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8GYW

Cryo-EM structure of human CEPT1 complexed with CDP-choline

Functional Information from GO Data
ChainGOidnamespacecontents
A0004142molecular_functiondiacylglycerol cholinephosphotransferase activity
A0004307molecular_functionethanolaminephosphotransferase activity
A0005737cellular_componentcytoplasm
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0006629biological_processlipid metabolic process
A0006646biological_processphosphatidylethanolamine biosynthetic process
A0006656biological_processphosphatidylcholine biosynthetic process
A0006657biological_processCDP-choline pathway
A0008654biological_processphospholipid biosynthetic process
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
A0031965cellular_componentnuclear membrane
A0046872molecular_functionmetal ion binding
A0047359molecular_function1-alkenyl-2-acylglycerol choline phosphotransferase activity
B0004142molecular_functiondiacylglycerol cholinephosphotransferase activity
B0004307molecular_functionethanolaminephosphotransferase activity
B0005737cellular_componentcytoplasm
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0006629biological_processlipid metabolic process
B0006646biological_processphosphatidylethanolamine biosynthetic process
B0006656biological_processphosphatidylcholine biosynthetic process
B0006657biological_processCDP-choline pathway
B0008654biological_processphospholipid biosynthetic process
B0012505cellular_componentendomembrane system
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
B0031965cellular_componentnuclear membrane
B0046872molecular_functionmetal ion binding
B0047359molecular_function1-alkenyl-2-acylglycerol choline phosphotransferase activity
Functional Information from PROSITE/UniProt
site_idPS00379
Number of Residues23
DetailsCDP_ALCOHOL_P_TRANSF CDP-alcohol phosphatidyltransferases signature. DGkqARrtnsssplGelfDhgcD
ChainResidueDetails
BASP136-ASP158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues378
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"37137909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GYX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"37137909","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37137909","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37137909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GYW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GYX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Increases basicity of active site His","evidences":[{"source":"UniProtKB","id":"Q4KLV1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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