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P40073

- SHO1_YEAST

UniProt

P40073 - SHO1_YEAST

Protein

High osmolarity signaling protein SHO1

Gene

SHO1

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 127 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity. Detects changes in external osmolarity and activates PBS2 through the stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2 activation leads to changes in glycerol production that helps to balance the intracellular and external osmotic pressures. Activates also HOG1 in response to heat stress and mediates resistance to oxidative stress. Involved in the regulation of the mating pathway. May be a receptor that feeds into the pseudohyphal growth pathway.20 Publications

    GO - Molecular functioni

    1. MAP-kinase scaffold activity Source: SGD
    2. osmosensor activity Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to heat Source: SGD
    2. establishment of cell polarity Source: SGD
    3. osmosensory signaling pathway Source: SGD
    4. positive regulation of signal transduction Source: GOC
    5. signal transduction involved in filamentous growth Source: SGD

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30282-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    High osmolarity signaling protein SHO1
    Alternative name(s):
    Osmosensor SHO1
    Suppressor of SUA8-1 mutation
    Synthetic high osmolarity-sensitive protein 1
    Gene namesi
    Name:SHO1
    Synonyms:SSU81
    Ordered Locus Names:YER118C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER118c.
    SGDiS000000920. SHO1.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Bud. Bud neck. Cell projection
    Note: Localizes at the tip of the mating projection during conjugation.

    GO - Cellular componenti

    1. cellular bud Source: SGD
    2. cellular bud neck Source: SGD
    3. HICS complex Source: SGD
    4. integral component of membrane Source: UniProtKB-KW
    5. mating projection tip Source: SGD
    6. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi166 – 1661S → E: Diminishes the formation of oligomers, dampens activation of the HOG1 kinase, and impairs growth in high-salt or sorbitol conditions. 1 Publication
    Mutagenesisi309 – 3091Y → A: Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. 1 Publication
    Mutagenesisi317 – 3171D → I or H: Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. 1 Publication
    Mutagenesisi355 – 3551Y → A, F, I or M: Decreases the interaction with PBS2 and leads to decreased HOG pathway response and increased aberrant mating pathway activation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 367367High osmolarity signaling protein SHO1PRO_0000072231Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Modified residuei166 – 1661Phosphoserine1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP40073.

    Expressioni

    Gene expression databases

    GenevestigatoriP40073.

    Interactioni

    Subunit structurei

    Forms homooligomers. Interacts (via the SH3 domain) with PBS2. Interacts with FUS1, STE11, STE50 and RNA polymerase II.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AAD14P428842EBI-18140,EBI-1994
    BCH2P361222EBI-18140,EBI-26374
    FUS1P117107EBI-18140,EBI-7179
    GIP2P400362EBI-18140,EBI-7612
    LAS17Q124465EBI-18140,EBI-10022
    LCL3P531532EBI-18140,EBI-23857
    PBS2P080185EBI-18140,EBI-12972
    PCF11P390812EBI-18140,EBI-12980
    RGA1P390832EBI-18140,EBI-15044
    STE11P235613EBI-18140,EBI-18259
    STE50P253443EBI-18140,EBI-18305
    TUS1Q064123EBI-18140,EBI-37117

    Protein-protein interaction databases

    BioGridi36863. 135 interactions.
    DIPiDIP-2472N.
    IntActiP40073. 76 interactions.
    MINTiMINT-518897.
    STRINGi4932.YER118C.

    Structurei

    Secondary structure

    1
    367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi302 – 3098
    Beta strandi315 – 3173
    Beta strandi328 – 3325
    Beta strandi336 – 3427
    Beta strandi348 – 3525
    Helixi353 – 3553
    Beta strandi356 – 3638

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VKNX-ray2.05A298-367[»]
    ProteinModelPortaliP40073.
    SMRiP40073. Positions 299-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40073.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3232CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini54 – 6512ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini87 – 937CytoplasmicSequence Analysis
    Topological domaini115 – 1228ExtracellularSequence Analysis
    Topological domaini144 – 367224CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei33 – 5321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei66 – 8621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei94 – 11421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei123 – 14321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini300 – 36162SH3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SHO1 family.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG44108.
    HOGENOMiHOG000174182.
    KOiK11246.
    OMAiDAYEISF.
    OrthoDBiEOG7MPRR4.

