Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P05374

- CHO2_YEAST

UniProt

P05374 - CHO2_YEAST

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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.
    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

    MSSCKTTLSE MVGSVTKDRG TINVEARTRS SNVTFKPPVT HDMVRSLFDP    50
    TLKKSLLEKC IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN 100
    LGIGLVLHYQ SHYETLTNCA KTHAIFSKIP QNKDANSNFS TNSNSFSEKF 150
    WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN VWLIFRQFVD LILMQDFVTY 200
    IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV VKDYAWYWGD 250
    FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH 300
    YSQFLFLKYV ENPHIERTYG DGTDSDSQMN SRIDDLISKE NYDYSRPLIN 350
    MGLSFNNFNK LRFTDYFTIG TVAALMLGTI MNARFINLNY LFITVFVTKL 400
    VSWLFISTIL YKQSQSKWFT RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT 450
    LMIIHTGLQI WSNFSNINNS QLIFGLILVA LQTWCDKETR LAISDFGWFY 500
    GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL MTNFAVTNII 550
    LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI 600
    VNRIENIIIK SLVDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR 650
    LSPYCELKIE NEQVETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR 700
    ADREKTRVGS GGHWSATSKD SYMNHGLRHK ESVTEIKATE KYVQGKVTFD 750
    TSLLYFENGI YEFRYHSGNS HKVLLISTPF EISLPVLNTT TPELFEKDLT 800
    EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS SEYMRRVNGD 850
    AHVISHRAWD IKQTLDSLA 869
    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.
    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

    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 1, 2014
    This is version 116 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