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P08018

- PBS2_YEAST

UniProt

P08018 - PBS2_YEAST

Protein

MAP kinase kinase PBS2

Gene

PBS2

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 151 (01 Oct 2014)
      Sequence version 4 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Seems to phosphorylate HOG1 on a tyrosine residue.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei389 – 3891ATPPROSITE-ProRule annotation
    Active sitei485 – 4851Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi366 – 3749ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase kinase activity Source: SGD
    3. MAP-kinase scaffold activity Source: SGD
    4. peptide alpha-N-acetyltransferase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein serine/threonine kinase activity Source: UniProtKB-KW
    7. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. actin filament organization Source: SGD
    2. activation of MAPK activity involved in osmosensory signaling pathway Source: SGD
    3. cellular response to heat Source: SGD
    4. hyperosmotic response Source: SGD
    5. MAPK import into nucleus involved in osmosensory signaling pathway Source: SGD
    6. N-terminal peptidyl-methionine acetylation Source: UniProtKB
    7. osmosensory signaling pathway Source: UniProtKB
    8. protein phosphorylation Source: UniProtKB
    9. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31578-MONOMER.
    BRENDAi2.7.12.2. 984.
    ReactomeiREACT_188484. Oxidative Stress Induced Senescence.
    REACT_189013. NOD1/2 Signaling Pathway.
    REACT_96987. activated TAK1 mediates p38 MAPK activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MAP kinase kinase PBS2 (EC:2.7.12.2)
    Alternative name(s):
    Polymyxin B resistance protein 2
    Suppressor of fluoride sensitivity 4
    Gene namesi
    Name:PBS2
    Synonyms:HOG4, SFS4, SSK4
    Ordered Locus Names:YJL128C
    ORF Names:J0699
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL128c.
    SGDiS000003664. PBS2.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cellular bud neck Source: SGD
    2. cellular bud tip Source: SGD
    3. cytoplasm Source: SGD
    4. NatB complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi96 – 961P → S in PBS2-13; loss of SH3-domain interaction. 1 Publication
    Mutagenesisi389 – 3891K → M: Loss of activity. 1 Publication
    Mutagenesisi514 – 5141S → A: Loss of phosphorylation. 1 Publication
    Mutagenesisi518 – 5181T → A: Loss of phosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 668668MAP kinase kinase PBS2PRO_0000086483Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681Phosphoserine1 Publication
    Modified residuei269 – 2691Phosphoserine1 Publication
    Modified residuei514 – 5141Phosphoserine2 Publications
    Modified residuei518 – 5181Phosphothreonine1 Publication

    Post-translational modificationi

    Activated by phosphorylation by SSK2 or SSK22. Ser/Thr phosphorylation is also necessary for SHO1-mediated activation.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP08018.
    PaxDbiP08018.
    PeptideAtlasiP08018.

    Expressioni

    Gene expression databases

    GenevestigatoriP08018.

    Interactioni

    Subunit structurei

    Interacts with NBP2, PTC1, SHO1 AND STE11.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NBP2Q121632EBI-12972,EBI-34713
    SHO1P400735EBI-12972,EBI-18140

    Protein-protein interaction databases

    BioGridi33628. 287 interactions.
    DIPiDIP-2368N.
    IntActiP08018. 21 interactions.
    MINTiMINT-546167.
    STRINGi4932.YJL128C.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VKNX-ray2.05C92-103[»]
    ProteinModelPortaliP08018.
    SMRiP08018. Positions 271-623.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08018.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini360 – 623264Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi91 – 10111Pro-richAdd
    BLAST