    Family and domain databases

    InterProiIPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40073-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSISSKIRPT PRKPSRMATD HSFKMKKFYA DPFAISSISL AIVSWVIAIG    50
    GSISSASTNE SFPRFTWWGI VYQFLIICSL MLFYCFDLVD HYRIFITTSI 100
    AVAFVYNTNS ATNLVYADGP KKAAASAGVI LLSIINLIWI LYYGGDNASP 150
    TNRWIDSFSI KGIRPSPLEN SLHRARRRGN RNTTPYQNNV YNDAIRDSGY 200
    ATQFDGYPQQ QPSHTNYVSS TALAGFENTQ PNTSEAVNLH LNTLQQRINS 250
    ASNAKETNDN SNNQTNTNIG NTFDTDFSNG NTETTMGDTL GLYSDIGDDN 300
    FIYKAKALYP YDADDDDAYE ISFEQNEILQ VSDIEGRWWK ARRANGETGI 350
    IPSNYVQLID GPEEMHR 367
    Length:367
    Mass (Da):41,126
    Last modified:February 1, 1995 - v1
    Checksum:iE467A4D50AA3EDB6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15653 Genomic DNA. Translation: AAA61904.1.
    L41926 Genomic DNA. Translation: AAC41664.1.
    U18916 Genomic DNA. Translation: AAC03216.1.
    BK006939 Genomic DNA. Translation: DAA07778.1.
    PIRiS50621.
    RefSeqiNP_011043.1. NM_001179008.1.

    Genome annotation databases

    EnsemblFungiiYER118C; YER118C; YER118C.
    GeneIDi856854.
    KEGGisce:YER118C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15653 Genomic DNA. Translation: AAA61904.1 .
    L41926 Genomic DNA. Translation: AAC41664.1 .
    U18916 Genomic DNA. Translation: AAC03216.1 .
    BK006939 Genomic DNA. Translation: DAA07778.1 .
    PIRi S50621.
    RefSeqi NP_011043.1. NM_001179008.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VKN X-ray 2.05 A 298-367 [» ]
    ProteinModelPortali P40073.
    SMRi P40073. Positions 299-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36863. 135 interactions.
    DIPi DIP-2472N.
    IntActi P40073. 76 interactions.
    MINTi MINT-518897.
    STRINGi 4932.YER118C.

    Proteomic databases

    PaxDbi P40073.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER118C ; YER118C ; YER118C .
    GeneIDi 856854.
    KEGGi sce:YER118C.

    Organism-specific databases

    CYGDi YER118c.
    SGDi S000000920. SHO1.

    Phylogenomic databases

    eggNOGi NOG44108.
    HOGENOMi HOG000174182.
    KOi K11246.
    OMAi DAYEISF.
    OrthoDBi EOG7MPRR4.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30282-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P40073.
    NextBioi 983195.

    Gene expression databases

    Genevestigatori P40073.

