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P32944

- SWE1_YEAST

UniProt

P32944 - SWE1_YEAST

Protein

Mitosis inhibitor protein kinase SWE1

Gene

SWE1

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 136 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylating and inhibiting the mitosis-promoting cyclin B-bound CDC28 at 'Tyr-19'. SWE1-mediated inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to delay mitosis in response to defects in growth, actin organization or bud formation. Inhibits the activity of B-type cyclins in replication initiation strongly for CLB2, moderately for CLB3 and CLB4, and there is no apparent inhibition for CLB5 and CLB6, correlating with the normal expression timing of those cyclins. Hyperphosphorylation and degradation of SWE1 when all checkpoint requirement are met releases CLB2-CDC28 from inhibition and allows for progression through the cell cycle. SWE1-dependent CDC28 phosphorylation is also required for pachytene arrest upon activation of the recombination checkpoint during meiosis. Also involved in the regulation of nitrogen starvation- and short chain alcohol-induced filamentous growth, or filamentous differentiation in response to slowed DNA synthesis. Can act both on serines and on tyrosines.18 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei473 – 4731ATPPROSITE-ProRule annotation
    Active sitei579 – 5791Proton acceptorPROSITE-ProRule annotation
    Metal bindingi584 – 5841Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi597 – 5971Magnesium; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi450 – 4589ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cytokinesis after mitosis checkpoint Source: SGD
    2. G2/M transition of mitotic cell cycle Source: SGD
    3. meiotic nuclear division Source: UniProtKB-KW
    4. mitotic nuclear division Source: UniProtKB-KW
    5. negative regulation of spindle pole body separation Source: SGD
    6. peptidyl-tyrosine phosphorylation Source: GOC
    7. re-entry into mitotic cell cycle Source: SGD
    8. regulation of cyclin-dependent protein serine/threonine kinase activity Source: SGD
    9. regulation of meiosis Source: SGD

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Cell cycle, Cell division, Meiosis, Mitosis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31620-MONOMER.
    ReactomeiREACT_188487. Cyclin A/B1 associated events during G2/M transition.
    REACT_188488. G2/M DNA replication checkpoint.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitosis inhibitor protein kinase SWE1 (EC:2.7.11.1)
    Alternative name(s):
    Wee1 homolog
    Gene namesi
    Name:SWE1
    Ordered Locus Names:YJL187C
    ORF Names:J0406
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL187c.
    SGDiS000003723. SWE1.

    Subcellular locationi

    Bud neck. Nucleus
    Note: When SWE1 first accumulates in G1, it is localized to the nucleus. After bud emergence, a subpopulation is recruited to the daughter side of the mother-bud neck through HSL1 and its adapter HSL7, where it is susceptible to hyperphosphorylation and degradation.

