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P32917

- STE5_YEAST

UniProt

P32917 - STE5_YEAST

Protein

Protein STE5

Gene

STE5

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 138 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    Component of the pheromone signal transduction pathway. It mediates pheromone signals acting between STE20 and STE11. It is absolutely required for pheromone-induced transcription of FUS1. May play a role in cell-cycle arrest in response to pheromone.

    GO - Molecular functioni

    1. MAP-kinase scaffold activity Source: SGD
    2. phosphatidylinositol-4,5-bisphosphate binding Source: SGD
    3. protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. invasive growth in response to glucose limitation Source: SGD
    2. negative regulation of MAPK cascade Source: SGD
    3. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
    4. positive regulation of protein phosphorylation Source: SGD
    5. positive regulation of signal transduction Source: GOC
    6. regulation of transposition, RNA-mediated Source: SGD

    Keywords - Biological processi

    Pheromone response

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29705-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein STE5
    Gene namesi
    Name:STE5
    Synonyms:NUL3
    Ordered Locus Names:YDR103W
    ORF Names:YD8557.12
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR103w.
    SGDiS000002510. STE5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. mating projection tip Source: SGD
    3. nucleus Source: SGD
    4. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 917917Protein STE5PRO_0000072266Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei329 – 3291Phosphoserine1 Publication

    Post-translational modificationi

    May be regulated at the phosphorylation level, and by the mating type of the cell and depends on an intact pheromone-response pathway.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32917.
    PaxDbiP32917.

    Expressioni

    Gene expression databases

    GenevestigatoriP32917.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAGL0J04290gQ6FPF22EBI-18373,EBI-8783845From a different organism.
    CEK1Q5A1D32EBI-18373,EBI-8783371From a different organism.
    CEK2Q5A2812EBI-18373,EBI-8785242From a different organism.
    FUS1P117102EBI-18373,EBI-7179
    FUS3P1689210EBI-18373,EBI-7193
    KLLA0E10539gQ6CNR32EBI-18373,EBI-8785667From a different organism.
    mpkBC8V7D12EBI-18373,EBI-8783425From a different organism.
    STE11P235617EBI-18373,EBI-18259
    STE4P188512EBI-18373,EBI-7390
    STE7P067848EBI-18373,EBI-18389

    Protein-protein interaction databases

    BioGridi32160. 48 interactions.
    DIPiDIP-858N.
    IntActiP32917. 20 interactions.
    MINTiMINT-1174440.
    STRINGi4932.YDR103W.

    Structurei

    Secondary structure

    1
    917
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi45 – 484
    Helixi49 – 513
    Turni52 – 543
    Helixi55 – 584
    Helixi59 – 635
    Turni64 – 663
    Helixi593 – 60412
    Beta strandi608 – 6169
    Helixi618 – 6203
    Beta strandi622 – 6243
    Helixi625 – 64016
    Beta strandi645 – 6506
    Beta strandi653 – 6608
    Helixi661 – 6644
    Helixi668 – 6725
    Helixi673 – 6764
    Helixi685 – 6928
    Beta strandi701 – 7077
    Turni713 – 7153
    Helixi717 – 7193
    Helixi723 – 7253
    Beta strandi735 – 7417
    Turni748 – 7503
    Beta strandi755 – 7584
    Helixi760 – 77011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KGNNMR-A44-67[»]
    2L4UNMR-A44-67[»]
    3FZEX-ray1.60A593-786[»]
    4F2HX-ray3.19A583-787[»]
    ProteinModelPortaliP32917.
    SMRiP32917. Positions 170-233, 584-774.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32917.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi775 – 876102Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    To yeast FAR1.Curated

    Phylogenomic databases

    eggNOGiNOG44001.
    HOGENOMiHOG000065959.
    KOiK11239.
    OMAiTLCDEPI.
    OrthoDBiEOG7712HK.