    Domaini

    Alternative way of activation involves binding the proline-rich motif to the SH3 domain of SHO1.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00690000101918.
    HOGENOMiHOG000234206.
    KOiK11227.
    OMAiTNILCSA.
    OrthoDBiEOG7380F1.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    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.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08018-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDKFANLSL HEKTGKSSIQ LNEQTGSDNG SAVKRTSSTS SHYNNINADL    50
    HARVKAFQEQ RALKRSASVG SNQSEQDKGS SQSPKHIQQI VNKPLPPLPV 100
    AGSSKVSQRM SSQVVQASSK STLKNVLDNQ ETQNITDVNI NIDTTKITAT 150
    TIGVNTGLPA TDITPSVSNT ASATHKAQLL NPNRRAPRRP LSTQHPTRPN 200
    VAPHKAPAII NTPKQSLSAR RGLKLPPGGM SLKMPTKTAQ QPQQFAPSPS 250
    NKKHIETLSN SKVVEGKRSN PGSLINGVQS TSTSSSTEGP HDTVGTTPRT 300
    GNSNNSSNSG SSGGGGLFAN FSKYVDIKSG SLNFAGKLSL SSKGIDFSNG 350
    SSSRITLDEL EFLDELGHGN YGNVSKVLHK PTNVIMATKE VRLELDEAKF 400
    RQILMELEVL HKCNSPYIVD FYGAFFIEGA VYMCMEYMDG GSLDKIYDES 450
    SEIGGIDEPQ LAFIANAVIH GLKELKEQHN IIHRDVKPTN ILCSANQGTV 500
    KLCDFGVSGN LVASLAKTNI GCQSYMAPER IKSLNPDRAT YTVQSDIWSL 550
    GLSILEMALG RYPYPPETYD NIFSQLSAIV DGPPPRLPSD KFSSDAQDFV 600
    SLCLQKIPER RPTYAALTEH PWLVKYRNQD VHMSEYITER LERRNKILRE 650
    RGENGLSKNV PALHMGGL 668
    Length:668
    Mass (Da):72,720
    Last modified:September 21, 2011 - v4
    Checksum:i9BC3435BDAFE8019
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti222 – 2232GL → AV(PubMed:8948101)Curated
    Sequence conflicti222 – 2232GL → AV in CAA89423. (PubMed:8641269)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02946 Unassigned DNA. Translation: AAA16819.1.
    U12237 Genomic DNA. Translation: AAA20392.1.
    Z49403 Genomic DNA. Translation: CAA89423.1.
    BK006943 Genomic DNA. Translation: DAA08673.2.
    PIRiS56909.
    RefSeqiNP_012407.2. NM_001181561.2.

    Genome annotation databases

    EnsemblFungiiYJL128C; YJL128C; YJL128C.
    GeneIDi853313.
    KEGGisce:YJL128C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02946 Unassigned DNA. Translation: AAA16819.1 .
    U12237 Genomic DNA. Translation: AAA20392.1 .
    Z49403 Genomic DNA. Translation: CAA89423.1 .
    BK006943 Genomic DNA. Translation: DAA08673.2 .
    PIRi S56909.
    RefSeqi NP_012407.2. NM_001181561.2.

    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 C 92-103 [» ]
    ProteinModelPortali P08018.
    SMRi P08018. Positions 271-623.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33628. 287 interactions.
    DIPi DIP-2368N.
    IntActi P08018. 21 interactions.
    MINTi MINT-546167.
    STRINGi 4932.YJL128C.

    Proteomic databases

    MaxQBi P08018.
    PaxDbi P08018.
    PeptideAtlasi P08018.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL128C ; YJL128C ; YJL128C .
    GeneIDi 853313.
    KEGGi sce:YJL128C.

    Organism-specific databases

    CYGDi YJL128c.
    SGDi S000003664. PBS2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00690000101918.
    HOGENOMi HOG000234206.
    KOi K11227.
    OMAi TNILCSA.
    OrthoDBi EOG7380F1.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31578-MONOMER.
    BRENDAi 2.7.12.2. 984.
    Reactomei REACT_188484. Oxidative Stress Induced Senescence.
    REACT_189013. NOD1/2 Signaling Pathway.
    REACT_96987. activated TAK1 mediates p38 MAPK activation.

    Miscellaneous databases

    EvolutionaryTracei P08018.
    NextBioi 973654.
    PROi P08018.

    Gene expression databases

    Genevestigatori P08018.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    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 PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of a gene conferring polymyxin B resistance on yeast: similarity of the predicted polypeptide to protein kinases."
      Boguslawski G., Polazzi J.O.
      Proc. Natl. Acad. Sci. U.S.A. 84:5848-5852(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "PBS2, a yeast gene encoding a putative protein kinase, interacts with the RAS2 pathway and affects osmotic sensitivity of Saccharomyces cerevisiae."
      Boguslawski G.
      J. Gen. Microbiol. 138:2425-2432(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 222-223 AND 668.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19 open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14, RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta elements and a Ty4 transposon."
      Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.
      Yeast 12:1471-1474(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    5. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 222-223.
      Strain: ATCC 204508 / S288c.
    7. "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 OF 91-101, DOMAIN, PHOSPHORYLATION AT SER-514 AND THR-518, MUTAGENESIS OF PRO-96; LYS-389; SER-514 AND THR-518.
    8. "An osmosensing signal transduction pathway in yeast."
      Brewster J.L., de Valoir T., Dwyer N.D., Winter E., Gustin M.C.
      Science 259:1760-1763(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "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, INTERACTION WITH SHO1.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "Nbp2 targets the Ptc1-type 2C Ser/Thr phosphatase to the HOG MAPK pathway."
      Mapes J., Ota I.M.
      EMBO J. 23:302-311(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NBP2 AND PTC1.
    13. "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 SHO1.
    14. "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: INTERACTION WITH SHO1 AND STE11.
    15. "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.
    16. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPBS2_YEAST
    AccessioniPrimary (citable) accession number: P08018
    Secondary accession number(s): D6VW57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 151 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2160 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 X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3