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P05374

- CHO2_YEAST

UniProt

P05374 - CHO2_YEAST

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Protein

Phosphatidylethanolamine N-methyltransferase

Gene

CHO2

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

Functioni

Catalyzes the first step in the conversion of phosphatidylethanolamine to phosphatidylcholine during the methylation pathway of phosphatidylcholine biosynthesis. Preferentially converts di-C16:1 substrates.7 Publications

Catalytic activityi

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.

Kineticsi

  1. KM=60 µM for S-adenosyl-L-methionine1 Publication

pH dependencei

Optimum pH is 9.9.1 Publication

Pathwayi

GO - Molecular functioni

  1. phosphatidylethanolamine N-methyltransferase activity Source: SGD

GO - Biological processi

  1. phosphatidylcholine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16680.
YEAST:YGR157W-MONOMER.
UniPathwayiUPA00753.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylethanolamine N-methyltransferase (EC:2.1.1.17)
Short name:
PEAMT
Alternative name(s):
Choline-requiring protein 2
Gene namesi
Name:CHO2
Synonyms:PEM1
Ordered Locus Names:YGR157W
ORF Names:G6673
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR157w.
SGDiS000003389. CHO2.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 869868Phosphatidylethanolamine N-methyltransferasePRO_0000058304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP05374.
PaxDbiP05374.
PeptideAtlasiP05374.

Expressioni

Inductioni

Repressed by myo-inositol and choline.2 Publications

Gene expression databases

GenevestigatoriP05374.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGP1P253761EBI-2049142,EBI-2357
CHO1P084561EBI-2049142,EBI-14055
ELO1P395401EBI-2049142,EBI-2049096
ERG11P106141EBI-2049142,EBI-5127
OST1P415431EBI-2049142,EBI-12651
PMP2P409751EBI-2049142,EBI-2043041
RTN1Q049471EBI-2049142,EBI-38020
SAC1P323681EBI-2049142,EBI-16210
SPF1P399861EBI-2049142,EBI-3128
YHR080CP388001EBI-2049142,EBI-24597

Protein-protein interaction databases

BioGridi33405. 354 interactions.
DIPiDIP-8037N.
IntActiP05374. 2 interactions.
MINTiMINT-1358409.
STRINGi4932.YGR157W.

Structurei

3D structure databases

ProteinModelPortaliP05374.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 5554ExtracellularSequence AnalysisAdd
BLAST
Topological domaini77 – 8610CytoplasmicSequence Analysis
Topological domaini108 – 18780ExtracellularSequence AnalysisAdd
BLAST
Topological domaini209 – 2124CytoplasmicSequence Analysis
Topological domaini234 – 25825ExtracellularSequence AnalysisAdd
BLAST
Topological domaini280 – 29112CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini311 – 36252ExtracellularSequence AnalysisAdd
BLAST
Topological domaini384 – 3896CytoplasmicSequence Analysis
Topological domaini411 – 43929ExtracellularSequence AnalysisAdd
BLAST
Topological domaini461 – 4633CytoplasmicSequence Analysis
Topological domaini485 – 53450ExtracellularSequence AnalysisAdd
BLAST
Topological domaini556 – 869314CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei56 – 7621HelicalSequence AnalysisAdd
BLAST
Transmembranei87 – 10721HelicalSequence AnalysisAdd
BLAST
Transmembranei188 – 20821HelicalSequence AnalysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence AnalysisAdd
BLAST
Transmembranei259 – 27921HelicalSequence AnalysisAdd
BLAST
Transmembranei292 – 31019HelicalSequence AnalysisAdd
BLAST
Transmembranei363 – 38321HelicalSequence AnalysisAdd
BLAST
Transmembranei390 – 41021HelicalSequence AnalysisAdd
BLAST
Transmembranei440 – 46021HelicalSequence AnalysisAdd
BLAST
Transmembranei464 – 48421HelicalSequence AnalysisAdd
BLAST
Transmembranei535 – 55521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG68139.
InParanoidiP05374.
KOiK16369.
OMAiEAWRQWK.
OrthoDBiEOG73Z333.

Family and domain databases

InterProiIPR007318. Phopholipid_MeTrfase.
IPR016219. Phosphatid-EA_MeTrfase_fun.
[Graphical view]
PfamiPF04191. PEMT. 2 hits.
[Graphical view]
PIRSFiPIRSF000383. PEAMT. 1 hit.
PROSITEiPS51598. SAM_CHO2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05374-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSCKTTLSE MVGSVTKDRG TINVEARTRS SNVTFKPPVT HDMVRSLFDP
60 70 80 90 100
TLKKSLLEKC IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN
110 120 130 140 150
LGIGLVLHYQ SHYETLTNCA KTHAIFSKIP QNKDANSNFS TNSNSFSEKF
160 170 180 190 200
WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN VWLIFRQFVD LILMQDFVTY
210 220 230 240 250
IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV VKDYAWYWGD
260 270 280 290 300
FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH
310 320 330 340 350
YSQFLFLKYV ENPHIERTYG DGTDSDSQMN SRIDDLISKE NYDYSRPLIN
360 370 380 390 400
MGLSFNNFNK LRFTDYFTIG TVAALMLGTI MNARFINLNY LFITVFVTKL
410 420 430 440 450
VSWLFISTIL YKQSQSKWFT RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT
460 470 480 490 500
LMIIHTGLQI WSNFSNINNS QLIFGLILVA LQTWCDKETR LAISDFGWFY
510 520 530 540 550
GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL MTNFAVTNII
560 570 580 590 600
LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI
610 620 630 640 650
VNRIENIIIK SLVDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR
660 670 680 690 700
LSPYCELKIE NEQVETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR
710 720 730 740 750
ADREKTRVGS GGHWSATSKD SYMNHGLRHK ESVTEIKATE KYVQGKVTFD
760 770 780 790 800
TSLLYFENGI YEFRYHSGNS HKVLLISTPF EISLPVLNTT TPELFEKDLT
810 820 830 840 850
EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS SEYMRRVNGD
860
AHVISHRAWD IKQTLDSLA
Length:869
Mass (Da):101,204
Last modified:November 1, 1988 - v1
Checksum:iA273F179B4E46A20
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16987 Genomic DNA. Translation: AAA34850.1.
X85807 Genomic DNA. Translation: CAA59814.1.
Z72942 Genomic DNA. Translation: CAA97171.1.
BK006941 Genomic DNA. Translation: DAA08248.1.
PIRiA28443.
RefSeqiNP_011673.1. NM_001181286.1.

