CEPT1
entrez
10390
canonical
uniprot
Q9Y6K0
canonical
ensembl
ENSG00000134255
resolver
ensp
ENSP00000349696
resolver
ensp
ENSP00000441980
resolver
ensp
ENSP00000515162
resolver
ensp
ENSP00000515163
resolver
ensp
ENSP00000544882
resolver
ensp
ENSP00000544883
resolver
ensp
ENSP00000544886
resolver
ensp
ENSP00000544887
resolver
ensp
ENSP00000544888
resolver
ensp
ENSP00000544889
resolver
ensp
ENSP00000609030
resolver
ensp
ENSP00000612399
resolver
ensp
ENSP00000612400
resolver
ensp
ENSP00000612401
resolver
enst
ENST00000357172
resolver
enst
ENST00000545121
resolver
enst
ENST00000700750
resolver
enst
ENST00000700751
resolver
enst
ENST00000874823
resolver
enst
ENST00000874824
resolver
enst
ENST00000874827
resolver
enst
ENST00000874828
resolver
enst
ENST00000874829
resolver
enst
ENST00000874830
resolver
enst
ENST00000938971
resolver
enst
ENST00000942340
resolver
enst
ENST00000942341
resolver
enst
ENST00000942342
resolver
genesymbol
CEPT1
resolver
hgnc
HGNC:24289
resolver
uniprot
A0A8V8TQ23
resolver
uniprot
A0A8V8TRF3
resolver
uniprot
Q69YJ9
resolver
uniprot
Q9P0Y8
resolver
uniprot_entry
A0A8V8TQ23_HUMAN
resolver
uniprot_entry
A0A8V8TRF3_HUMAN
resolver
uniprot_entry
CEPT1_HUMAN
resolver
uniprot_sec
Q69YJ9
resolver
uniprot_sec
Q9P0Y8
resolver
amino_acid_sequence
MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIPVLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH
uniprot
proteins
ec_number
2.7.8.1
uniprot
proteins
ec_number
2.7.8.2
uniprot
proteins
ec_number
2.7.8.22
uniprot
proteins
function
FUNCTION: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively (PubMed:10191259, PubMed:10893425, PubMed:12216837, PubMed:37137909). Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface (PubMed:10191259, PubMed:10893425, PubMed:12216837). Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity (PubMed:10191259, PubMed:12216837). {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:10893425, ECO:0000269|PubMed:12216837, ECO:0000269|PubMed:37137909}.
uniprot
proteins
mass_dalton
46554
uniprot
proteins
mutagenesis
MUTAGEN 86; /note="N->A: Strongly decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 136; /note="D->A: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 138; /note="K->M: Induces a reduction in both cholinephosphotransferase and ethanolaminephosphotransferase activities."; MUTAGEN 144; /note="N->G: No effect."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 146; /note="S->Q,C: No effect."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 151; /note="E->A: Strongly decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 154; /note="D->A: Abolished cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 156; /note="G->C,S,A: Induces a reduction in cholinephosphotransferase activity and abolishes ethanolaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 158; /note="D->A: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 162; /note="T->F: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 169; /note="T->N: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 196; /note="A->L: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 212; /note="D->A: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 214; /note="T->A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 215; /note="E->A,D: Induces a strong reduction in enzyme activity without altering diacylglycerol specificity."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 215; /note="E->Q: Induces a strong reduction in enzyme activity and alters diacylglycerol specificity."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 216; /note="V->A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity."; /evidence="ECO:0000269|PubMed:12221122, ECO:0000269|PubMed:37137909"; MUTAGEN 217; /note="Q->L: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 221; /note="I->A: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 226; /note="L->A: Does not affect either the enzyme activity or the diacylglycerol specificity."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 228; /note="V->A: Does not affect either the enzyme activity or the diacylglycerol specificity."; /evidence="ECO:0000269|PubMed:12221122"; MUTAGEN 261; /note="S->A: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909"; MUTAGEN 265; /note="Y->A: Decreased cholinephosphotransferase activity."; /evidence="ECO:0000269|PubMed:37137909
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3. {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:10893425}.; PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2. {ECO:0000269|PubMed:10191259, ECO:0000269|PubMed:10893425}.
uniprot
proteins
protein_family
CDP-alcohol phosphatidyltransferase class-I family
uniprot
proteins
pubmed
10191259
uniprot
proteins
pubmed
10893425
uniprot
proteins
pubmed
12216837
uniprot
proteins
pubmed
12221122
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
37137909
uniprot
proteins
sequence_length
416
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein {ECO:0000269|PubMed:12221122}. Nucleus membrane {ECO:0000269|PubMed:12221122}; Multi-pass membrane protein {ECO:0000269|PubMed:12221122}.
uniprot
proteins
transmembrane_region
TRANSMEM 89..108; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 116..133; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 156..176; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 180..199; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 210..230; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 246..267; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 286..306; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 315..334; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 349..363; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX"; TRANSMEM 368..388; /note="Helical"; /evidence="ECO:0000269|PubMed:37137909, ECO:0007744|PDB:8GYW, ECO:0007744|PDB:8GYX
uniprot
proteins