Q9Y6K0 (CEPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Choline/ethanolaminephosphotransferase 1
Short name=hCEPT1
EC=2.7.8.1
EC=2.7.8.2

Gene names

Name:	CEPT1
ORF Names:	PRO1101

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.6
Catalytic activity	CDP-ethanolamine + 1,2-diacylglycerol = CMP + a phosphatidylethanolamine. Ref.1 CDP-choline + 1,2-diacylglycerol = CMP + a phosphatidylcholine. Ref.1
Cofactor	Magnesium or manganese. Ref.1
Pathway	Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3. Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein Ref.8.
Tissue specificity	Ubiquitously expressed. Ref.1
Sequence similarities	Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Biophysicochemical properties	Kinetic parameters: KM=37 µM for CDP-choline Ref.1 Ref.7 KM=101 µM for CDP-ethanolamine Vmax=10.5 nmol/min/mg enzyme with CDP-choline as substrate Vmax=4.35 nmol/min/mg enzyme with CDP-ethanolamine as substrate
Sequence caution	The sequence AAF61194.1 differs from that shown. Reason: Frameshift at position 276.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane Nucleus
Domain	Transmembrane Transmembrane helix
Ligand	Magnesium Manganese Metal-binding
Molecular function	Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Traceable author statement. Source: ProtInc nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	diacylglycerol cholinephosphotransferase activity Inferred from electronic annotation. Source: EC ethanolaminephosphotransferase activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 416	416	Choline/ethanolaminephosphotransferase 1		PRO_0000289245
Regions
	Transmembrane	87 – 107	21	Helical; Potential
	Transmembrane	115 – 135	21	Helical; Potential
	Transmembrane	186 – 206	21	Helical; Potential
	Transmembrane	209 – 229	21	Helical; Potential
	Transmembrane	239 – 259	21	Helical; Potential
	Transmembrane	283 – 303	21	Helical; Potential
	Transmembrane	317 – 337	21	Helical; Potential
	Transmembrane	365 – 385	21	Helical; Potential
Amino acid modifications
	Modified residue	18	1	Phosphoserine Ref.9
	Modified residue	40	1	Phosphothreonine Ref.9
	Glycosylation	144	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	138	1	K → M: Induces a reduction in both cholinephosphotransferase and ethanolaminephosphotransferase activities.
	Mutagenesis	144	1	N → G: No effect. Ref.8
	Mutagenesis	146	1	S → Q or C: No effect. Ref.8
	Mutagenesis	156	1	G → C, S or A: Induces a reduction in cholinephosphotransferase activity and abolishes ethanolaminephosphotransferase activity. Ref.8
	Mutagenesis	214	1	T → A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity. Ref.8
	Mutagenesis	215	1	E → A or D: Induces a strong reduction in enzyme activity without altering diacylglycerol specificity. Ref.8
	Mutagenesis	215	1	E → Q: Induces a strong reduction in enzyme activity and alters diacylglycerol specificity. Ref.8
	Mutagenesis	216	1	V → A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity. Ref.8
	Mutagenesis	221	1	I → A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity. Ref.8
	Mutagenesis	226	1	L → A: Does not affect either the enzyme activity or the diacylglycerol specificity. Ref.8
	Mutagenesis	228	1	V → A: Does not affect either the enzyme activity or the diacylglycerol specificity. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6K0 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: A25FED1193342FD9	FASTA	416	46,554
	10 20 30 40 50 60 MSGHRSTRKR CGDSHPESPV GFGHMSTTGC VLNKLFQLPT PPLSRHQLKR LEEHRYQSAG 70 80 90 100 110 120 RSLLEPLMQG YWEWLVRRVP SWIAPNLITI IGLSINICTT ILLVFYCPTA TEQAPLWAYI 130 140 150 160 170 180 ACACGLFIYQ SLDAIDGKQA RRTNSSSPLG ELFDHGCDSL STVFVVLGTC IAVQLGTNPD 190 200 210 220 230 240 WMFFCCFAGT FMFYCAHWQT YVSGTLRFGI IDVTEVQIFI IIMHLLAVIG GPPFWQSMIP 250 260 270 280 290 300 VLNIQMKIFP ALCTVAGTIF SCTNYFRVIF TGGVGKNGST IAGTSVLSPF LHIGSVITLA 310 320 330 340 350 360 AMIYKKSAVQ LFEKHPCLYI LTFGFVSAKI TNKLVVAHMT KSEMHLHDTA FIGPALLFLD 370 380 390 400 410 QYFNSFIDEY IVLWIALVFS FFDLIRYCVS VCNQIASHLH IHVFRIKVST AHSNHH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10191259] [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: 16710414] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Pancreas.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] 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: 10893425] [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: 12216837] [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: 12221122] [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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-40, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00005775.
RefSeq	NP_001007795.1. NM_001007794.1. NP_006081.1. NM_006090.3.
UniGene	Hs.363572. Hs.636850.
3D structure databases
ProteinModelPortal	Q9Y6K0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y6K0. 2 interactions.
STRING	Q9Y6K0.
PTM databases
PhosphoSite	Q9Y6K0.
Polymorphism databases
DMDM	74753524.
Proteomic databases
PRIDE	Q9Y6K0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357172; ENSP00000349696; ENSG00000134255.
GeneID	10390.
KEGG	hsa:10390.
UCSC	uc001eah.1. human.
Organism-specific databases
CTD	10390.
GeneCards	GC01P111682.
H-InvDB	HIX0000871.
HGNC	HGNC:24289. CEPT1.
neXtProt	NX_Q9Y6K0.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16251.
GeneTree	ENSGT00530000063048.
HOGENOM	HBG386512.
HOVERGEN	HBG107647.
InParanoid	Q9Y6K0.
OMA	CCFAGMF.
OrthoDB	EOG4V6ZGJ.
PhylomeDB	Q9Y6K0.
Gene expression databases
ArrayExpress	Q9Y6K0.
Bgee	Q9Y6K0.
CleanEx	HS_CEPT1.
Genevestigator	Q9Y6K0.
Family and domain databases
InterPro	IPR000462. CDP-OH_P_trans. IPR014472. CHOPT. [Graphical view]
KO	K13644.
Pfam	PF01066. CDP-OH_P_transf. 1 hit. [Graphical view]
PIRSF	PIRSF015665. CHOPT. 1 hit.
PROSITE	PS00379. CDP_ALCOHOL_P_TRANSF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00122. Choline.
NextBio	39360.

Entry information

Entry name

CEPT1_HUMAN

Accession

Primary (citable) accession number: Q9Y6K0
Secondary accession number(s): Q69YJ9, Q9P0Y8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 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.