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P16892

- FUS3_YEAST

UniProt

P16892 - FUS3_YEAST

Protein

Mitogen-activated protein kinase FUS3

Gene

FUS3

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 161 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Together with closely related KSS1, FUS3 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation after pheromone treatment.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421ATPPROSITE-ProRule annotation
    Active sitei137 – 1371Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. MAP kinase activity Source: SGD
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle arrest Source: SGD
    2. invasive growth in response to glucose limitation Source: SGD
    3. MAPK cascade Source: GOC
    4. mitotic nuclear division Source: UniProtKB-KW
    5. negative regulation of MAPK cascade Source: SGD
    6. negative regulation of transposition, RNA-mediated Source: SGD
    7. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
    8. positive regulation of protein export from nucleus Source: SGD
    9. protein phosphorylation Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Conjugation, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28920-MONOMER.
    BRENDAi2.7.11.24. 984.
    ReactomeiREACT_191508. Signaling by FGFR.
    REACT_205607. Regulation of HSF1-mediated heat shock response.
    REACT_207653. Signal transduction by L1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase FUS3 (EC:2.7.11.24)
    Short name:
    MAP kinase FUS3
    Gene namesi
    Name:FUS3
    Synonyms:DAC2
    Ordered Locus Names:YBL016W
    ORF Names:YBL03.21, YBL0303
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL016w.
    SGDiS000000112. FUS3.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Periplasm 1 Publication
    Note: FUS3 shuttles rapidly between the cytoplasm and the nucleus independent of pheromone treatment or FUS3 phosphorylation level. Activated FUS3 translocates rapidly to the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. mating projection tip Source: SGD
    3. nucleus Source: SGD
    4. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 353353Mitogen-activated protein kinase FUS3PRO_0000186326Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei180 – 1801Phosphothreonine1 Publication
    Modified residuei182 – 1821Phosphotyrosine1 Publication

    Post-translational modificationi

    Dually phosphorylated on Thr-180 and Tyr-182 by STE7 in response to pheromone induction, which activates the enzyme. Activated FUS3 initiates a feedback signal, down-regulating phosphorylation of both, FUS3 and KSS1.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP16892.
    PaxDbiP16892.
    PeptideAtlasiP16892.

    Expressioni

    Gene expression databases

    GenevestigatoriP16892.

    Interactioni

    Subunit structurei

    In the nucleus, FUS3 forms a complex with DIG1, DIG2 and STE12. The interaction of FUS3 with STE12 depends on the presence of both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone treatment. During its activation and phosphorylation, FUS3 forms a membrane-associated complex with the scaffold protein STE5, the MAPKK STE7, the MAPKKK STE11, and the G-protein beta subunit GBB/STE4; interacting directly with STE7 and STE5.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-7193,EBI-7193
    BCK2P333062EBI-7193,EBI-3480
    Kpol_1061p54A7TJH82EBI-7193,EBI-8783719From a different organism.
    STE11P235616EBI-7193,EBI-18259
    STE5P3291710EBI-7193,EBI-18373
    STE7P0678415EBI-7193,EBI-18389
    TIM12P328302EBI-7193,EBI-11303

    Protein-protein interaction databases

    BioGridi32682. 293 interactions.
    DIPiDIP-714N.
    IntActiP16892. 29 interactions.
    MINTiMINT-376832.
    STRINGi4932.YBL016W.

    Structurei

    Secondary structure

    1
    353
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Beta strandi13 – 219
    Beta strandi23 – 3210
    Turni33 – 353
    Beta strandi38 – 447
    Helixi50 – 6516
    Beta strandi74 – 774
    Turni83 – 853
    Beta strandi89 – 935
    Beta strandi97 – 993
    Helixi100 – 1067
    Helixi111 – 13020
    Helixi140 – 1423
    Beta strandi143 – 1453
    Beta strandi151 – 1533
    Helixi156 – 1583
    Beta strandi182 – 1843
    Helixi186 – 1883
    Helixi191 – 1955
    Helixi202 – 21817
    Helixi228 – 23912
    Turni245 – 2506
    Helixi254 – 2618
    Helixi271 – 2744
    Helixi280 – 28910
    Helixi294 – 2963
    Helixi300 – 3045
    Helixi307 – 3093
    Turni310 – 3123
    Helixi326 – 3327
    Helixi340 – 35112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B9FX-ray1.80A1-353[»]
    2B9HX-ray1.55A1-353[»]
    2B9IX-ray2.50A1-353[»]
    2B9JX-ray2.30A1-353[»]
    2F49X-ray1.90A/B1-353[»]
    2F9GX-ray2.10A1-353[»]
    2FA2X-ray2.85A/B1-353[»]
    ProteinModelPortaliP16892.
    SMRiP16892. Positions 1-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16892.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 309297Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi180 – 1823TXY

