Mitosis inhibitor protein kinase SWE1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32944 (SWE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Mitosis inhibitor protein kinase SWE1
EC=2.7.11.1

Alternative name(s):
Wee1 homolog

Gene names

Name:	SWE1
Ordered Locus Names:	YJL187C
ORF Names:	J0406

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	819 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	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. Ref.7 Ref.10 Ref.11 Ref.14 Ref.15 Ref.19 Ref.26
Subcellular location	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. Ref.12 Ref.15 Ref.17 Ref.25
Induction	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). Ref.4 Ref.5 Ref.6 Ref.8 Ref.23
Post-translational modification	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. Ref.1 Ref.6 Ref.22 Ref.24 Ref.26 Ref.28 Ref.31
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis Mitosis
Cellular component	Nucleus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Inferred from mutant phenotype Ref.1. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW cell shape checkpoint Inferred from direct assay Ref.5. Source: SGD meiosis Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of spindle pole body separation Inferred from mutant phenotype PubMed 8887667. Source: SGD re-entry into mitotic cell cycle Inferred from genetic interaction PubMed 15107621. Source: SGD regulation of cell size Inferred from mutant phenotype PubMed 12089449. Source: SGD regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: SGD regulation of meiosis Inferred from genetic interaction Ref.8. Source: SGD
Cellular_component	cellular bud neck Inferred from direct assay Ref.12 Ref.25. Source: SGD nucleus Inferred from direct assay Ref.12 Ref.25. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CDC14	Q00684	3	EBI-18607,EBI-4192
CDC5	P32562	4	EBI-18607,EBI-4440
KIN1	P13185	3	EBI-18607,EBI-9716

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 819

819

Mitosis inhibitor protein kinase SWE1

PRO_0000086727

Regions

Domain

444 – 794

351

Protein kinase

Nucleotide binding

450 – 458

ATP By similarity

Compositional bias

88 – 96

Poly-Glu

Sites

Active site

579

Proton acceptor By similarity

Metal binding

584

Magnesium; via carbonyl oxygen By similarity

Metal binding

597

Magnesium; via carbonyl oxygen By similarity

Binding site

473

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine; by CDC5 Ref.24 Ref.26

Modified residue

Phosphothreonine; by CDC28 Ref.26

Modified residue

Phosphoserine; by CDC28 Ref.26

Modified residue

Phosphoserine; by CDC28 Ref.26

Modified residue

Phosphoserine Ref.26

Modified residue

Phosphothreonine; by CDC28 Ref.26

Modified residue

102

Phosphoserine; by CDC5 Ref.24

Modified residue

105

Phosphoserine; by CDC28 Ref.26

Modified residue

111

Phosphoserine; by CDC5, CDC28 and CLA4 Ref.24 Ref.26

Modified residue

118

Phosphoserine; by CDC5 Ref.24 Ref.26

Modified residue

121

Phosphothreonine; by CDC28 Ref.26

Modified residue

124

Phosphothreonine; by CDC28 Ref.26

Modified residue

127

Phosphoserine; by CDC28 Ref.26

Modified residue

131

Phosphothreonine; by CDC5 Ref.24

Modified residue

133

Phosphoserine; by CDC28 Ref.26 Ref.33

Modified residue

136

Phosphoserine; by CDC28 and CLA4 Ref.24 Ref.26

Modified residue

156

Phosphoserine; by CDC5 Ref.24

Modified residue

169

Phosphoserine; by CDC5 Ref.24

Modified residue

196

Phosphothreonine; by CDC28 Ref.26

Modified residue

201

Phosphoserine; by CDC28 Ref.26

Modified residue

225

Phosphoserine; by CDC5 Ref.24

Modified residue

254

Phosphoserine; by CDC5 Ref.24

Modified residue

262

Phosphoserine Ref.26 Ref.32

Modified residue

263

Phosphoserine; by CDC28 Ref.26

Modified residue

266

Phosphoserine; by CDC28 Ref.26

Modified residue

280

Phosphothreonine; by CDC5 Ref.24

Modified residue

284

Phosphoserine Ref.26

Modified residue

294

Phosphoserine Ref.26

Modified residue

312

Phosphoserine; by CLA4 Ref.24

Modified residue

345

Phosphoserine Ref.26

Modified residue

367

Phosphothreonine; by CDC28 Ref.26

Modified residue

373

Phosphothreonine; by CDC28 Ref.26

Modified residue

379

Phosphoserine; by CDC5 and CLA4 Ref.24 Ref.26

Modified residue

384

Phosphothreonine; by CDC28 Ref.26

Modified residue

395

Phosphoserine; by CDC5 and CLA4 Ref.24

Modified residue

438

Phosphoserine; by CDC5 and CLA4 Ref.24

Modified residue

610

Phosphoserine; by CDC5 Ref.24 Ref.26

Modified residue

629

Phosphothreonine; by CDC5 Ref.24

Modified residue

688

Phosphothreonine; by CDC5 and CLA4 Ref.24

Modified residue

692

Phosphothreonine Ref.26

Experimental info

Mutagenesis

318 – 328

Missing: Impairs interaction with HSL7 and prevents bud neck localization and degradation. Ref.17

