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Protein

Choline/ethanolaminephosphotransferase 1

Gene

CEPT1

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

Functioni

Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity.2 Publications

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 Publication

Kineticsi

  1. KM=37 µM for CDP-choline2 Publications
  2. KM=101 µM for CDP-ethanolamine2 Publications
  1. Vmax=10.5 nmol/min/mg enzyme with CDP-choline as substrate2 Publications
  2. Vmax=4.35 nmol/min/mg enzyme with CDP-ethanolamine as substrate2 Publications

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.

Pathwayi: phosphatidylcholine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes phosphatidylcholine from phosphocholine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Choline-phosphate cytidylyltransferase A (PCYT1A), Choline-phosphate cytidylyltransferase B (PCYT1B)
  2. Cholinephosphotransferase 1 (CHPT1), Choline/ethanolaminephosphotransferase 1 (CEPT1)
This subpathway is part of the pathway phosphatidylcholine 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 phosphatidylcholine from phosphocholine, the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-HSA-1483191. Synthesis of PC.
R-HSA-1483213. Synthesis of PE.
SABIO-RKQ9Y6K0.
UniPathwayiUPA00558; UER00743.
UPA00753; UER00740.

Protein family/group databases

TCDBi4.F.1.1.1. the choline/ethanolaminephosphotransferase 1 (cept1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline/ethanolaminephosphotransferase 1 (EC:2.7.8.1, EC:2.7.8.2)
Short name:
hCEPT1
Gene namesi
Name:CEPT1
ORF Names:PRO1101
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24289. CEPT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei87 – 10721HelicalSequence analysisAdd
BLAST
Transmembranei115 – 13521HelicalSequence analysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence analysisAdd
BLAST
Transmembranei209 – 22921HelicalSequence analysisAdd
BLAST
Transmembranei239 – 25921HelicalSequence analysisAdd
BLAST
Transmembranei283 – 30321HelicalSequence analysisAdd
BLAST
Transmembranei317 – 33721HelicalSequence analysisAdd
BLAST
Transmembranei365 – 38521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: ProtInc
  • nuclear membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381K → M: Induces a reduction in both cholinephosphotransferase and ethanolaminephosphotransferase activities.
Mutagenesisi144 – 1441N → G: No effect. 1 Publication
Mutagenesisi146 – 1461S → Q or C: No effect. 1 Publication
Mutagenesisi156 – 1561G → C, S or A: Induces a reduction in cholinephosphotransferase activity and abolishes ethanolaminephosphotransferase activity. 1 Publication
Mutagenesisi214 – 2141T → A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity. 1 Publication
Mutagenesisi215 – 2151E → A or D: Induces a strong reduction in enzyme activity without altering diacylglycerol specificity. 1 Publication
Mutagenesisi215 – 2151E → Q: Induces a strong reduction in enzyme activity and alters diacylglycerol specificity. 1 Publication
Mutagenesisi216 – 2161V → A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity. 1 Publication
Mutagenesisi221 – 2211I → A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity. 1 Publication
Mutagenesisi226 – 2261L → A: Does not affect either the enzyme activity or the diacylglycerol specificity. 1 Publication
Mutagenesisi228 – 2281V → A: Does not affect either the enzyme activity or the diacylglycerol specificity. 1 Publication

Organism-specific databases

PharmGKBiPA134892657.

Chemistry

DrugBankiDB00122. Choline.

Polymorphism and mutation databases

BioMutaiCEPT1.
DMDMi74753524.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Choline/ethanolaminephosphotransferase 1PRO_0000289245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei40 – 401PhosphothreonineCombined sources
Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9Y6K0.
MaxQBiQ9Y6K0.
PaxDbiQ9Y6K0.
PRIDEiQ9Y6K0.

PTM databases

iPTMnetiQ9Y6K0.
PhosphoSiteiQ9Y6K0.
SwissPalmiQ9Y6K0.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ9Y6K0.
CleanExiHS_CEPT1.
ExpressionAtlasiQ9Y6K0. baseline and differential.
GenevisibleiQ9Y6K0. HS.

Organism-specific databases

HPAiHPA054432.

Interactioni

Protein-protein interaction databases

BioGridi115662. 29 interactions.
IntActiQ9Y6K0. 27 interactions.
STRINGi9606.ENSP00000349696.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6K0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2877. Eukaryota.
COG5050. LUCA.
GeneTreeiENSGT00530000063048.
HOGENOMiHOG000034808.
HOVERGENiHBG107647.
InParanoidiQ9Y6K0.
KOiK13644.
OMAiEYLVLWI.
OrthoDBiEOG7SR4MH.
PhylomeDBiQ9Y6K0.
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.

Q9Y6K0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGHRSTRKR CGDSHPESPV GFGHMSTTGC VLNKLFQLPT PPLSRHQLKR
60 70 80 90 100
LEEHRYQSAG RSLLEPLMQG YWEWLVRRVP SWIAPNLITI IGLSINICTT
110 120 130 140 150
ILLVFYCPTA TEQAPLWAYI ACACGLFIYQ SLDAIDGKQA RRTNSSSPLG
160 170 180 190 200
ELFDHGCDSL STVFVVLGTC IAVQLGTNPD WMFFCCFAGT FMFYCAHWQT
210 220 230 240 250
YVSGTLRFGI IDVTEVQIFI IIMHLLAVIG GPPFWQSMIP VLNIQMKIFP
260 270 280 290 300
ALCTVAGTIF SCTNYFRVIF TGGVGKNGST IAGTSVLSPF LHIGSVITLA
310 320 330 340 350
AMIYKKSAVQ LFEKHPCLYI LTFGFVSAKI TNKLVVAHMT KSEMHLHDTA
360 370 380 390 400
FIGPALLFLD QYFNSFIDEY IVLWIALVFS FFDLIRYCVS VCNQIASHLH
410
IHVFRIKVST AHSNHH
Length:416
Mass (Da):46,554
Last modified:November 1, 1999 - v1
Checksum:iA25FED1193342FD9
GO

