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P06784

- STE7_YEAST

UniProt

P06784 - STE7_YEAST

Protein

Serine/threonine-protein kinase STE7

Gene

STE7

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 155 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it is phosphorylated by the ste11 protein kinase and that it can phosphorylate the FUS3 and or KSS1 kinases.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Phosphorylated at multiple sites in response to pheromone.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei220 – 2201ATPPROSITE-ProRule annotation
    Active sitei331 – 3311Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi197 – 2059ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of MAPK activity involved in conjugation with cellular fusion Source: SGD
    2. invasive growth in response to glucose limitation Source: SGD
    3. MAPK cascade involved in cell wall organization or biogenesis Source: SGD
    4. MAPK cascade involved in conjugation with cellular fusion Source: SGD
    5. protein phosphorylation Source: SGD
    6. pseudohyphal growth Source: SGD
    7. regulation of transposition, RNA-mediated Source: SGD
    8. signal transduction involved in filamentous growth Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Pheromone response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29553-MONOMER.
    BRENDAi2.7.12.2. 984.
    ReactomeiREACT_191508. Signaling by FGFR.
    REACT_207653. Signal transduction by L1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase STE7 (EC:2.7.12.2)
    Gene namesi
    Name:STE7
    Ordered Locus Names:YDL159W
    ORF Names:D1525
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL159w.
    SGDiS000002318. STE7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. mating projection tip Source: SGD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi353 – 3531S → A: No loss of activity. 1 Publication
    Mutagenesisi359 – 3591S → A: Inactivation. 1 Publication
    Mutagenesisi363 – 3631T → A: Inactivation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 515515Serine/threonine-protein kinase STE7PRO_0000086688Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei359 – 3591Phosphoserine1 Publication
    Modified residuei363 – 3631Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP06784.
    PaxDbiP06784.
    PeptideAtlasiP06784.

    Expressioni

    Gene expression databases

    GenevestigatoriP06784.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC14Q006842EBI-18389,EBI-4192
    FUS3P1689215EBI-18389,EBI-7193
    HOG1P324852EBI-18389,EBI-8437
    KSS1P1468114EBI-18389,EBI-9945
    STE5P329178EBI-18389,EBI-18373

    Protein-protein interaction databases

    BioGridi31905. 44 interactions.
    DIPiDIP-9N.
    IntActiP06784. 27 interactions.
    MINTiMINT-411435.
    STRINGi4932.YDL159W.

    Structurei

    3D structure databases

    ProteinModelPortaliP06784.
    SMRiP06784. Positions 190-494.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini191 – 466276Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00690000102311.
    HOGENOMiHOG000234206.
    KOiK11226.
    OMAiEIIILME.
    OrthoDBiEOG7380F1.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    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.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06784-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFQRKTLQRR NLKGLNLNLH PDVGNNGQLQ EKTETHQGQS RIEGHVMSNI    50
    NAIQNNSNLF LRRGIKKKLT LDAFGDDQAI SKPNTVVIQQ PQNEPVLVLS 100
    SLSQSPCVSS SSSLSTPCII DAYSNNFGLS PSSTNSTPST IQGLSNIATP 150
    VENEHSISLP PLEESLSPAA ADLKDTLSGT SNGNYIQLQD LVQLGKIGAG 200
    NSGTVVKALH VPDSKIVAKK TIPVEQNNST IINQLVRELS IVKNVKPHEN 250
    IITFYGAYYN QHINNEIIIL MEYSDCGSLD KILSVYKRFV QRGTVSSKKT 300
    WFNELTISKI AYGVLNGLDH LYRQYKIIHR DIKPSNVLIN SKGQIKLCDF 350
    GVSKKLINSI ADTFVGTSTY MSPERIQGNV YSIKGDVWSL GLMIIELVTG 400
    EFPLGGHNDT PDGILDLLQR IVNEPSPRLP KDRIYSKEMT DFVNRCCIKN 450
    ERERSSIHEL LHHDLIMKYV SPSKDDKFRH WCRKIKSKIK EDKRIKREAL 500
    DRAKLEKKQS ERSTH 515
    Length:515
    Mass (Da):57,709
    Last modified:January 1, 1988 - v1
    Checksum:iC8A75899CFBE8BDE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14097 Genomic DNA. Translation: AAA35118.1.
    Z67750 Genomic DNA. Translation: CAA91587.1.
    Z74207 Genomic DNA. Translation: CAA98732.1.
    X97751 Genomic DNA. Translation: CAA66332.1.
    BK006938 Genomic DNA. Translation: DAA11702.1.
    PIRiA25048.
    RefSeqiNP_010122.1. NM_001180219.1.

    Genome annotation databases

    EnsemblFungiiYDL159W; YDL159W; YDL159W.
    GeneIDi851396.
    KEGGisce:YDL159W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14097 Genomic DNA. Translation: AAA35118.1 .
    Z67750 Genomic DNA. Translation: CAA91587.1 .
    Z74207 Genomic DNA. Translation: CAA98732.1 .
    X97751 Genomic DNA. Translation: CAA66332.1 .
    BK006938 Genomic DNA. Translation: DAA11702.1 .
    PIRi A25048.
    RefSeqi NP_010122.1. NM_001180219.1.

    3D structure databases

    ProteinModelPortali P06784.
    SMRi P06784. Positions 190-494.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31905. 44 interactions.
    DIPi DIP-9N.
    IntActi P06784. 27 interactions.
    MINTi MINT-411435.
    STRINGi 4932.YDL159W.

    Proteomic databases

    MaxQBi P06784.
    PaxDbi P06784.
    PeptideAtlasi P06784.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL159W ; YDL159W ; YDL159W .
    GeneIDi 851396.
    KEGGi sce:YDL159W.

    Organism-specific databases

    CYGDi YDL159w.
    SGDi S000002318. STE7.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00690000102311.
    HOGENOMi HOG000234206.
    KOi K11226.
    OMAi EIIILME.
    OrthoDBi EOG7380F1.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29553-MONOMER.
    BRENDAi 2.7.12.2. 984.
    Reactomei REACT_191508. Signaling by FGFR.
    REACT_207653. Signal transduction by L1.

    Miscellaneous databases

    NextBioi 968558.
    PROi P06784.

    Gene expression databases

    Genevestigatori P06784.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    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 PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the yeast regulatory gene STE7 predicts a protein homologous to protein kinases."
      Teague M.A., Chaleff D.T., Errede B.
      Proc. Natl. Acad. Sci. U.S.A. 83:7371-7375(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Analysis of a 23 kb region on the left arm of yeast chromosome IV."
      Delaveau T.T.D., Blugeon C., Jacq C., Perea J.
      Yeast 12:1587-1592(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-515.
      Strain: ATCC 96604 / S288c / FY1679.
    5. "Order of action of components in the yeast pheromone response pathway revealed with a dominant allele of the STE11 kinase and the multiple phosphorylation of the STE7 kinase."
      Cairns B.R., Ramer S.W., Kornberg K.D.
      Genes Dev. 6:1305-1318(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE FUNCTION.
    6. "Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues."
      Zheng C.-F., Guan K.-L.
      EMBO J. 13:1123-1131(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-359 AND THR-363, MUTAGENESIS.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSTE7_YEAST
    AccessioniPrimary (citable) accession number: P06784
    Secondary accession number(s): D6VRJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 155 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 672 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3