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Protein

Ethanolaminephosphotransferase 1

Gene

EPT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (EPT1), 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
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.7.8.1. 2681.
ReactomeiR-HSA-1483213. Synthesis of PE.
UniPathwayiUPA00558; UER00743.

Names & Taxonomyi

Protein namesi
Recommended name:
Ethanolaminephosphotransferase 1 (EC:2.7.8.1)
Short name:
hEPT1
Alternative name(s):
Selenoprotein I
Short name:
SelI
Gene namesi
Name:EPT1
Synonyms:KIAA1724, SELI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:29361. EPT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei47 – 6923HelicalSequence analysisAdd
BLAST
Transmembranei84 – 10320HelicalSequence analysisAdd
BLAST
Transmembranei123 – 14523HelicalSequence analysisAdd
BLAST
Transmembranei150 – 17223HelicalSequence analysisAdd
BLAST
Transmembranei179 – 20123HelicalSequence analysisAdd
BLAST
Transmembranei221 – 24323HelicalSequence analysisAdd
BLAST
Transmembranei256 – 27823HelicalSequence analysisAdd
BLAST
Transmembranei291 – 31020HelicalSequence analysisAdd
BLAST
Transmembranei317 – 33923HelicalSequence analysisAdd
BLAST
Transmembranei344 – 36623HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165696581.

Polymorphism and mutation databases

BioMutaiEPT1.
DMDMi172046233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 397396Ethanolaminephosphotransferase 1PRO_0000056813Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9C0D9.
MaxQBiQ9C0D9.
PaxDbiQ9C0D9.
PeptideAtlasiQ9C0D9.
PRIDEiQ9C0D9.

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

BgeeiQ9C0D9.
ExpressionAtlasiQ9C0D9. baseline and differential.
GenevisibleiQ9C0D9. HS.

Interactioni

Protein-protein interaction databases

BioGridi124549. 5 interactions.
IntActiQ9C0D9. 2 interactions.
MINTiMINT-1465883.
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.
OMAiVPLFSPC.
PhylomeDBiQ9C0D9.
TreeFamiTF313270.

Family and domain databases

InterProiIPR000462. CDP-OH_P_trans.
IPR014472. CHOPT.
[Graphical view]
PANTHERiPTHR10414. PTHR10414. 1 hit.
PfamiPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF015665. CHOPT. 1 hit.
PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]

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 BAB21815.1 differs from that shown. Reason: Erroneous termination at position 387. Translated as Sec.Curated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei387 – 3871Selenocysteine

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_033505.2.
UniGeneiHs.189073.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

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_033505.2.
UniGeneiHs.189073.

3D structure databases

ProteinModelPortaliQ9C0D9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124549. 5 interactions.
IntActiQ9C0D9. 2 interactions.
MINTiMINT-1465883.
STRINGi9606.ENSP00000260585.

Polymorphism and mutation databases

BioMutaiEPT1.
DMDMi172046233.

Proteomic databases

EPDiQ9C0D9.
MaxQBiQ9C0D9.
PaxDbiQ9C0D9.
PeptideAtlasiQ9C0D9.
PRIDEiQ9C0D9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi85465.
GeneCardsiEPT1.
HGNCiHGNC:29361. EPT1.
MIMi607915. gene.
neXtProtiNX_Q9C0D9.
PharmGKBiPA165696581.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2877. Eukaryota.
COG5050. LUCA.
GeneTreeiENSGT00530000063048.
HOGENOMiHOG000008114.
HOVERGENiHBG044519.
InParanoidiQ9C0D9.
KOiK00993.
OMAiVPLFSPC.
PhylomeDBiQ9C0D9.
TreeFamiTF313270.

Enzyme and pathway databases

UniPathwayiUPA00558; UER00743.
BRENDAi2.7.8.1. 2681.
ReactomeiR-HSA-1483213. Synthesis of PE.

Miscellaneous databases

ChiTaRSiEPT1. human.
GenomeRNAii85465.
PROiQ9C0D9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9C0D9.
ExpressionAtlasiQ9C0D9. baseline and differential.
GenevisibleiQ9C0D9. HS.

Family and domain databases

InterProiIPR000462. CDP-OH_P_trans.
IPR014472. CHOPT.
[Graphical view]
PANTHERiPTHR10414. PTHR10414. 1 hit.
PfamiPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF015665. CHOPT. 1 hit.
PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Identification and characterization of human ethanolaminephosphotransferase1."
    Horibata Y., Hirabayashi Y.
    J. Lipid Res. 48:503-508(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, TISSUE SPECIFICITY.
  4. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEPT1_HUMAN
AccessioniPrimary (citable) accession number: Q9C0D9
Secondary accession number(s): Q63ZE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: February 26, 2008
Last modified: July 6, 2016
This is version 116 of the entry and version 3 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 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

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.