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P14681

- KSS1_YEAST

UniProt

P14681 - KSS1_YEAST

Protein

Mitogen-activated protein kinase KSS1

Gene

KSS1

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 163 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Together with closely related FUS3, KSS1 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 KSS1 activates both pathways, whereas activated FUS3 activates the mating but suppresses the filamentation pathway. KSS1 activity is down-regulated by FUS3 during pheromone induction to prevent inappropriate activation of the filamentation pathway. During induction of filamentation, KSS1 activates the transcription factor STE12 resulting in its binding to and activation of filamentation specific genes. Non-activated KSS1 has a kinase-independent repressive effect on STE12 transcriptional activity, that is mediated by direct binding to STE12 and depends on the presence of DIG1 and DIG2, and that is required for the suppression of filamentation under normal growth conditions. SSN3/SRB10 contributes further to the suppression of filamentation under these conditions by reducing STE12 stability independent of KSS1. FUS3 can partially compensate for the lack of KSS1 but filamentation becomes constitutively induced at a low level in the absence of any signal. KSS1 phosphorylates STE7, STE5, FAR1, DIG1, DIG2, STE12, and SST2.8 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by tyrosine and threonine phosphorylation after pheromone treatment or carbon/nitrogen limitation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421ATPPROSITE-ProRule annotation
    Active sitei143 – 1431Proton 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. MAP kinase activity Source: SGD
    3. protein binding Source: IntAct
    4. transcription factor binding Source: SGD

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. invasive growth in response to glucose limitation Source: SGD
    3. MAPK cascade Source: GOC
    4. negative regulation of sequence-specific DNA binding transcription factor activity Source: SGD
    5. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
    6. protein phosphorylation Source: SGD
    7. signal transduction involved in filamentous growth Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30760-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 KSS1 (EC:2.7.11.24)
    Short name:
    MAP kinase KSS1
    Alternative name(s):
    Kinase suppressor of SST2
    Gene namesi
    Name:KSS1
    Ordered Locus Names:YGR040W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR040w.
    SGDiS000003272. KSS1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Periplasm 1 Publication
    Note: KSS1 shuttles rapidly between the cytoplasm and the nucleus independent of its activation state.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: SGD
    3. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 368368Mitogen-activated protein kinase KSS1PRO_0000186333Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831Phosphothreonine2 Publications
    Modified residuei185 – 1851Phosphotyrosine2 Publications

    Post-translational modificationi

    Dually phosphorylated on Thr-183 and Tyr-185 by STE7 in response to pheromone or carbon/nitrogen limitation, which activates the enzyme. Activated FUS3 down-regulates KSS1 phosphorylation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP14681.
    PaxDbiP14681.
    PeptideAtlasiP14681.

    Expressioni

    Gene expression databases

    GenevestigatoriP14681.

    Interactioni

    Subunit structurei

    In the nucleus, KSS1 forms a complex with DIG1, DIG2 and STE12; in contrast to FUS3 the interaction of KSS1 with STE12 does not depend on DIG1 and DIG2. Phosphorylated KSS1 shows reduced interaction with STE12. During pheromone activation and phosphorylation, KSS1 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 POF1, STE7 and STE5 proteins.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCK2P333064EBI-9945,EBI-3480
    DIG1Q030633EBI-9945,EBI-29752
    DIG2Q033733EBI-9945,EBI-34019
    STE11P235614EBI-9945,EBI-18259
    STE12P135746EBI-9945,EBI-18264
    STE7P0678414EBI-9945,EBI-18389

    Protein-protein interaction databases

    BioGridi33287. 176 interactions.
    DIPiDIP-60N.
    IntActiP14681. 18 interactions.
    MINTiMINT-411417.
    STRINGi4932.YGR040W.

    Structurei

    3D structure databases

    ProteinModelPortaliP14681.
    SMRiP14681. Positions 1-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 313301Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi183 – 1853TXY

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi345 – 3495Poly-Glu

    Domaini

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

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074298.
    HOGENOMiHOG000233024.
    KOiK04371.
    OMAiGPRYTDL.
    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.