    GO - Cellular componenti

    1. cellular bud neck Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi318 – 32811Missing: Impairs interaction with HSL7 and prevents bud neck localization and degradation. Add
    BLAST
    Mutagenesisi320 – 3201L → P or Q: Prevents degradation. 1 Publication
    Mutagenesisi324 – 3241L → S: Prevents degradation. 1 Publication
    Mutagenesisi327 – 3271F → S: Prevents degradation. 1 Publication
    Mutagenesisi328 – 3281K → E: Prevents degradation. 1 Publication
    Mutagenesisi331 – 3311L → I: Prevents degradation. 1 Publication
    Mutagenesisi332 – 3321Y → C: Prevents degradation. 1 Publication
    Mutagenesisi473 – 4731K → A or P: Loss of catalytic activity. 1 Publication
    Mutagenesisi797 – 7971E → K, V or G: Prevents degradation. 1 Publication
    Mutagenesisi806 – 8061I → T, A or N: Prevents degradation. 1 Publication
    Mutagenesisi807 – 8071Q → R or E: Prevents degradation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 819819Mitosis inhibitor protein kinase SWE1PRO_0000086727Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361Phosphoserine; by CDC52 Publications
    Modified residuei45 – 451Phosphothreonine; by CDC281 Publication
    Modified residuei56 – 561Phosphoserine; by CDC281 Publication
    Modified residuei63 – 631Phosphoserine; by CDC281 Publication
    Modified residuei70 – 701Phosphoserine1 Publication
    Modified residuei74 – 741Phosphothreonine; by CDC281 Publication
    Modified residuei102 – 1021Phosphoserine; by CDC51 Publication
    Modified residuei105 – 1051Phosphoserine; by CDC281 Publication
    Modified residuei111 – 1111Phosphoserine; by CDC5, CDC28 and CLA42 Publications
    Modified residuei118 – 1181Phosphoserine; by CDC52 Publications
    Modified residuei121 – 1211Phosphothreonine; by CDC281 Publication
    Modified residuei124 – 1241Phosphothreonine; by CDC281 Publication
    Modified residuei127 – 1271Phosphoserine; by CDC281 Publication
    Modified residuei131 – 1311Phosphothreonine; by CDC51 Publication
    Modified residuei133 – 1331Phosphoserine; by CDC281 Publication
    Modified residuei136 – 1361Phosphoserine; by CDC28 and CLA42 Publications
    Modified residuei156 – 1561Phosphoserine; by CDC51 Publication
    Modified residuei169 – 1691Phosphoserine; by CDC51 Publication
    Modified residuei196 – 1961Phosphothreonine; by CDC281 Publication
    Modified residuei201 – 2011Phosphoserine; by CDC281 Publication
    Modified residuei225 – 2251Phosphoserine; by CDC51 Publication
    Modified residuei254 – 2541Phosphoserine; by CDC51 Publication
    Modified residuei262 – 2621Phosphoserine1 Publication
    Modified residuei263 – 2631Phosphoserine; by CDC281 Publication
    Modified residuei266 – 2661Phosphoserine; by CDC281 Publication
    Modified residuei280 – 2801Phosphothreonine; by CDC51 Publication
    Modified residuei284 – 2841Phosphoserine1 Publication
    Modified residuei294 – 2941Phosphoserine1 Publication
    Modified residuei312 – 3121Phosphoserine; by CLA41 Publication
    Modified residuei345 – 3451Phosphoserine1 Publication
    Modified residuei367 – 3671Phosphothreonine; by CDC281 Publication
    Modified residuei373 – 3731Phosphothreonine; by CDC281 Publication
    Modified residuei379 – 3791Phosphoserine; by CDC5 and CLA43 Publications
    Modified residuei384 – 3841Phosphothreonine; by CDC281 Publication
    Modified residuei395 – 3951Phosphoserine; by CDC5 and CLA41 Publication
    Modified residuei438 – 4381Phosphoserine; by CDC5 and CLA41 Publication
    Modified residuei610 – 6101Phosphoserine; by CDC52 Publications
    Modified residuei629 – 6291Phosphothreonine; by CDC51 Publication
    Modified residuei688 – 6881Phosphothreonine; by CDC5 and CLA41 Publication
    Modified residuei692 – 6921Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated progressively by CLA4, CLB2-CDC28 and CDC5. CLA4-dependent phosphorylation occurs in late S phase, followed by phosphorylation by CLB2-CDC28 in early G2, when the levels of mitotic CLB2 increases. This phosphorylation is critical for triggering subsequent SWE1-CDC5 interaction and CDC5-dependent phosphorylation. The resulting cumulative hyperphosphorylation down-regulates SWE1 by targeting it for ubiquitin-mediated degradation. This stepwise phosphorylation is thought to be a mechanism to integrate the different checkpoint requirements before entry into mitosis.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32944.
    PaxDbiP32944.
    PeptideAtlasiP32944.

    Expressioni

    Inductioni

    Expressed periodically during the cell cycle, with a peak in late G1. Transcriptional repression requires ZDS1. Protein accumulation is also periodic, peaking during S/G2 and declining prior to and during nuclear division of the unperturbed cell cycle. Stabilized during a checkpoint response in G2. Induced during meiosis. Induced by ethanol (at protein level).5 Publications

    Gene expression databases

    GenevestigatoriP32944.

    Interactioni

    Subunit structurei

    Interacts with CLB2-CDC28. Partial hyperphosphorylation of SWE1 by CLB2-CDC28 stabilizes the ternary complex of SWE1 and CLB2-CDC28 and stimulates kinase activity of SWE1 in a positive feedback loop, maintaining CLB2-CDC28 in the tyrosine-phosphorylated state. Fully hyperphosphorylated SWE1 dissociates from CLB2-CDC28. Interacts with HSL7, KCC4 and MET30.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC14Q006843EBI-18607,EBI-4192
    CDC5P325624EBI-18607,EBI-4440
    KIN1P131853EBI-18607,EBI-9716

    Protein-protein interaction databases

    BioGridi33575. 295 interactions.
    DIPiDIP-2410N.
    IntActiP32944. 31 interactions.
    MINTiMINT-532694.
    STRINGi4932.YJL187C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32944.
    SMRiP32944. Positions 403-714.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini444 – 794351Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi88 – 969Poly-Glu

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000063230.
    HOGENOMiHOG000057137.
    KOiK03114.
    OMAiDFGMATH.
    OrthoDBiEOG7380FJ.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32944-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSLDEDEED FEMLDTENLQ FMGKKMFGKQ AGEDESDDFA IGGSTPTNKL    50
    KFYPYSNNKL TRSTGTLNLS LSNTALSEAN SKFLGKIEEE EEEEEEGKDE 100
    ESVDSRIKRW SPFHENESVT TPITKRSAEK TNSPISLKQW NQRWFPKNDA 150
    RTENTSSSSS YSVAKPNQSA FTSSGLVSKM SMDTSLYPAK LRIPETPVKK 200
    SPLVEGRDHK HVHLSSSKNA SSSLSVSPLN FVEDNNLQED LLFSDSPSSK 250
    ALPSIHVPTI DSSPLSEAKY HAHDRHNNQT NILSPTNSLV TNSSPQTLHS 300
    NKFKKIKRAR NSVILKNREL TNSLQQFKDD LYGTDENFPP PIIISSHHST 350
    RKNPQPYQFR GRYDNDTDEE ISTPTRRKSI IGATSQTHRE SRPLSLSSAI 400
    VTNTTSAETH SISSTDSSPL NSKRRLISSN KLSANPDSHL FEKFTNVHSI 450
    GKGQFSTVYQ VTFAQTNKKY AIKAIKPNKY NSLKRILLEI KILNEVTNQI 500
    TMDQEGKEYI IDYISSWKFQ NSYYIMTELC ENGNLDGFLQ EQVIAKKKRL 550
    EDWRIWKIIV ELSLALRFIH DSCHIVHLDL KPANVMITFE GNLKLGDFGM 600
    ATHLPLEDKS FENEGDREYI APEIISDCTY DYKADIFSLG LMIVEIAANV 650
    VLPDNGNAWH KLRSGDLSDA GRLSSTDIHS ESLFSDITKV DTNDLFDFER 700
    DNISGNSNNA GTSTVHNNSN INNPNMNNGN DNNNVNTAAT KNRLILHKSS 750
    KIPAWVPKFL IDGESLERIV RWMIEPNYER RPTANQILQT EECLYVEMTR 800
    NAGAIIQEDD FGPKPKFFI 819
    Length:819
    Mass (Da):92,468
    Last modified:October 1, 1993 - v1
    Checksum:iF49FE73937958A02
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73966 Genomic DNA. Translation: CAA52150.1.
    Z49462 Genomic DNA. Translation: CAA89482.1.
    BK006943 Genomic DNA. Translation: DAA08619.1.
    PIRiS40400.
    RefSeqiNP_012348.1. NM_001181620.1.

    Genome annotation databases

    EnsemblFungiiYJL187C; YJL187C; YJL187C.
    GeneIDi853252.
    KEGGisce:YJL187C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73966 Genomic DNA. Translation: CAA52150.1 .
    Z49462 Genomic DNA. Translation: CAA89482.1 .
    BK006943 Genomic DNA. Translation: DAA08619.1 .
    PIRi S40400.
    RefSeqi NP_012348.1. NM_001181620.1.

    3D structure databases

    ProteinModelPortali P32944.
    SMRi P32944. Positions 403-714.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33575. 295 interactions.
    DIPi DIP-2410N.
    IntActi P32944. 31 interactions.
    MINTi MINT-532694.
    STRINGi 4932.YJL187C.

    Proteomic databases

    MaxQBi P32944.
    PaxDbi P32944.
    PeptideAtlasi P32944.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL187C ; YJL187C ; YJL187C .
    GeneIDi 853252.
    KEGGi sce:YJL187C.

