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P32944

- SWE1_YEAST

UniProt

P32944 - SWE1_YEAST

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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

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 serine/threonine kinase activity Source: UniProtKB-KW
  4. 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
Complete GO annotation...

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_259128. Polo-like kinase mediated events.

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
Complete GO annotation...

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. 1 PublicationAdd
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.
InParanoidiP32944.
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

        10         20         30         40         50
MSSLDEDEED FEMLDTENLQ FMGKKMFGKQ AGEDESDDFA IGGSTPTNKL
60 70 80 90 100
KFYPYSNNKL TRSTGTLNLS LSNTALSEAN SKFLGKIEEE EEEEEEGKDE
110 120 130 140 150
ESVDSRIKRW SPFHENESVT TPITKRSAEK TNSPISLKQW NQRWFPKNDA
160 170 180 190 200
RTENTSSSSS YSVAKPNQSA FTSSGLVSKM SMDTSLYPAK LRIPETPVKK
210 220 230 240 250
SPLVEGRDHK HVHLSSSKNA SSSLSVSPLN FVEDNNLQED LLFSDSPSSK
260 270 280 290 300
ALPSIHVPTI DSSPLSEAKY HAHDRHNNQT NILSPTNSLV TNSSPQTLHS
310 320 330 340 350
NKFKKIKRAR NSVILKNREL TNSLQQFKDD LYGTDENFPP PIIISSHHST
360 370 380 390 400
RKNPQPYQFR GRYDNDTDEE ISTPTRRKSI IGATSQTHRE SRPLSLSSAI
410 420 430 440 450
VTNTTSAETH SISSTDSSPL NSKRRLISSN KLSANPDSHL FEKFTNVHSI
460 470 480 490 500
GKGQFSTVYQ VTFAQTNKKY AIKAIKPNKY NSLKRILLEI KILNEVTNQI
510 520 530 540 550
TMDQEGKEYI IDYISSWKFQ NSYYIMTELC ENGNLDGFLQ EQVIAKKKRL
560 570 580 590 600
EDWRIWKIIV ELSLALRFIH DSCHIVHLDL KPANVMITFE GNLKLGDFGM
610 620 630 640 650
ATHLPLEDKS FENEGDREYI APEIISDCTY DYKADIFSLG LMIVEIAANV
660 670 680 690 700
VLPDNGNAWH KLRSGDLSDA GRLSSTDIHS ESLFSDITKV DTNDLFDFER
710 720 730 740 750
DNISGNSNNA GTSTVHNNSN INNPNMNNGN DNNNVNTAAT KNRLILHKSS
760 770 780 790 800
KIPAWVPKFL IDGESLERIV RWMIEPNYER RPTANQILQT EECLYVEMTR
810
NAGAIIQEDD FGPKPKFFI
Length:819
Mass (Da):92,468
Last modified:October 1, 1993 - v1
Checksum:iF49FE73937958A02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P32944.
KOi K03114.
OMAi DFGMATH.
OrthoDBi EOG7380FJ.

Enzyme and pathway databases

BioCyci YEAST:G3O-31620-MONOMER.
Reactomei REACT_259128. Polo-like kinase mediated events.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 138 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