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P53938

- EOS1_YEAST

UniProt

P53938 - EOS1_YEAST

Protein

N-glycosylation protein EOS1

Gene

EOS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in oxidative stress resistance and N-glycosylation.1 Publication

    GO - Biological processi

    1. cellular response to oxidative stress Source: SGD
    2. protein N-linked glycosylation Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33109-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-glycosylation protein EOS1
    Alternative name(s):
    ER-localized and oxidants sensitive protein 1
    Gene namesi
    Name:EOS1
    Ordered Locus Names:YNL080C
    ORF Names:N2327
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL080c.
    SGDiS000005024. EOS1.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: SGD
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366N-glycosylation protein EOS1PRO_0000203446Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP53938.
    PaxDbiP53938.

    Expressioni

    Gene expression databases

    GenevestigatoriP53938.

    Interactioni

    Protein-protein interaction databases

    BioGridi35743. 186 interactions.
    IntActiP53938. 1 interaction.
    STRINGi4932.YNL080C.

    Structurei

    3D structure databases

    ProteinModelPortaliP53938.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 136136LumenalSequence AnalysisAdd
    BLAST
    Topological domaini158 – 16710CytoplasmicSequence Analysis
    Topological domaini189 – 1957LumenalSequence Analysis
    Topological domaini217 – 321105CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini343 – 36624LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei137 – 15721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei168 – 18821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei196 – 21621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei322 – 34221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the EOS1 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46394.
    HOGENOMiHOG000248035.
    OMAiHTWILIS.
    OrthoDBiEOG7DFXP8.

    Family and domain databases

    InterProiIPR021100. N-glycosylation_EOS1.
    [Graphical view]
    PfamiPF12326. EOS1. 1 hit.
    [Graphical view]
    PRINTSiPR02070. NGLYCOSEOS1.

    Sequencei

    Sequence statusi: Complete.

    P53938-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTWILSTGMG PHEDKYAKHE RATFKKTYSS MKTLSLNHLT AKQHMLMALC    50
    RDISLLPPLT YIFTSLRKAW RVSMRTSITL YEPQSLRDAF TYFWQKLNSA 100
    YDNNSSFEGA SQKAVNGDGK DSLLLSALTT ARASEYLLCS LWCLVSLYLS 150
    YAILDSLMVR WIVKYSTVAA ILRMFSMSLI IVTLELLLLS SLSPELDYFL 200
    HTWILISCVL TAVYIWQSYL TSDLRYIRNQ EGEVQEDTNV PEETEDYEDG 250
    EDDADEDSHV VVADESTVDV PSNDSLSDNS DGGLFPVNRP SVSHSQSPKR 300
    PKKYPKKAFN FTTKRTIDLY KITVLCVVPV GLASFITMLG LLRNLFIQRL 350
    DVEQLERILH EMHPPA 366
    Length:366
    Mass (Da):41,674
    Last modified:October 1, 1996 - v1
    Checksum:iCFE1BA51A638DF5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ115393 Genomic DNA. Translation: AAZ22528.1.
    X86470 Genomic DNA. Translation: CAA60178.1.
    Z71356 Genomic DNA. Translation: CAA95954.1.
    BK006947 Genomic DNA. Translation: DAA10465.1.
    PIRiS53898.
    RefSeqiNP_014319.1. NM_001182918.1.

    Genome annotation databases

    EnsemblFungiiYNL080C; YNL080C; YNL080C.
    GeneIDi855644.
    KEGGisce:YNL080C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ115393 Genomic DNA. Translation: AAZ22528.1 .
    X86470 Genomic DNA. Translation: CAA60178.1 .
    Z71356 Genomic DNA. Translation: CAA95954.1 .
    BK006947 Genomic DNA. Translation: DAA10465.1 .
    PIRi S53898.
    RefSeqi NP_014319.1. NM_001182918.1.

    3D structure databases

    ProteinModelPortali P53938.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35743. 186 interactions.
    IntActi P53938. 1 interaction.
    STRINGi 4932.YNL080C.

    Proteomic databases

    MaxQBi P53938.
    PaxDbi P53938.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL080C ; YNL080C ; YNL080C .
    GeneIDi 855644.
    KEGGi sce:YNL080C.

    Organism-specific databases

    CYGDi YNL080c.
    SGDi S000005024. EOS1.

    Phylogenomic databases

    eggNOGi NOG46394.
    HOGENOMi HOG000248035.
    OMAi HTWILIS.
    OrthoDBi EOG7DFXP8.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33109-MONOMER.

    Miscellaneous databases

    NextBioi 979878.

    Gene expression databases

    Genevestigatori P53938.

    Family and domain databases

    InterProi IPR021100. N-glycosylation_EOS1.
    [Graphical view ]
    Pfami PF12326. EOS1. 1 hit.
    [Graphical view ]
    PRINTSi PR02070. NGLYCOSEOS1.
    ProtoNeti Search...

    Publicationsi

    1. "Quantitative trait loci mapped to single-nucleotide resolution in yeast."
      Deutschbauer A.M., Davis R.W.
      Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SK1.
    2. "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs."
      Poehlmann R., Philippsen P.
      Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(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. "Analysis of deletion phenotypes and GFP fusions of 21 novel Saccharomyces cerevisiae open reading frames."
      Brachat A., Liebundguth N., Rebischung C., Lemire S., Schaerer F., Hoepfner D., Demchyshyn V., Howald I., Duesterhoeft A., Moestl D., Poehlmann R., Koetter P., Hall M.N., Wach A., Philippsen P.
      Yeast 16:241-253(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "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.
    8. "EOS1, whose deletion confers sensitivity to oxidative stress, is involved in N-glycosylation in Saccharomyces cerevisiae."
      Nakamura T., Ando A., Takagi H., Shima J.
      Biochem. Biophys. Res. Commun. 353:293-298(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
      Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
      Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEOS1_YEAST
    AccessioniPrimary (citable) accession number: P53938
    Secondary accession number(s): D6W199, Q45TY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 85 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 937 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3