    Family and domain databases

    InterProiIPR021651. Scaffold_Ste5_Fus5-binding.
    IPR021106. Ste5_Fus3-bd.
    IPR001841. Znf_RING.
    [Graphical view]
    PfamiPF11610. Ste5. 1 hit.
    PF12194. Ste5_C. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32917-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMETPTDNIV SPFHNFGSST QYSGTLSRTP NQIIELEKPS TLSPLSRGKK    50
    WTEKLARFQR SSAKKKRFSP SPISSSTFSF SPKSRVTSSN SSGNEDGNLM 100
    NTPSTVSTDY LPQHPHRTSS LPRPNSNLFH ASNSNLSRAN EPPRAENLSD 150
    NIPPKVAPFG YPIQRTSIKK SFLNASCTLC DEPISNRRKG EKIIELACGH 200
    LSHQECLIIS FGTTSKADVR ALFPFCTKCK KDTNKAVQCI PENDELKDIL 250
    ISDFLIHKIP DSELSITPQS RFPPYSPLLP PFGLSYTPVE RQTIYSQAPS 300
    LNPNLILAAP PKERNQIPQK KSNYTFLHSP LGHRRIPSGA NSILADTSVA 350
    LSANDSISAV SNSVRAKDDE TKTTLPLLRS YFIQILLNNF QEELQDWRID 400
    GDYGLLRLVD KLMISKDGQR YIQCWCFLFE DAFVIAEVDN DVDVLEIRLK 450
    NLEVFTPIAN LRMTTLEASV LKCTLNKQHC ADLSDLYIVQ NINSDESTTV 500
    QKWISGILNQ DFVFNEDNIT STLPILPIIK NFSKDVGNGR HETSTFLGLI 550
    NPNKVVEVGN VHDNDTVIIR RGFTLNSGEC SRQSTVDSIQ SVLTTISSIL 600
    SLKREKPDNL AIILQIDFTK LKEEDSLIVV YNSLKALTIK FARLQFCFVD 650
    RNNYVLDYGS VLHKIDSLDS ISNLKSKSSS TQFSPIWLKN TLYPENIHEH 700
    LGIVAVSNSN MEAKKSILFQ DYRCFTSFGR RRPNELKIKV GYLNVDYSDK 750
    IDELVEASSW TFVLETLCYS FGLSFDEHDD DDEEDNDDST DNELDNSSGS 800
    LSDAESTTTI HIDSPFDNEN ATANMVNDRN LLTEGEHSNI ENLETVASSV 850
    QPALIPNIRF SLHSEEEGTN ENENENDMPV LLLSDMDKGI DGITRRSSFS 900
    SLIESGNNNC PLHMDYI 917
    Length:917
    Mass (Da):102,727
    Last modified:February 1, 1994 - v2
    Checksum:i0435BDA0196B2D6F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti331 – 3322LG → W in AAA35108. (PubMed:8516289)Curated
    Sequence conflicti341 – 3433NSI → TLS in AAA35108. (PubMed:8516289)Curated
    Sequence conflicti821 – 8211A → R in BAA02301. (PubMed:8455598)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12917 Genomic DNA. Translation: BAA02301.1.
    L01620 Genomic DNA. Translation: AAA35108.1.
    L23856 Genomic DNA. Translation: AAA35115.1.
    L07865 Unassigned DNA. Translation: AAA16896.1.
    Z47746 Genomic DNA. Translation: CAA87679.1.
    BK006938 Genomic DNA. Translation: DAA11949.1.
    PIRiS51254.
    RefSeqiNP_010388.1. NM_001180411.1.

    Genome annotation databases

    EnsemblFungiiYDR103W; YDR103W; YDR103W.
    GeneIDi851680.
    KEGGisce:YDR103W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12917 Genomic DNA. Translation: BAA02301.1 .
    L01620 Genomic DNA. Translation: AAA35108.1 .
    L23856 Genomic DNA. Translation: AAA35115.1 .
    L07865 Unassigned DNA. Translation: AAA16896.1 .
    Z47746 Genomic DNA. Translation: CAA87679.1 .
    BK006938 Genomic DNA. Translation: DAA11949.1 .
    PIRi S51254.
    RefSeqi NP_010388.1. NM_001180411.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KGN NMR - A 44-67 [» ]
    2L4U NMR - A 44-67 [» ]
    3FZE X-ray 1.60 A 593-786 [» ]
    4F2H X-ray 3.19 A 583-787 [» ]
    ProteinModelPortali P32917.
    SMRi P32917. Positions 170-233, 584-774.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32160. 48 interactions.
    DIPi DIP-858N.
    IntActi P32917. 20 interactions.
    MINTi MINT-1174440.
    STRINGi 4932.YDR103W.

    Proteomic databases

    MaxQBi P32917.
    PaxDbi P32917.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR103W ; YDR103W ; YDR103W .
    GeneIDi 851680.
    KEGGi sce:YDR103W.

    Organism-specific databases

    CYGDi YDR103w.
    SGDi S000002510. STE5.

    Phylogenomic databases

    eggNOGi NOG44001.
    HOGENOMi HOG000065959.
    KOi K11239.
    OMAi TLCDEPI.
    OrthoDBi EOG7712HK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29705-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32917.
    NextBioi 969315.

    Gene expression databases

    Genevestigatori P32917.

    Family and domain databases

    InterProi IPR021651. Scaffold_Ste5_Fus5-binding.
    IPR021106. Ste5_Fus3-bd.
    IPR001841. Znf_RING.
    [Graphical view ]
    Pfami PF11610. Ste5. 1 hit.
    PF12194. Ste5_C. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Function of the ste signal transduction pathway for mating pheromones sustains MAT alpha 1 transcription in Saccharomyces cerevisiae."
      Mukai Y., Harashima S., Oshima Y.
      Mol. Cell. Biol. 13:2050-2060(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning of the STE5 gene of Saccharomyces cerevisiae as a suppressor of the mating defect of cdc25 temperature-sensitive mutants."
      Perlman R., Yablonski D., Simchen G., Levitzki A.
      Proc. Natl. Acad. Sci. U.S.A. 90:5474-5478(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Sequence and characterization of the STE5 gene required for signal transduction and mating in Saccharomyces cerevisiae."
      Mackay V.L., Mathewes S., Bell L., O'Hara P.J.
      Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    4. "Cloning of Saccharomyces cerevisiae STE5 as a suppressor of a Ste20 protein kinase mutant: structural and functional similarity of Ste5 to Far1."
      Leberer E., Dignard D., Harcus D., Hougan L., Whiteway M., Thomas D.Y.
      Mol. Gen. Genet. 241:241-254(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DBY939.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "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-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "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].
    10. "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].

    Entry informationi

    Entry nameiSTE5_YEAST
    AccessioniPrimary (citable) accession number: P32917
    Secondary accession number(s): D6VS89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1900 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. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3