    Family and domain databases

    InterProi IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Berroteran R.W., Hampsey M.
      Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor."
      Maeda T., Takekawa M., Saito H.
      Science 269:554-558(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK."
      Posas F., Saito H.
      Science 276:1702-1705(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PBS2.
    6. "The Hog1 MAPK prevents cross talk between the HOG and pheromone response MAPK pathways in Saccharomyces cerevisiae."
      O'Rourke S.M., Herskowitz I.
      Genes Dev. 12:2874-2886(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway."
      Raitt D.C., Posas F., Saito H.
      EMBO J. 19:4623-4631(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PBS2.
    8. "The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion."
      Singh K.K.
      Free Radic. Biol. Med. 29:1043-1050(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Calcofluor antifungal action depends on chitin and a functional high-osmolarity glycerol response (HOG) pathway: evidence for a physiological role of the Saccharomyces cerevisiae HOG pathway under noninducing conditions."
      Garcia-Rodriguez L.J., Duran A., Roncero C.
      J. Bacteriol. 182:2428-2437(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway."
      Van Wuytswinkel O., Reiser V., Siderius M., Kelders M.C., Ammerer G., Ruis H., Mager W.H.
      Mol. Microbiol. 37:382-397(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42."
      Reiser V., Salah S.M., Ammerer G.
      Nat. Cell Biol. 2:620-627(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "Defects in glycosylphosphatidylinositol (GPI) anchor synthesis activate Hog1 kinase and confer copper-resistance in Saccharomyces cerevisisae."
      Toh-e A., Oguchi T.
      Genes Genet. Syst. 76:393-410(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress."
      Winkler A., Arkind C., Mattison C.P., Burkholder A., Knoche K., Ota I.M.
      Eukaryot. Cell 1:163-173(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: SUBCELLULAR LOCATION.
    15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    16. "Optimization of specificity in a cellular protein interaction network by negative selection."
      Zarrinpar A., Park S.H., Lim W.A.
      Nature 426:676-680(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, INTERACTION WITH PBS2.
    17. "Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms."
      Park S.H., Zarrinpar A., Lim W.A.
      Science 299:1061-1064(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous growth pathway in yeast."
      Cullen P.J., Sabbagh W. Jr., Graham E., Irick M.M., van Olden E.K., Neal C., Delrow J., Bardwell L., Sprague G.F. Jr.
      Genes Dev. 18:1695-1708(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MSB2.
    19. "Fus1p interacts with components of the Hog1p mitogen-activated protein kinase and Cdc42p morphogenesis signaling pathways to control cell fusion during yeast mating."
      Nelson B., Parsons A.B., Evangelista M., Schaefer K., Kennedy K., Ritchie S., Petryshen T.L., Boone C.
      Genetics 166:67-77(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FUS1.
    20. "Unique and redundant roles for HOG MAPK pathway components as revealed by whole-genome expression analysis."
      O'Rourke S.M., Herskowitz I.
      Mol. Biol. Cell 15:532-542(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast."
      Marles J.A., Dahesh S., Haynes J., Andrews B.J., Davidson A.R.
      Mol. Cell 14:813-823(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PBS2, DOMAIN, MUTAGENESIS OF TYR-309; ASP-317 AND TYR-355.
    22. "Sho1 and Pbs2 act as coscaffolds linking components in the yeast high osmolarity MAP kinase pathway."
      Zarrinpar A., Bhattacharyya R.P., Nittler M.P., Lim W.A.
      Mol. Cell 14:825-832(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STE11.
    23. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    24. "Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway."
      Tatebayashi K., Yamamoto K., Tanaka K., Tomida T., Maruoka T., Kasukawa E., Saito H.
      EMBO J. 25:3033-3044(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STE11 AND STE50.
    25. "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.
    26. "A systems-biology analysis of feedback inhibition in the Sho1 osmotic-stress-response pathway."
      Hao N., Behar M., Parnell S.C., Torres M.P., Borchers C.H., Elston T.C., Dohlman H.G.
      Curr. Biol. 17:659-667(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-166, MUTAGENESIS OF SER-166, SUBUNIT.
    27. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: FUNCTION.
    29. "The signaling mucins Msb2 and Hkr1 differentially regulate the filamentation mitogen-activated protein kinase pathway and contribute to a multimodal response."
      Pitoniak A., Birkaya B., Dionne H.M., Vadaie N., Cullen P.J.
      Mol. Biol. Cell 20:3101-3114(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "Dynamic signaling in the Hog1 MAPK pathway relies on high basal signal transduction."
      Macia J., Regot S., Peeters T., Conde N., Sole R., Posas F.
      Sci. Signal. 2:RA13-RA13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. "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].
    32. "Structural genomics of yeast SH3 domains."
      Kursula P., Kursula I., Song Y.H., Paraskevopoulos M., Wilmanns M.
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 298-367.

    Entry informationi

    Entry nameiSHO1_YEAST
    AccessioniPrimary (citable) accession number: P40073
    Secondary accession number(s): D3DM24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 127 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 2330 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3