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P38272

- SHE3_YEAST

UniProt

P38272 - SHE3_YEAST

Protein

SWI5-dependent HO expression protein 3

Gene

SHE3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into the emerging bud.11 Publications

    GO - Molecular functioni

    1. mRNA binding Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. endoplasmic reticulum inheritance Source: SGD
    2. intracellular mRNA localization Source: SGD
    3. mating type switching Source: SGD
    4. mRNA transport Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA transport, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29085-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SWI5-dependent HO expression protein 3
    Gene namesi
    Name:SHE3
    Ordered Locus Names:YBR130C
    ORF Names:YBR1005
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR130c.
    SGDiS000000334. SHE3.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Peripheral membrane protein 2 Publications

    GO - Cellular componenti

    1. cellular bud tip Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi343 – 3431S → E: Prevents correct localization of ASH1 mRNA; when associated with E-361. 1 Publication
    Mutagenesisi348 – 3481S → E: Prevents correct localization of ASH1 mRNA. 1 Publication
    Mutagenesisi361 – 3611S → E: Prevents correct localization of ASH1 mRNA; when associated with E-343. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 425425SWI5-dependent HO expression protein 3PRO_0000202490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei343 – 3431Phosphoserine2 Publications
    Modified residuei394 – 3941Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38272.
    PaxDbiP38272.
    PeptideAtlasiP38272.
    PRIDEiP38272.

    Expressioni

    Gene expression databases

    GenevestigatoriP38272.

    Interactioni

    Subunit structurei

    Interacts with SHE2 and MYO4.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MYO4P324927EBI-21600,EBI-11681
    SHE2P360683EBI-21600,EBI-26866

    Protein-protein interaction databases

    BioGridi32831. 63 interactions.
    DIPiDIP-2037N.
    IntActiP38272. 17 interactions.
    MINTiMINT-572712.
    STRINGi4932.YBR130C.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 7128
    Helixi74 – 13461

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LL7X-ray2.31A/B/C/D/E/F/G/H42-137[»]
    4LL8X-ray3.58B/E81-311[»]
    ProteinModelPortaliP38272.
    SMRiP38272. Positions 43-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili68 – 197130Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi377 – 3815Poly-Ser

    Sequence similaritiesi

    Belongs to the SHE3 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG130615.
    OMAiFMANLES.
    OrthoDBiEOG7J44J8.

    Sequencei

    Sequence statusi: Complete.

    P38272-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDQDNTQTS SSKLAPHHNI FMANLESSPT KDRNTSSQNA SSSRVIESLH    50
    DQIDMLTKTN LQLTTQSQNL LSKLELAQSK ESKLLENLNL LKNENENLNS 100
    IFERKNKKLK ELEKDYSELS NRYNEQKEKM DQLSKLAKNS SAIEQSCSEK 150
    LQNMEVNYNS LLESQNLYRD HYSDEISKLN EKIGLLELEL SNQNLNYGSD 200
    TSSNSDIELN LNKFNDSVKD LKSLETEKDS KLSKIITHSL DELNLQSWLN 250
    LYQTNENLIS TFAEKMDLKD VLKRNDEKIS NKGAVVQTLK KNVQTQVESN 300
    NADALSSNNA QDMLPIKMVK LRKTPNTNDS SSNGNSSNNK RRSFYTASPL 350
    LSSGSIPKSA SPVLPGVKRT ASVRKPSSSS SKTNVTHNND PSTSPTISVP 400
    PGVTRTVSST HKKKGNSMVV HGAQS 425
    Length:425
    Mass (Da):47,417
    Last modified:October 1, 1994 - v1
    Checksum:i590404D2E140BB7A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75891 Genomic DNA. Translation: CAA53489.1.
    Z35999 Genomic DNA. Translation: CAA85087.1.
    BK006936 Genomic DNA. Translation: DAA07247.1.
    PIRiS45999.
    RefSeqiNP_009688.3. NM_001178478.3.