Mutagenesis

320

L → P or Q: Prevents degradation. Ref.17

Mutagenesis

324

L → S: Prevents degradation. Ref.17

Mutagenesis

327

F → S: Prevents degradation. Ref.17

Mutagenesis

328

K → E: Prevents degradation. Ref.17

Mutagenesis

331

L → I: Prevents degradation. Ref.17

Mutagenesis

332

Y → C: Prevents degradation. Ref.17

Mutagenesis

473

K → A or P: Loss of catalytic activity. Ref.9

Mutagenesis

797

E → K, V or G: Prevents degradation. Ref.17

Mutagenesis

806

I → T, A or N: Prevents degradation. Ref.17

Mutagenesis

807

Q → R or E: Prevents degradation. Ref.17

Sequences

Sequence

Length

Mass (Da)

Tools

P32944 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: F49FE73937958A02
Show »

FASTA

819

92,468

        10         20         30         40         50         60 
MSSLDEDEED FEMLDTENLQ FMGKKMFGKQ AGEDESDDFA IGGSTPTNKL KFYPYSNNKL 

        70         80         90        100        110        120 
TRSTGTLNLS LSNTALSEAN SKFLGKIEEE EEEEEEGKDE ESVDSRIKRW SPFHENESVT 

       130        140        150        160        170        180 
TPITKRSAEK TNSPISLKQW NQRWFPKNDA RTENTSSSSS YSVAKPNQSA FTSSGLVSKM 

       190        200        210        220        230        240 
SMDTSLYPAK LRIPETPVKK SPLVEGRDHK HVHLSSSKNA SSSLSVSPLN FVEDNNLQED 

       250        260        270        280        290        300 
LLFSDSPSSK ALPSIHVPTI DSSPLSEAKY HAHDRHNNQT NILSPTNSLV TNSSPQTLHS 

       310        320        330        340        350        360 
NKFKKIKRAR NSVILKNREL TNSLQQFKDD LYGTDENFPP PIIISSHHST RKNPQPYQFR 

       370        380        390        400        410        420 
GRYDNDTDEE ISTPTRRKSI IGATSQTHRE SRPLSLSSAI VTNTTSAETH SISSTDSSPL 

       430        440        450        460        470        480 
NSKRRLISSN KLSANPDSHL FEKFTNVHSI GKGQFSTVYQ VTFAQTNKKY AIKAIKPNKY 

       490        500        510        520        530        540 
NSLKRILLEI KILNEVTNQI TMDQEGKEYI IDYISSWKFQ NSYYIMTELC ENGNLDGFLQ 

       550        560        570        580        590        600 
EQVIAKKKRL EDWRIWKIIV ELSLALRFIH DSCHIVHLDL KPANVMITFE GNLKLGDFGM 

       610        620        630        640        650        660 
ATHLPLEDKS FENEGDREYI APEIISDCTY DYKADIFSLG LMIVEIAANV VLPDNGNAWH 

       670        680        690        700        710        720 
KLRSGDLSDA GRLSSTDIHS ESLFSDITKV DTNDLFDFER DNISGNSNNA GTSTVHNNSN 

       730        740        750        760        770        780 
INNPNMNNGN DNNNVNTAAT KNRLILHKSS KIPAWVPKFL IDGESLERIV RWMIEPNYER 

       790        800        810 
RPTANQILQT EECLYVEMTR NAGAIIQEDD FGPKPKFFI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Cdc5 interacts with the Wee1 kinase in budding yeast." Bartholomew C.R., Woo S.H., Chung Y.S., Jones C., Hardy C.F. Mol. Cell. Biol. 21:4949-4959(2001) [PubMed] [Europe PMC] [Abstract] 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]	"Targets of the cyclin-dependent kinase Cdk1." Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K., Shokat K.M., Morgan D.O. Nature 425:859-864(2003) [PubMed] [Europe PMC] [Abstract] 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]	"Coupling morphogenesis to mitotic entry." Sakchaisri K., Asano S., Yu L.-R., Shulewitz M.J., Park C.J., Park J.-E., Cho Y.-W., Veenstra T.D., Thorner J., Lee K.S. Proc. Natl. Acad. Sci. U.S.A. 101:4124-4129(2004) [PubMed] [Europe PMC] [Abstract] 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]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, MASS SPECTROMETRY.
[33]	"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-133, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X73966 Genomic DNA. Translation: CAA52150.1. Z49462 Genomic DNA. Translation: CAA89482.1. BK006943 Genomic DNA. Translation: DAA08619.1.
PIR	S40400.
RefSeq	NP_012348.1. NM_001181620.1.
3D structure databases
ProteinModelPortal	P32944.
SMR	P32944. Positions 403-714.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2410N.
IntAct	P32944. 34 interactions.
MINT	MINT-532694.
STRING	4932.YJL187C.
Proteomic databases
PaxDb	P32944.
PeptideAtlas	P32944.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL187C; YJL187C; YJL187C.
GeneID	853252.
KEGG	sce:YJL187C.
Organism-specific databases
CYGD	YJL187c.
SGD	S000003723. SWE1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00530000063230.
HOGENOM	HOG000057137.
KO	K03114.
OMA	DFGMATH.
OrthoDB	EOG486CN1.
Gene expression databases
Genevestigator	P32944.
GermOnline	YJL187C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	973496.

Entry information

Entry name

SWE1_YEAST

Accession

Primary (citable) accession number: P32944
Secondary accession number(s): D6VW03

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents