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Protein

Ethanolaminephosphotransferase 1

Gene

SELENOI

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

Functioni

Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the formation of phosphatidylethanolamine via 'Kennedy' pathway.

Catalytic activityi

CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 Publication

Kineticsi

  1. KM=1.8 µM for CDP-ethanolamine1 Publication
  1. Vmax=76.3 pmol/min/mg enzyme with CDP-ethanolamine as substrate1 Publication

Pathwayi: phosphatidylethanolamine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes phosphatidylethanolamine from ethanolamine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Choline/ethanolamine kinase (CHKB), Ethanolamine kinase 2 (ETNK2), Choline kinase alpha (CHKA), Ethanolamine kinase 1 (ETNK1)
  2. Ethanolamine-phosphate cytidylyltransferase (PCYT2)
  3. Ethanolaminephosphotransferase 1 (SELENOI), Choline/ethanolaminephosphotransferase 1 (CEPT1)
This subpathway is part of the pathway phosphatidylethanolamine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylethanolamine from ethanolamine, the pathway phosphatidylethanolamine biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • ethanolaminephosphotransferase activity Source: HGNC
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • phosphatidylethanolamine biosynthetic process Source: HGNC

Keywordsi

Molecular functionTransferase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06434-MONOMER
BRENDAi2.7.8.1 2681
ReactomeiR-HSA-1483213 Synthesis of PE
UniPathwayiUPA00558; UER00743

Names & Taxonomyi

Protein namesi
Recommended name:
Ethanolaminephosphotransferase 1Curated (EC:2.7.8.1)
Short name:
hEPT1
Alternative name(s):
Selenoprotein I1 PublicationImported
Short name:
SelI1 Publication
Gene namesi
Name:SELENOIImported
Synonyms:EPT1Imported, KIAA1724Imported, SELI1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000138018.17
HGNCiHGNC:29361 SELENOI
MIMi607915 gene
neXtProtiNX_Q9C0D9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei47 – 69HelicalSequence analysisAdd BLAST23
Transmembranei84 – 103HelicalSequence analysisAdd BLAST20
Transmembranei123 – 145HelicalSequence analysisAdd BLAST23
Transmembranei150 – 172HelicalSequence analysisAdd BLAST23
Transmembranei179 – 201HelicalSequence analysisAdd BLAST23
Transmembranei221 – 243HelicalSequence analysisAdd BLAST23
Transmembranei256 – 278HelicalSequence analysisAdd BLAST23
Transmembranei291 – 310HelicalSequence analysisAdd BLAST20
Transmembranei317 – 339HelicalSequence analysisAdd BLAST23
Transmembranei344 – 366HelicalSequence analysisAdd BLAST23

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi85465
OpenTargetsiENSG00000138018
PharmGKBiPA165696581

Polymorphism and mutation databases

BioMutaiEPT1
DMDMi172046233

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000568132 – 397Ethanolaminephosphotransferase 1Add BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9C0D9
MaxQBiQ9C0D9
PaxDbiQ9C0D9
PeptideAtlasiQ9C0D9
PRIDEiQ9C0D9
ProteomicsDBi80018

PTM databases

iPTMnetiQ9C0D9
PhosphoSitePlusiQ9C0D9

Expressioni

Tissue specificityi

Widely expressed. Abundant in brain, placenta, liver and pancreas, followed by heart, skeletal muscle, lung and kidney. In brain it is strongly expressed in cerebellum, followed by the occipital pole and the frontal lobe.1 Publication

Gene expression databases

BgeeiENSG00000138018
ExpressionAtlasiQ9C0D9 baseline and differential
GenevisibleiQ9C0D9 HS

Interactioni

Protein-protein interaction databases

BioGridi124549, 6 interactors
IntActiQ9C0D9, 2 interactors
STRINGi9606.ENSP00000260585

Structurei

3D structure databases

ProteinModelPortaliQ9C0D9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2877 Eukaryota
COG5050 LUCA
GeneTreeiENSGT00530000063048
HOGENOMiHOG000008114
HOVERGENiHBG044519
InParanoidiQ9C0D9
KOiK00993
OMAiGYFNGPT
OrthoDBiEOG091G0GJ5
PhylomeDBiQ9C0D9
TreeFamiTF313270

Family and domain databases

InterProiView protein in InterPro
IPR000462 CDP-OH_P_trans
IPR014472 CHOPT
PANTHERiPTHR10414 PTHR10414, 1 hit
PfamiView protein in Pfam
PF01066 CDP-OH_P_transf, 1 hit
PIRSFiPIRSF015665 CHOPT, 1 hit
PROSITEiView protein in PROSITE
PS00379 CDP_ALCOHOL_P_TRANSF, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9C0D9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGYEYVSPE QLAGFDKYKY SAVDTNPLSL YVMHPFWNTI VKVFPTWLAP
60 70 80 90 100
NLITFSGFLL VVFNFLLMAY FDPDFYASAP GHKHVPDWVW IVVGILNFVA
110 120 130 140 150
YTLDGVDGKQ ARRTNSSTPL GELFDHGLDS WSCVYFVVTV YSIFGRGSTG
160 170 180 190 200
VSVFVLYLLL WVVLFSFILS HWEKYNTGIL FLPWGYDISQ VTISFVYIVT
210 220 230 240 250
AVVGVEAWYE PFLFNFLYRD LFTAMIIGCA LCVTLPMSLL NFFRSYKNNT
260 270 280 290 300
LKLNSVYEAM VPLFSPCLLF ILSTAWILWS PSDILELHPR VFYFMVGTAF
310 320 330 340 350
ANSTCQLIVC QMSSTRCPTL NWLLVPLFLV VLVVNLGVAS YVESILLYTL
360 370 380 390
TTAFTLAHIH YGVRVVKQLS SHFQIYPFSL RKPNSDULGM EEKNIGL
Length:397
Mass (Da):45,229
Last modified:February 26, 2008 - v3
Checksum:i24CDB1F19EFE4202
GO

Sequence cautioni

The sequence BAB21815 differs from that shown. Reason: Erroneous termination at position 387. Translated as Sec.Curated

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei387Selenocysteine1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BK001426 mRNA Translation: DAA01514.1
AB051511 mRNA Translation: BAB21815.1 Sequence problems.
CCDSiCCDS46240.1
RefSeqiNP_277040.1, NM_033505.3
UniGeneiHs.189073

Genome annotation databases

EnsembliENST00000260585; ENSP00000260585; ENSG00000138018
GeneIDi85465
KEGGihsa:85465
UCSCiuc021veu.2 human

Keywords - Coding sequence diversityi

Selenocysteine

Similar proteinsi

Entry informationi

Entry nameiEPT1_HUMAN
AccessioniPrimary (citable) accession number: Q9C0D9
Secondary accession number(s): Q63ZE3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: February 26, 2008
Last modified: June 20, 2018
This is version 128 of the entry and version 3 of the sequence. See 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

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