Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ethanolamine-phosphate cytidylyltransferase

Gene

ECT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ethanolamine-phosphate cytidylyltransferase which catalyzes the second step of phosphatidylethanolamine biosynthesis. Involved in the maintenance of plasma membrane and required for proper sporulation.2 Publications

Catalytic activityi

CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine.

Pathwayi: phosphatidylethanolamine biosynthesis

This protein is involved in step 2 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. Ethanolamine kinase (EKI1)
  2. Ethanolamine-phosphate cytidylyltransferase (ECT1)
  3. Choline/ethanolaminephosphotransferase 1 (EPT1)
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.

GO - Molecular functioni

  • ethanolamine-phosphate cytidylyltransferase activity Source: SGD

GO - Biological processi

  • phosphatidylethanolamine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciYEAST:YGR007W-MONOMER.
ReactomeiR-SCE-1483213. Synthesis of PE.
UniPathwayiUPA00558; UER00742.

Chemistry

SwissLipidsiSLP:000000067.

Names & Taxonomyi

Protein namesi
Recommended name:
Ethanolamine-phosphate cytidylyltransferase (EC:2.7.7.14)
Alternative name(s):
CTP:phosphoethanolamine cytidylyltransferase
Phosphorylethanolamine transferase
Gene namesi
Name:ECT1
Synonyms:MUQ1
Ordered Locus Names:YGR007W
ORF Names:G3856
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR007W.
SGDiS000003239. ECT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Ethanolamine-phosphate cytidylyltransferasePRO_0000208465Add
BLAST

Proteomic databases

MaxQBiP33412.
PeptideAtlasiP33412.

Expressioni

Inductioni

By isooctane.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi33251. 28 interactions.
MINTiMINT-4486677.

Structurei

3D structure databases

ProteinModelPortaliP33412.
SMRiP33412. Positions 7-319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytidylyltransferase family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075065.
HOGENOMiHOG000187618.
InParanoidiP33412.
KOiK00967.
OMAiCHGRTEI.
OrthoDBiEOG7XWPZQ.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_like. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

P33412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVNLDPDKV WIDGCFDFTH HGHAGAILQA RRTVSKENGK LFCGVHTDED
60 70 80 90 100
IQHNKGTPVM NSSERYEHTR SNRWCSEVVE AAPYVTDPNW MDKYQCQYVV
110 120 130 140 150
HGDDITIDAN GEDCYKLVKE MGRFKVVKRT YGVSTTEIIH RILTKKSLPP
160 170 180 190 200
THPDYYPTTQ ELSFYSVAQD AVSKHCYVFQ RDLDNVLVNG GYKFDAEDCV
210 220 230 240 250
YVDGDFDLFH MGDIDQLRKL KMDLHPDKKL IVGITTSDYS STIMTMKERV
260 270 280 290 300
LSVLSCKYVD AVIIDADATS MSQYNCEKYH IGTAVLTAAG KFSEYLTKEL
310 320
IVKRVESQRE VYIARNQKKG MSI
Length:323
Mass (Da):36,863
Last modified:February 1, 1994 - v1
Checksum:i9BC6DF97007EB689
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521S → I in BAA09310 (PubMed:8982874).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03536 Genomic DNA. Translation: AAA34916.1.
D50644 Genomic DNA. Translation: BAA09310.1.
Z72792 Genomic DNA. Translation: CAA96990.1.
AY557830 Genomic DNA. Translation: AAS56156.1.
BK006941 Genomic DNA. Translation: DAA08105.1.
PIRiB48067.
RefSeqiNP_011521.1. NM_001181136.1.

Genome annotation databases

EnsemblFungiiYGR007W; YGR007W; YGR007W.
GeneIDi852890.
KEGGisce:YGR007W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03536 Genomic DNA. Translation: AAA34916.1.
D50644 Genomic DNA. Translation: BAA09310.1.
Z72792 Genomic DNA. Translation: CAA96990.1.
AY557830 Genomic DNA. Translation: AAS56156.1.
BK006941 Genomic DNA. Translation: DAA08105.1.
PIRiB48067.
RefSeqiNP_011521.1. NM_001181136.1.

3D structure databases

ProteinModelPortaliP33412.
SMRiP33412. Positions 7-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33251. 28 interactions.
MINTiMINT-4486677.

Chemistry

SwissLipidsiSLP:000000067.

Proteomic databases

MaxQBiP33412.
PeptideAtlasiP33412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR007W; YGR007W; YGR007W.
GeneIDi852890.
KEGGisce:YGR007W.

Organism-specific databases

EuPathDBiFungiDB:YGR007W.
SGDiS000003239. ECT1.

Phylogenomic databases

GeneTreeiENSGT00550000075065.
HOGENOMiHOG000187618.
InParanoidiP33412.
KOiK00967.
OMAiCHGRTEI.
OrthoDBiEOG7XWPZQ.

Enzyme and pathway databases

UniPathwayiUPA00558; UER00742.
BioCyciYEAST:YGR007W-MONOMER.
ReactomeiR-SCE-1483213. Synthesis of PE.

Miscellaneous databases

NextBioi972553.
PROiP33412.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
InterProiIPR004821. Cyt_trans-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_like. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A U5 small nuclear ribonucleoprotein particle protein involved only in the second step of pre-mRNA splicing in Saccharomyces cerevisiae."
    Horowitz D.S., Abelson J.N.
    Mol. Cell. Biol. 13:2959-2970(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation and characterization of ECT1 gene encoding CTP: phosphoethanolamine cytidylyltransferase of Saccharomyces cerevisiae."
    Min-Seok R., Kawamata Y., Nakamura H., Ohta A., Takagi M.
    J. Biochem. 120:1040-1047(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: S288c / GRF88.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Screening of genes involved in isooctane tolerance in Saccharomyces cerevisiae by using mRNA differential display."
    Miura S., Zou W., Ueda M., Tanaka A.
    Appl. Environ. Microbiol. 66:4883-4889(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Respiratory deficiency mediates the regulation of CHO1-encoded phosphatidylserine synthase by mRNA stability in Saccharomyces cerevisiae."
    Choi H.-S., Carman G.M.
    J. Biol. Chem. 282:31217-31227(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Manipulation of major membrane lipid synthesis and its effects on sporulation in Saccharomyces cerevisiae."
    Deng L., Nagasawa J., Ono Y., Ishikawa Y., Kakihara T., Fukuda R., Ohta A.
    Biosci. Biotechnol. Biochem. 72:2362-2368(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Crystallization and preliminary X-ray analysis of CTP:phosphoethanolamine cytidylyltransferase (ECT) from Saccharomyces cerevisiae."
    Ohtsuka J., Nagata K., Lee W.C., Ono Y., Fukuda R., Ohta A., Tanokura M.
    Acta Crystallogr. F 62:1003-1005(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.

Entry informationi

Entry nameiECT1_YEAST
AccessioniPrimary (citable) accession number: P33412
Secondary accession number(s): D6VUE4, Q05725
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.