    Domaini

    The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074298.
    HOGENOMiHOG000233024.
    KOiK04371.
    OMAiNDEPEGE.
    OrthoDBiEOG7K3TWD.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16892-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKRIVYNIS SDFQLKSLLG EGAYGVVCSA THKPTGEIVA IKKIEPFDKP    50
    LFALRTLREI KILKHFKHEN IITIFNIQRP DSFENFNEVY IIQELMQTDL 100
    HRVISTQMLS DDHIQYFIYQ TLRAVKVLHG SNVIHRDLKP SNLLINSNCD 150
    LKVCDFGLAR IIDESAADNS EPTGQQSGMT EYVATRWYRA PEVMLTSAKY 200
    SRAMDVWSCG CILAELFLRR PIFPGRDYRH QLLLIFGIIG TPHSDNDLRC 250
    IESPRAREYI KSLPMYPAAP LEKMFPRVNP KGIDLLQRML VFDPAKRITA 300
    KEALEHPYLQ TYHDPNDEPE GEPIPPSFFE FDHYKEALTT KDLKKLIWNE 350
    IFS 353
    Length:353
    Mass (Da):40,772
    Last modified:October 1, 1993 - v2
    Checksum:i5117980D20A1E7E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti334 – 3341Y → H in AAA34613. (PubMed:2406028)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31132 Genomic DNA. Translation: AAA34613.1.
    X69572 Genomic DNA. Translation: CAA49292.1.
    X68577 Genomic DNA. Translation: CAA48569.1.
    Z35777 Genomic DNA. Translation: CAA84835.1.
    AY693096 Genomic DNA. Translation: AAT93115.1.
    BK006936 Genomic DNA. Translation: DAA07104.1.
    PIRiS28548.
    RefSeqiNP_009537.1. NM_001178256.1.

    Genome annotation databases

    EnsemblFungiiYBL016W; YBL016W; YBL016W.
    GeneIDi852265.
    KEGGisce:YBL016W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31132 Genomic DNA. Translation: AAA34613.1 .
    X69572 Genomic DNA. Translation: CAA49292.1 .
    X68577 Genomic DNA. Translation: CAA48569.1 .
    Z35777 Genomic DNA. Translation: CAA84835.1 .
    AY693096 Genomic DNA. Translation: AAT93115.1 .
    BK006936 Genomic DNA. Translation: DAA07104.1 .
    PIRi S28548.
    RefSeqi NP_009537.1. NM_001178256.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B9F X-ray 1.80 A 1-353 [» ]
    2B9H X-ray 1.55 A 1-353 [» ]
    2B9I X-ray 2.50 A 1-353 [» ]
    2B9J X-ray 2.30 A 1-353 [» ]
    2F49 X-ray 1.90 A/B 1-353 [» ]
    2F9G X-ray 2.10 A 1-353 [» ]
    2FA2 X-ray 2.85 A/B 1-353 [» ]
    ProteinModelPortali P16892.
    SMRi P16892. Positions 1-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32682. 293 interactions.
    DIPi DIP-714N.
    IntActi P16892. 29 interactions.
    MINTi MINT-376832.
    STRINGi 4932.YBL016W.

    Proteomic databases

    MaxQBi P16892.
    PaxDbi P16892.
    PeptideAtlasi P16892.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL016W ; YBL016W ; YBL016W .
    GeneIDi 852265.
    KEGGi sce:YBL016W.

    Organism-specific databases

    CYGDi YBL016w.
    SGDi S000000112. FUS3.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074298.
    HOGENOMi HOG000233024.
    KOi K04371.
    OMAi NDEPEGE.
    OrthoDBi EOG7K3TWD.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28920-MONOMER.
    BRENDAi 2.7.11.24. 984.
    Reactomei REACT_191508. Signaling by FGFR.
    REACT_205607. Regulation of HSF1-mediated heat shock response.
    REACT_207653. Signal transduction by L1.

    Miscellaneous databases

    EvolutionaryTracei P16892.
    NextBioi 970865.
    PROi P16892.

    Gene expression databases

    Genevestigatori P16892.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "FUS3 encodes a cdc2+/CDC28-related kinase required for the transition from mitosis into conjugation."
      Elion E.A., Grisafi P.L., Fink G.R.
      Cell 60:649-664(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The DAC2/FUS3 protein kinase is not essential for transcriptional activation of the mating pheromone response pathway in Saccharomyces cerevisiae."
      Fujimura H.A.
      Mol. Gen. Genet. 235:450-452(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "An 11.4 kb DNA segment on the left arm of yeast chromosome II carries the carboxypeptidase Y sorting gene PEP1, as well as ACH1, FUS3 and a putative ARS."
      van Dyck L., Purnelle B., Skala J., Goffeau A.
      Yeast 8:769-776(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "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.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. "Signal transduction in Saccharomyces cerevisiae requires tyrosine and threonine phosphorylation of FUS3 and KSS1."
      Gartner A., Nasmyth K., Ammerer G.
      Genes Dev. 6:1280-1292(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-180 AND TYR-182.
    8. "MAP kinases with distinct inhibitory functions impart signaling specificity during yeast differentiation."
      Madhani H.D., Styles C.A., Fink G.R.
      Cell 91:673-684(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REGULATION OF STE12 ACTIVITY.
    9. "Regulation of the mating pheromone and invasive growth responses in yeast by two MAP kinase substrates."
      Tedford K., Kim S., Sa D., Stevens K., Tyers M.
      Curr. Biol. 7:228-238(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPLEX WITH DIG1; DIG2 AND STE12.
    10. "Specificity of MAP kinase signaling in yeast differentiation involves transient versus sustained MAPK activation."
      Sabbagh W. Jr., Flatauer L.J., Bardwell A.J., Bardwell L.
      Mol. Cell 8:683-691(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REGULATION OF KSS1 ACTIVITY.
    11. "MAP kinase dynamics in response to pheromones in budding yeast."
      van Drogen F., Stucke V.M., Jorritsma G., Peter M.
      Nat. Cell Biol. 3:1051-1059(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Program-specific distribution of a transcription factor dependent on partner transcription factor and MAPK signaling."
      Zeitlinger J., Simon I., Harbison C.T., Hannett N.M., Volkert T.L., Fink G.R., Young R.A.
      Cell 113:395-404(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REGULATION OF STE12 PROMOTER SELECTIVITY.
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    15. "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].
    16. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFUS3_YEAST
    AccessioniPrimary (citable) accession number: P16892
    Secondary accession number(s): D6VPY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 161 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 8480 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