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Identification
HMDB Protein ID HMDBP07306
Secondary Accession Numbers
  • 12928
Name Ethanolaminephosphotransferase 1
Synonyms
  1. SelI
  2. Selenoprotein I
  3. hEPT1
Gene Name EPT1
Protein Type Unknown
Biological Properties
General Function Involved in phosphotransferase activity, for other substituted phosphate groups
Specific Function 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.
Pathways
  • Ether lipid metabolism
  • Glycerophospholipid metabolism
  • phosphatidylethanolamine biosynthesis
Reactions
CDP-ethanolamine + 1,2-diacylglycerol → Cytidine monophosphate + a phosphatidylethanolamine details
CDP-ethanolamine + 1,2-Diacyl-sn-glycerol → Cytidine monophosphate + Phosphatidylethanolamine details
CMP-2-aminoethylphosphonate + Diacylglycerol → Cytidine monophosphate + Diacylglyceryl-2-aminoethylphosphonate details
CDP-ethanolamine + 1-Alkyl-2-acylglycerol → Cytidine monophosphate + 1-Alkyl-2-acylglycerophosphoethanolamine details
O-1-Alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + Cytidine monophosphate → 1-Alkenyl-2-acylglycerol + CDP-ethanolamine details
GO Classification
Biological Process
small molecule metabolic process
phosphatidylethanolamine biosynthetic process
Cellular Component
endoplasmic reticulum membrane
integral to membrane
Component
membrane
cell part
Function
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
phosphotransferase activity, for other substituted phosphate groups
Molecular Function
metal ion binding
ethanolaminephosphotransferase activity
Process
metabolic process
phospholipid biosynthetic process
organophosphate metabolic process
phospholipid metabolic process
Cellular Location
  1. Membrane
  2. Multi-pass membrane protein (Potential)
Gene Properties
Chromosome Location 2
Locus 2p23.3
SNPs EPT1
Gene Sequence
>1194 bp
ATGGCTGGCTACGAATACGTGAGCCCGGAGCAGCTGGCTGGCTTTGATAAGTACAAGTAC
AGTGCTGTGGATACCAATCCACTTTCTCTGTATGTCATGCATCCATTCTGGAACACTATA
GTAAAGGTATTTCCTACTTGGCTGGCGCCCAATCTGATAACTTTTTCTGGCTTTCTGCTG
GTCGTATTCAATTTTCTGCTAATGGCATACTTTGATCCTGACTTTTATGCCTCAGCACCA
GGTCACAAGCACGTGCCTGACTGGGTTTGGATTGTAGTGGGCATCCTCAACTTCGTAGCC
TACACTCTAGATGGTGTGGACGGAAAGCAAGCTCGCAGAACCAATTCTAGCACTCCCTTA
GGGGAGCTTTTTGATCATGGCCTGGATAGTTGGTCATGTGTTTACTTTGTTGTGACTGTT
TATTCCATCTTTGGAAGAGGATCAACTGGTGTCAGTGTTTTTGTTCTTTATCTCCTGCTA
TGGGTAGTTTTGTTTTCTTTCATCCTGTCCCACTGGGAAAAGTATAACACAGGGATTCTT
TTCCTGCCATGGGGATATGACATTAGCCAGGTGACTATTTCTTTTGTCTACATAGTGACT
GCAGTTGTGGGAGTTGAGGCCTGGTATGAACCTTTCCTGTTTAATTTCTTATATAGAGAC
CTATTCACTGCAATGATTATTGGTTGTGCATTATGTGTGACTCTTCCAATGAGTTTATTA
AACTTTTTCAGAAGCTATAAAAATAACACCTTGAAACTCAATTCAGTCTATGAAGCTATG
GTTCCCTTATTTTCTCCATGCTTGCTGTTCATTTTGTCTACAGCGTGGATCCTTTGGTCA
CCTTCAGATATTTTAGAGCTACATCCTAGAGTATTCTACTTTATGGTTGGAACAGCCTTT
GCCAACAGTACATGTCAGCTGATTGTTTGCCAAATGAGTAGTACCCGGTGTCCAACTTTG
AATTGGTTGCTGGTTCCTCTCTTCTTGGTTGTCTTAGTGGTAAACCTAGGAGTAGCCTCT
TACGTTGAGAGCATTCTCCTGTATACATTAACAACTGCTTTTACTCTGGCCCACATCCAT
TATGGAGTACGAGTGGTAAAGCAGCTGAGCAGCCATTTTCAGATTTACCCCTTCTCATTG
AGGAAACCAAACTCAGATTGACTAGGAATGGAAGAAAAGAATATTGGCCTGTAA
Protein Properties
Number of Residues 397
Molecular Weight 45228.42
Theoretical pI 6.599
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ethanolaminephosphotransferase 1
MAGYEYVSPEQLAGFDKYKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLL
VVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPL
GELFDHGLDSWSCVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGIL
FLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLL
NFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAF
ANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIH
YGVRVVKQLSSHFQIYPFSLRKPNSDULGMEEKNIGL
GenBank ID Protein 52078126
UniProtKB/Swiss-Prot ID Q9C0D9
UniProtKB/Swiss-Prot Entry Name EPT1_HUMAN
PDB IDs Not Available
GenBank Gene ID BK001426
GeneCard ID EPT1
GenAtlas ID EPT1
HGNC ID HGNC:29361
References
General References
  1. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  2. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: 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. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed:11214970 ]
  3. Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed:12775843 ]
  4. Horibata Y, Hirabayashi Y: Identification and characterization of human ethanolaminephosphotransferase1. J Lipid Res. 2007 Mar;48(3):503-8. Epub 2006 Nov 28. [PubMed:17132865 ]