 110 120 FNPLYWNVVA RWEHKTRKLS RAFGSPYLAC YSLSVTILLL NFLRSHCFTQ AMLSQPRMES 130 140 150 160 170 180 LDTPAAYSLG LALLGLGVVL VLSSFFALGF AGTFLGDYFG ILKEARVTVF PFNILDNPMY 190 200 210 220 230 WGSTANYLGW AIMHASPTGL LLTVLVALTY IVALLYEEPF TAEIYRQKAS GSHKRS
	Isoform 3 [UniParc]. Checksum: ACB01FB93D481894	FASTA	232	24,967
	10 20 30 40 50 60 MKRSGNPGAE VTNSSVAGPD CCGGLGNIDF RQADFCVMTR LLGYVDPLDP SFVAAVITIT 70 80 90 100 110 120 FNPLYWNVVA RWEHKTRKLS RAFGSPYLAC YSLSVTILLL NFLRSHCFTQ AMLSQPRMES 130 140 150 160 170 180 LDTPAAYSLG LALLGLGVVL VLSSFFALGF AGTFLGDYFG ILKEARVTVF PFNILDNPMY 190 200 210 220 230 WGSTANYLGW AIIPAPAGAV GSEARQPHGP APDGAGGPHL HSGSPIRRAL HR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of three novel cDNAs for human phosphatidylethanolamine N-methyltransferase and localization of the human gene on chromosome 17p11.2." Walkey C.J., Shields D.J., Vance D.E. Biochim. Biophys. Acta 1436:405-412(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-175. Tissue: Liver.
[2]	"Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene." Shields D.J., Agellon L.B., Vance D.E. Biochim. Biophys. Acta 1532:105-114(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-175.
[3]	"Homo sapiens phosphatidylethanolamine N-methyltransferase mRNA." Maeda E., Watanabe M., Wang J., Kasuga M. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ILE-58 AND MET-175. Tissue: Liver.
[4]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hypothalamus.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ILE-58. Tissue: Testis.
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-58 AND MET-175.
[7]	NIEHS SNPs program Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-3; ILE-58; MET-175 AND ARG-194 (ISOFORM 1), VARIANT ALA-11 (ISOFORM 2).
[8]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-175.
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS ILE-58 AND MET-175. Tissue: Brain and Skin.
[11]	"Phosphatidylethanolamine N-methyltransferase (PEMT) gene expression is induced by estrogen in human and mouse primary hepatocytes." Resseguie M., Song J., Niculescu M.D., da Costa K.A., Randall T.A., Zeisel S.H. FASEB J. 21:2622-2632(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00328909. IPI00328921. IPI00791039.
RefSeq	NP_001254480.1. NM_001267551.1. NP_001254481.1. NM_001267552.1. NP_009100.2. NM_007169.2. NP_680477.1. NM_148172.2. NP_680478.1. NM_148173.1.
UniGene	Hs.714193.
3D structure databases
ProteinModelPortal	Q9UBM1.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000255389.
Polymorphism databases
DMDM	148887406.
Proteomic databases
PaxDb	Q9UBM1.
Protocols and materials databases
DNASU	10400.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000255389; ENSP00000255389; ENSG00000133027. ENST00000395781; ENSP00000379127; ENSG00000133027. ENST00000395782; ENSP00000379128; ENSG00000133027. ENST00000395783; ENSP00000379129; ENSG00000133027.
GeneID	10400.
KEGG	hsa:10400.
UCSC	uc002grj.3. human. uc002grl.3. human. uc010vwx.2. human.
Organism-specific databases
CTD	10400.
GeneCards	GC17M017408.
HGNC	HGNC:8830. PEMT.
HPA	HPA042375.
MIM	602391. gene.
neXtProt	NX_Q9UBM1.
PharmGKB	PA33175.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG261676.
HOVERGEN	HBG000990.
InParanoid	Q9UBM1.
KO	K00551.
OMA	FWNIVAR.
OrthoDB	EOG4V9TRP.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00753.
Gene expression databases
ArrayExpress	Q9UBM1.
Bgee	Q9UBM1.
CleanEx	HS_PEMT. HS_PNMT.
Genevestigator	Q9UBM1.
GermOnline	ENSG00000133027. Homo sapiens.
Family and domain databases
InterPro	IPR024960. PEMT/MFAP. IPR007318. Phopholipid_MeTrfase. [Graphical view]
PANTHER	PTHR15458. PTHR15458. 1 hit.
Pfam	PF04191. PEMT. 1 hit. [Graphical view]
PIRSF	PIRSF005444. PEMT. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10400.
NextBio	39408.
SOURCE	Search...

Entry information

Entry name

PEMT_HUMAN

Accession

Primary (citable) accession number: Q9UBM1
Secondary accession number(s): A8MZ66 , B4DY41, D3DXC3, Q6IAQ5, Q86VL3, Q9BW86, Q9UHY6, Q9Y6V9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 12, 2007
Last modified:	May 29, 2013
This is version 104 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.