    Organism-specific databases

    CYGDi YJL187c.
    SGDi S000003723. SWE1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000063230.
    HOGENOMi HOG000057137.
    KOi K03114.
    OMAi DFGMATH.
    OrthoDBi EOG7380FJ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31620-MONOMER.
    Reactomei REACT_188487. Cyclin A/B1 associated events during G2/M transition.
    REACT_188488. G2/M DNA replication checkpoint.

    Miscellaneous databases

    NextBioi 973496.
    PROi P32944.

    Gene expression databases

    Genevestigatori P32944.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    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. "Properties of Saccharomyces cerevisiae wee1 and its differential regulation of p34CDC28 in response to G1 and G2 cyclins."
      Booher R.N., Deshaies R.J., Kirschner M.W.
      EMBO J. 12:3417-3426(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION OF CDC28.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "A search for proteins that interact genetically with histone H3 and H4 amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces cerevisiae."
      Ma X.-J., Lu Q., Grunstein M.
      Genes Dev. 10:1327-1340(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    5. "Cdc28 tyrosine phosphorylation and the morphogenesis checkpoint in budding yeast."
      Sia R.A.L., Herald H.A., Lew D.J.
      Mol. Biol. Cell 7:1657-1666(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    6. "Control of Swe1p degradation by the morphogenesis checkpoint."
      Sia R.A.L., Bardes E.S.G., Lew D.J.
      EMBO J. 17:6678-6688(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INDUCTION.
    7. "Cdc34 and the F-box protein Met30 are required for degradation of the Cdk-inhibitory kinase Swe1."
      Kaiser P., Sia R.A.L., Bardes E.S.G., Lew D.J., Reed S.I.
      Genes Dev. 12:2587-2597(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MET30, DEGRADATION.
    8. "The pachytene checkpoint in S. cerevisiae depends on Swe1-mediated phosphorylation of the cyclin-dependent kinase Cdc28."
      Leu J.-Y., Roeder G.S.
      Mol. Cell 4:805-814(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEIOSIS, INDUCTION.
    9. "Phosphorylation-independent inhibition of Cdc28p by the tyrosine kinase Swe1p in the morphogenesis checkpoint."
      McMillan J.N., Sia R.A.L., Bardes E.S.G., Lew D.J.
      Mol. Cell. Biol. 19:5981-5990(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-473.
    10. "The morphogenesis checkpoint in Saccharomyces cerevisiae: cell cycle control of Swe1p degradation by Hsl1p and Hsl7p."
      McMillan J.N., Longtine M.S., Sia R.A.L., Theesfeld C.L., Bardes E.S.G., Pringle J.R., Lew D.J.
      Mol. Cell. Biol. 19:6929-6939(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSL7.
    11. "Hsl7 localizes to a septin ring and serves as an adapter in a regulatory pathway that relieves tyrosine phosphorylation of Cdc28 protein kinase in Saccharomyces cerevisiae."
      Shulewitz M.J., Inouye C.J., Thorner J.
      Mol. Cell. Biol. 19:7123-7137(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSL7.
    12. "Septin-dependent assembly of a cell cycle-regulatory module in Saccharomyces cerevisiae."
      Longtine M.S., Theesfeld C.L., McMillan J.N., Weaver E., Pringle J.R., Lew D.J.
      Mol. Cell. Biol. 20:4049-4061(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "A role for the Swe1 checkpoint kinase during filamentous growth of Saccharomyces cerevisiae."
      La Valle R., Wittenberg C.
      Genetics 158:549-562(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Dynamic localization of the Swe1 regulator Hsl7 during the Saccharomyces cerevisiae cell cycle."
      Cid V.J., Shulewitz M.J., McDonald K.L., Thorner J.
      Mol. Biol. Cell 12:1645-1669(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSL7.
    15. Cited for: INTERACTION WITH CDC5, SUBCELLULAR LOCATION.
    16. "A role for the Pkc1p/Mpk1p kinase cascade in the morphogenesis checkpoint."
      Harrison J.C., Bardes E.S.G., Ohya Y., Lew D.J.
      Nat. Cell Biol. 3:417-420(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Determinants of Swe1p degradation in Saccharomyces cerevisiae."
      McMillan J.N., Theesfeld C.L., Harrison J.C., Bardes E.S.G., Lew D.J.
      Mol. Biol. Cell 13:3560-3575(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 318-ARG--LYS-328; LEU-320; LEU-324; PHE-327; LYS-328; LEU-331; TYR-332; GLU-797; ILE-806 AND GLN-807.
    18. "Conservation of mechanisms controlling entry into mitosis: budding yeast wee1 delays entry into mitosis and is required for cell size control."
      Harvey S.L., Kellogg D.R.
      Curr. Biol. 13:264-275(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "The Saccharomyces cerevisiae bud-neck proteins Kcc4 and Gin4 have distinct but partially-overlapping cellular functions."
      Okuzaki D., Watanabe T., Tanaka S., Nojima H.
      Genes Genet. Syst. 78:113-126(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCC4.
    20. "In yeast, the pseudohyphal phenotype induced by isoamyl alcohol results from the operation of the morphogenesis checkpoint."
      Martinez-Anaya C., Dickinson J.R., Sudbery P.E.
      J. Cell Sci. 116:3423-3431(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Induction of S. cerevisiae filamentous differentiation by slowed DNA synthesis involves Mec1, Rad53 and Swe1 checkpoint proteins."
      Jiang Y.W., Kang C.M.
      Mol. Biol. Cell 14:5116-5124(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FILAMENTOUS GROWTH REGULATION.
    22. Cited for: PHOSPHORYLATION BY CDC28.
    23. "Effect of ethanol on cell growth of budding yeast: genes that are important for cell growth in the presence of ethanol."
      Kubota S., Takeo I., Kume K., Kanai M., Shitamukai A., Mizunuma M., Miyakawa T., Shimoi H., Iefuji H., Hirata D.
      Biosci. Biotechnol. Biochem. 68:968-972(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ETHANOL.
    24. Cited for: PHOSPHORYLATION AT SER-36; SER-102; SER-111; SER-118; THR-131; SER-136; SER-156; SER-169; SER-225; SER-254; THR-280; SER-312; SER-379; SER-395; SER-438; SER-610; THR-629 AND THR-688.
    25. "Localization of proteins that are coordinately expressed with Cln2 during the cell cycle."
      Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.
      Yeast 21:793-800(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    26. "Cdk1-dependent regulation of the mitotic inhibitor Wee1."
      Harvey S.L., Charlet A., Haas W., Gygi S.P., Kellogg D.R.
      Cell 122:407-420(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-36; THR-45; SER-56; SER-63; SER-70; THR-74; SER-105; SER-111; SER-118; THR-121; THR-124; SER-127; SER-133; SER-136; THR-196; SER-201; SER-262; SER-263; SER-266; SER-284; SER-294; SER-345; THR-367; THR-373; SER-379; THR-384; SER-610 AND THR-692, INTERACTION WITH CLB2-CDC28.
    27. "Swe1p responds to cytoskeletal perturbation, not bud size, in S. cerevisiae."
      McNulty J.J., Lew D.J.
      Curr. Biol. 15:2190-2198(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "Concerted mechanism of Swe1/Wee1 regulation by multiple kinases in budding yeast."
      Asano S., Park J.-E., Sakchaisri K., Yu L.-R., Song S., Supavilai P., Veenstra T.D., Lee K.S.
      EMBO J. 24:2194-2204(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY CLB2-CDC28.
    29. "Swe1 regulation and transcriptional control restrict the activity of mitotic cyclins toward replication proteins in Saccharomyces cerevisiae."
      Hu F., Aparicio O.M.
      Proc. Natl. Acad. Sci. U.S.A. 102:8910-8915(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "The function and regulation of budding yeast Swe1 in response to interrupted DNA synthesis."
      Liu H., Wang Y.
      Mol. Biol. Cell 17:2746-2756(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. "Differential susceptibility of yeast S and M phase CDK complexes to inhibitory tyrosine phosphorylation."
      Keaton M.A., Bardes E.S.G., Marquitz A.R., Freel C.D., Zyla T.R., Rudolph J., Lew D.J.
      Curr. Biol. 17:1181-1189(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CLB-CDC28.
    32. "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].
    33. "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-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "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 nameiSWE1_YEAST
    AccessioniPrimary (citable) accession number: P32944
    Secondary accession number(s): D6VW03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

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

    External Data

    Dasty 3