Genome annotation databases

EnsemblFungiiYGR157W; YGR157W; YGR157W.
GeneIDi853061.
KEGGisce:YGR157W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16987 Genomic DNA. Translation: AAA34850.1 .
X85807 Genomic DNA. Translation: CAA59814.1 .
Z72942 Genomic DNA. Translation: CAA97171.1 .
BK006941 Genomic DNA. Translation: DAA08248.1 .
PIRi A28443.
RefSeqi NP_011673.1. NM_001181286.1.

3D structure databases

ProteinModelPortali P05374.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33405. 354 interactions.
DIPi DIP-8037N.
IntActi P05374. 2 interactions.
MINTi MINT-1358409.
STRINGi 4932.YGR157W.

Proteomic databases

MaxQBi P05374.
PaxDbi P05374.
PeptideAtlasi P05374.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR157W ; YGR157W ; YGR157W .
GeneIDi 853061.
KEGGi sce:YGR157W.

Organism-specific databases

CYGDi YGR157w.
SGDi S000003389. CHO2.

Phylogenomic databases

eggNOGi NOG68139.
InParanoidi P05374.
KOi K16369.
OMAi EAWRQWK.
OrthoDBi EOG73Z333.

Enzyme and pathway databases

UniPathwayi UPA00753 .
BioCyci MetaCyc:MONOMER-16680.
YEAST:YGR157W-MONOMER.

Miscellaneous databases

NextBioi 972998.

Gene expression databases

Genevestigatori P05374.

Family and domain databases

InterProi IPR007318. Phopholipid_MeTrfase.
IPR016219. Phosphatid-EA_MeTrfase_fun.
[Graphical view ]
Pfami PF04191. PEMT. 2 hits.
[Graphical view ]
PIRSFi PIRSF000383. PEAMT. 1 hit.
PROSITEi PS51598. SAM_CHO2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes."
    Kodaki T., Yamashita S.
    J. Biol. Chem. 262:15428-15435(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames."
    Skala J., Nawrocki A., Goffeau A.
    Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  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. "Regulation of phosphatidylethanolamine methyltransferase level by myo-inositol in Saccaromyces cerevisiae."
    Yamashita S., Oshima A.
    Eur. J. Biochem. 104:611-616(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Regulation of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae."
    Yamashita S., Oshima A., Nikawa J., Hosaka K.
    Eur. J. Biochem. 128:589-595(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Expression of the Saccharomyces cerevisiae inositol-1-phosphate synthase (INO1) gene is regulated by factors that affect phospholipid synthesis."
    Hirsch J.P., Henry S.A.
    Mol. Cell. Biol. 6:3320-3328(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Saccharomyces cerevisiae cho2 mutants are deficient in phospholipid methylation and cross-pathway regulation of inositol synthesis."
    Summers E.F., Letts V.A., McGraw P., Henry S.A.
    Genetics 120:909-922(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Inositol regulates phosphatidylglycerolphosphate synthase expression in Saccharomyces cerevisiae."
    Greenberg M.L., Hubbell S., Lam C.
    Mol. Cell. Biol. 8:4773-4779(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Characterization of the methyltransferases in the yeast phosphatidylethanolamine methylation pathway by selective gene disruption."
    Kodaki T., Yamashita S.
    Eur. J. Biochem. 185:243-251(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Regulation of phosphatidylethanolamine methyltransferase and phospholipid methyltransferase by phospholipid precursors in Saccharomyces cerevisiae."
    Gaynor P.M., Gill T., Toutenhoofd S., Summers E.F., McGraw P., Homann M.J., Henry S.A., Carman G.M.
    Biochim. Biophys. Acta 1090:326-332(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. "Identification of the upstream activation sequences responsible for the expression and regulation of the PEM1 and PEM2 genes encoding the enzymes of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae."
    Kodaki T., Hosaka K., Nikawa J., Yamashita S.
    J. Biochem. 109:276-287(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. "The yeast phospholipid N-methyltransferases catalyzing the synthesis of phosphatidylcholine preferentially convert di-C16:1 substrates both in vivo and in vitro."
    Boumann H.A., Chin P.T., Heck A.J., De Kruijff B., De Kroon A.I.
    J. Biol. Chem. 279:40314-40319(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHO2_YEAST
AccessioniPrimary (citable) accession number: P05374
Secondary accession number(s): D6VUT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 29, 2014
This is version 117 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 1810 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

External Data

Dasty 3