    Genome annotation databases

    EnsemblFungiiYBR130C; YBR130C; YBR130C.
    GeneIDi852427.
    KEGGisce:YBR130C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75891 Genomic DNA. Translation: CAA53489.1 .
    Z35999 Genomic DNA. Translation: CAA85087.1 .
    BK006936 Genomic DNA. Translation: DAA07247.1 .
    PIRi S45999.
    RefSeqi NP_009688.3. NM_001178478.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4LL7 X-ray 2.31 A/B/C/D/E/F/G/H 42-137 [» ]
    4LL8 X-ray 3.58 B/E 81-311 [» ]
    ProteinModelPortali P38272.
    SMRi P38272. Positions 43-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32831. 63 interactions.
    DIPi DIP-2037N.
    IntActi P38272. 17 interactions.
    MINTi MINT-572712.
    STRINGi 4932.YBR130C.

    Proteomic databases

    MaxQBi P38272.
    PaxDbi P38272.
    PeptideAtlasi P38272.
    PRIDEi P38272.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR130C ; YBR130C ; YBR130C .
    GeneIDi 852427.
    KEGGi sce:YBR130C.

    Organism-specific databases

    CYGDi YBR130c.
    SGDi S000000334. SHE3.

    Phylogenomic databases

    eggNOGi NOG130615.
    OMAi FMANLES.
    OrthoDBi EOG7J44J8.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29085-MONOMER.

    Miscellaneous databases

    NextBioi 971303.

    Gene expression databases

    Genevestigatori P38272.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "The sequence of 29.7 kb from the right arm of chromosome II reveals 13 complete open reading frames, of which ten correspond to new genes."
      Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F., Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M., Herbert C.J.
      Yeast 10:S1-S11(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: FUNCTION.
    5. "Localization and anchoring of mRNA in budding yeast."
      Beach D.L., Salmon E.D., Bloom K.
      Curr. Biol. 9:569-578(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins."
      Munchow S., Sauter C., Jansen R.P.
      J. Cell Sci. 112:1511-1518(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p."
      Bohl F., Kruse C., Frank A., Ferring D., Jansen R.P.
      EMBO J. 19:5514-5524(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SHE2 AND MYO4.
    8. "She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA."
      Long R.M., Gu W., Lorimer E., Singer R.H., Chartrand P.
      EMBO J. 19:6592-6601(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH SHE2.
    9. "The myosin motor, Myo4p, binds Ash1 mRNA via the adapter protein, She3p."
      Takizawa P.A., Vale R.D.
      Proc. Natl. Acad. Sci. U.S.A. 97:5273-5278(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, INTERACTION WITH MYO4.
    10. "Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p."
      Kruse C., Jaedicke A., Beaudouin J., Bohl F., Ferring D., Guttler T., Ellenberg J., Jansen R.P.
      J. Cell Biol. 159:971-982(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Myo4p and She3p are required for cortical ER inheritance in Saccharomyces cerevisiae."
      Estrada P., Kim J., Coleman J., Walker L., Dunn B., Takizawa P., Novick P., Ferro-Novick S.
      J. Cell Biol. 163:1255-1266(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex."
      Gonsalvez G.B., Lehmann K.A., Ho D.K., Stanitsa E.S., Williamson J.R., Long R.M.
      RNA 9:1383-1399(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SHE2.
    14. "ASH1 mRNA anchoring requires reorganization of the Myo4p-She3p-She2p transport complex."
      Gonsalvez G.B., Little J.L., Long R.M.
      J. Biol. Chem. 279:46286-46294(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Coordination of endoplasmic reticulum and mRNA localization to the yeast bud."
      Schmid M., Jaedicke A., Du T.G., Jansen R.P.
      Curr. Biol. 16:1538-1543(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    17. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "She3p possesses a novel activity required for ASH1 mRNA localization in Saccharomyces cerevisiae."
      Landers S.M., Gallas M.R., Little J., Long R.M.
      Eukaryot. Cell 8:1072-1083(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF SER-343; SER-348 AND SER-361.
    20. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "The structure of the Myo4p globular tail and its function in ASH1 mRNA localization."
      Heuck A., Fetka I., Brewer D.N., Huls D., Munson M., Jansen R.P., Niessing D.
      J. Cell Biol. 189:497-510(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYO4.

    Entry informationi

    Entry nameiSHE3_YEAST
    AccessioniPrimary (citable) accession number: P38272
    Secondary accession number(s): D6VQC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 110 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 1010 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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 II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3