    P14681-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTITFDIP SQYKLVDLIG EGAYGTVCSA IHKPSGIKVA IKKIQPFSKK    50
    LFVTRTIREI KLLRYFHEHE NIISILDKVR PVSIDKLNAV YLVEELMETD 100
    LQKVINNQNS GFSTLSDDHV QYFTYQILRA LKSIHSAQVI HRDIKPSNLL 150
    LNSNCDLKVC DFGLARCLAS SSDSRETLVG FMTEYVATRW YRAPEIMLTF 200
    QEYTTAMDIW SCGCILAEMV SGKPLFPGRD YHHQLWLILE VLGTPSFEDF 250
    NQIKSKRAKE YIANLPMRPP LPWETVWSKT DLNPDMIDLL DKMLQFNPDK 300
    RISAAEALRH PYLAMYHDPS DEPEYPPLNL DDEFWKLDNK IMRPEEEEEV 350
    PIEMLKDMLY DELMKTME 368
    Length:368
    Mass (Da):42,692
    Last modified:April 1, 1990 - v1
    Checksum:i5FA42161B5FD51B5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26398 Genomic DNA. Translation: AAA34882.1.
    DQ115391 Genomic DNA. Translation: AAZ22456.1.
    Z72825 Genomic DNA. Translation: CAA97038.1.
    AY557773 Genomic DNA. Translation: AAS56099.1.
    BK006941 Genomic DNA. Translation: DAA08139.1.
    PIRiA33297.
    RefSeqiNP_011554.3. NM_001181169.3.

    Genome annotation databases

    EnsemblFungiiYGR040W; YGR040W; YGR040W.
    GeneIDi852931.
    KEGGisce:YGR040W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26398 Genomic DNA. Translation: AAA34882.1 .
    DQ115391 Genomic DNA. Translation: AAZ22456.1 .
    Z72825 Genomic DNA. Translation: CAA97038.1 .
    AY557773 Genomic DNA. Translation: AAS56099.1 .
    BK006941 Genomic DNA. Translation: DAA08139.1 .
    PIRi A33297.
    RefSeqi NP_011554.3. NM_001181169.3.

    3D structure databases

    ProteinModelPortali P14681.
    SMRi P14681. Positions 1-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33287. 176 interactions.
    DIPi DIP-60N.
    IntActi P14681. 18 interactions.
    MINTi MINT-411417.
    STRINGi 4932.YGR040W.

    Proteomic databases

    MaxQBi P14681.
    PaxDbi P14681.
    PeptideAtlasi P14681.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR040W ; YGR040W ; YGR040W .
    GeneIDi 852931.
    KEGGi sce:YGR040W.

    Organism-specific databases

    CYGDi YGR040w.
    SGDi S000003272. KSS1.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30760-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

    NextBioi 972657.
    PROi P14681.

    Gene expression databases

    Genevestigatori P14681.

    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. "A putative protein kinase overcomes pheromone-induced arrest of cell cycling in S. cerevisiae."
      Courchesne W.E., Kunisawa R., Thorner J.
      Cell 58:1107-1119(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
      Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
      Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [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.
    8. "Two novel targets of the MAP kinase Kss1 are negative regulators of invasive growth in the yeast Saccharomyces cerevisiae."
      Cook J.G., Bardwell L., Kron S.J., Thorner J.
      Genes Dev. 10:2831-2848(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPLEX WITH DIG1; DIG2 AND STE12.
    9. "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, INHIBITION OF FILAMENTATION.
    10. "Repression of yeast Ste12 transcription factor by direct binding of unphosphorylated Kss1 MAPK and its regulation by the Ste7 MEK."
      Bardwell L., Cook J.G., Voora D., Baggott D.M., Martinez A.R., Thorner J.
      Genes Dev. 12:2887-2898(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STE12.
    11. "Differential regulation of transcription: repression by unactivated mitogen-activated protein kinase Kss1 requires the Dig1 and Dig2 proteins."
      Bardwell L., Cook J.G., Zhu-Shimoni J.X., Voora D., Thorner J.
      Proc. Natl. Acad. Sci. U.S.A. 95:15400-15405(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, FUNCTIONAL DEPENDENCE ON DIG1/DIG2.
    12. "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 ACTIVITY BY FUS3.
    13. "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.
    14. "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.
    15. "Srb10/Cdk8 regulates yeast filamentous growth by phosphorylating the transcription factor Ste12."
      Nelson C., Goto S., Lund K., Hung W., Sadowski I.
      Nature 421:187-190(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, STE12 STABILITY.
    16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    17. "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 THR-183 AND TYR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    18. "Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes."
      Fasolo J., Sboner A., Sun M.G., Yu H., Chen R., Sharon D., Kim P.M., Gerstein M., Snyder M.
      Genes Dev. 25:767-778(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH POF1.

    Entry informationi

    Entry nameiKSS1_YEAST
    AccessioniPrimary (citable) accession number: P14681
    Secondary accession number(s): D6VUH8, Q45U43
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 163 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 5480 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3