Sequence cautioni

The sequence AAF61194.1 differs from that shown. Reason: Frameshift at position 276. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068302 mRNA. Translation: AAD25170.1.
AF138862 mRNA. Translation: AAF61194.1. Frameshift.
AL355816 Genomic DNA. Translation: CAI19367.1.
BC032610 mRNA. Translation: AAH32610.1.
BC049196 mRNA. Translation: AAH49196.1.
AL833102 mRNA. Translation: CAH10403.1.
CCDSiCCDS830.1.
RefSeqiNP_001007795.1. NM_001007794.1.
NP_006081.1. NM_006090.3.
XP_006710348.1. XM_006710285.2.
UniGeneiHs.363572.
Hs.636850.

Genome annotation databases

EnsembliENST00000357172; ENSP00000349696; ENSG00000134255.
ENST00000545121; ENSP00000441980; ENSG00000134255.
GeneIDi10390.
KEGGihsa:10390.
UCSCiuc001eah.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068302 mRNA. Translation: AAD25170.1.
AF138862 mRNA. Translation: AAF61194.1. Frameshift.
AL355816 Genomic DNA. Translation: CAI19367.1.
BC032610 mRNA. Translation: AAH32610.1.
BC049196 mRNA. Translation: AAH49196.1.
AL833102 mRNA. Translation: CAH10403.1.
CCDSiCCDS830.1.
RefSeqiNP_001007795.1. NM_001007794.1.
NP_006081.1. NM_006090.3.
XP_006710348.1. XM_006710285.2.
UniGeneiHs.363572.
Hs.636850.

3D structure databases

ProteinModelPortaliQ9Y6K0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115662. 29 interactions.
IntActiQ9Y6K0. 27 interactions.
STRINGi9606.ENSP00000349696.

Chemistry

DrugBankiDB00122. Choline.

Protein family/group databases

TCDBi4.F.1.1.1. the choline/ethanolaminephosphotransferase 1 (cept1) family.

PTM databases

iPTMnetiQ9Y6K0.
PhosphoSiteiQ9Y6K0.
SwissPalmiQ9Y6K0.

Polymorphism and mutation databases

BioMutaiCEPT1.
DMDMi74753524.

Proteomic databases

EPDiQ9Y6K0.
MaxQBiQ9Y6K0.
PaxDbiQ9Y6K0.
PRIDEiQ9Y6K0.

Protocols and materials databases

DNASUi10390.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357172; ENSP00000349696; ENSG00000134255.
ENST00000545121; ENSP00000441980; ENSG00000134255.
GeneIDi10390.
KEGGihsa:10390.
UCSCiuc001eah.1. human.

Organism-specific databases

CTDi10390.
GeneCardsiCEPT1.
HGNCiHGNC:24289. CEPT1.
HPAiHPA054432.
MIMi616751. gene.
neXtProtiNX_Q9Y6K0.
PharmGKBiPA134892657.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2877. Eukaryota.
COG5050. LUCA.
GeneTreeiENSGT00530000063048.
HOGENOMiHOG000034808.
HOVERGENiHBG107647.
InParanoidiQ9Y6K0.
KOiK13644.
OMAiEYLVLWI.
OrthoDBiEOG7SR4MH.
PhylomeDBiQ9Y6K0.
TreeFamiTF313270.

Enzyme and pathway databases

UniPathwayiUPA00558; UER00743.
UPA00753; UER00740.
ReactomeiR-HSA-1483191. Synthesis of PC.
R-HSA-1483213. Synthesis of PE.
SABIO-RKQ9Y6K0.

Miscellaneous databases

GenomeRNAii10390.
PROiQ9Y6K0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y6K0.
CleanExiHS_CEPT1.
ExpressionAtlasiQ9Y6K0. baseline and differential.
GenevisibleiQ9Y6K0. 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. "Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine."
    Henneberry A.L., McMaster C.R.
    Biochem. J. 339:291-298(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, TISSUE SPECIFICITY.
  2. "Functional prediction of the coding sequences of 5 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Zhou G., Wei H., Bi J., Xu W., Zai Y., Feng F., Liu M., He F.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal liver.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Lymph and Pancreas.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-162.
    Tissue: Bone marrow.
  6. "Cloning, genomic organization, and characterization of a human cholinephosphotransferase."
    Henneberry A.L., Wistow G., McMaster C.R.
    J. Biol. Chem. 275:29808-29815(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1)."
    Wright M.M., McMaster C.R.
    Lipids 37:663-672(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  8. "The major sites of cellular phospholipid synthesis and molecular determinants of fatty acid and lipid head group specificity."
    Henneberry A.L., Wright M.M., McMaster C.R.
    Mol. Biol. Cell 13:3148-3161(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-144; SER-146; GLY-156; THR-214; GLU-215; VAL-216; ILE-221; LEU-226 AND VAL-228.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCEPT1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6K0
Secondary accession number(s): Q69YJ9, Q9P0Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 126 of the entry and version 1 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 1
    Human chromosome 1: 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.