Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitosis inhibitor protein kinase SWE1

Gene

SWE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei473ATPPROSITE-ProRule annotation1
Active sitei579Proton acceptorPROSITE-ProRule annotation1
Metal bindingi584Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi597Magnesium; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi450 – 458ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • G2/M transition of mitotic cell cycle Source: SGD
  • meiotic cell cycle Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • morphogenesis checkpoint Source: SGD
  • negative regulation of spindle pole body separation Source: SGD
  • positive regulation of sphingolipid biosynthetic process Source: SGD
  • protein phosphorylation Source: SGD
  • re-entry into mitotic cell cycle Source: SGD
  • regulation of cyclin-dependent protein serine/threonine kinase activity Source: SGD
  • regulation of meiotic nuclear division 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.
ReactomeiR-SCE-156711. Polo-like kinase mediated events.
R-SCE-69202. Cyclin E associated events during G1/S transition.
R-SCE-69273. Cyclin A/B1 associated events during G2/M transition.
R-SCE-69478. G2/M DNA replication checkpoint.
R-SCE-69656. Cyclin A:Cdk2-associated events at S phase entry.
R-SCE-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

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
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL187C.
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

  • cellular bud neck Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi318 – 328Missing : Impairs interaction with HSL7 and prevents bud neck localization and degradation. 1 PublicationAdd BLAST11
Mutagenesisi320L → P or Q: Prevents degradation. 1 Publication1
Mutagenesisi324L → S: Prevents degradation. 1 Publication1
Mutagenesisi327F → S: Prevents degradation. 1 Publication1
Mutagenesisi328K → E: Prevents degradation. 1 Publication1
Mutagenesisi331L → I: Prevents degradation. 1 Publication1
Mutagenesisi332Y → C: Prevents degradation. 1 Publication1
Mutagenesisi473K → A or P: Loss of catalytic activity. 1 Publication1
Mutagenesisi797E → K, V or G: Prevents degradation. 1 Publication1
Mutagenesisi806I → T, A or N: Prevents degradation. 1 Publication1
Mutagenesisi807Q → R or E: Prevents degradation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000867271 – 819Mitosis inhibitor protein kinase SWE1Add BLAST819

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36Phosphoserine; by CDC52 Publications1
Modified residuei45Phosphothreonine; by CDC281 Publication1
Modified residuei56Phosphoserine; by CDC281 Publication1
Modified residuei63Phosphoserine; by CDC281 Publication1
Modified residuei70Phosphoserine1 Publication1
Modified residuei74Phosphothreonine; by CDC281 Publication1
Modified residuei102Phosphoserine; by CDC51 Publication1
Modified residuei105Phosphoserine; by CDC281 Publication1
Modified residuei111Phosphoserine; by CDC5, CDC28 and CLA42 Publications1
Modified residuei118Phosphoserine; by CDC52 Publications1
Modified residuei121Phosphothreonine; by CDC281 Publication1
Modified residuei124Phosphothreonine; by CDC281 Publication1
Modified residuei127Phosphoserine; by CDC281 Publication1
Modified residuei131Phosphothreonine; by CDC51 Publication1
Modified residuei133Phosphoserine; by CDC281 Publication1
Modified residuei136Phosphoserine; by CDC28 and CLA42 Publications1
Modified residuei156Phosphoserine; by CDC51 Publication1
Modified residuei169Phosphoserine; by CDC51 Publication1
Modified residuei196Phosphothreonine; by CDC281 Publication1
Modified residuei201Phosphoserine; by CDC281 Publication1
Modified residuei225Phosphoserine; by CDC51 Publication1
Modified residuei254Phosphoserine; by CDC51 Publication1
Modified residuei262Phosphoserine1 Publication1
Modified residuei263Phosphoserine; by CDC281 Publication1
Modified residuei266Phosphoserine; by CDC281 Publication1
Modified residuei280Phosphothreonine; by CDC51 Publication1
Modified residuei284Phosphoserine1 Publication1
Modified residuei294Phosphoserine1 Publication1
Modified residuei312Phosphoserine; by CLA41 Publication1
Modified residuei345Phosphoserine1 Publication1
Modified residuei367Phosphothreonine; by CDC281 Publication1
Modified residuei373Phosphothreonine; by CDC281 Publication1
Modified residuei379Phosphoserine; by CDC5 and CLA4Combined sources2 Publications1
Modified residuei384Phosphothreonine; by CDC281 Publication1
Modified residuei395Phosphoserine; by CDC5 and CLA41 Publication1
Modified residuei438Phosphoserine; by CDC5 and CLA41 Publication1
Modified residuei610Phosphoserine; by CDC52 Publications1
Modified residuei629Phosphothreonine; by CDC51 Publication1
Modified residuei688Phosphothreonine; by CDC5 and CLA41 Publication1
Modified residuei692Phosphothreonine1 Publication1
Cross-linki741Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

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.7 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP32944.
PRIDEiP32944.

PTM databases

iPTMnetiP32944.

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

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. 309 interactors.
DIPiDIP-2410N.
IntActiP32944. 31 interactors.
MINTiMINT-532694.

Structurei

3D structure databases

ProteinModelPortaliP32944.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini444 – 794Protein kinasePROSITE-ProRule annotationAdd BLAST351

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi88 – 96Poly-Glu9

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

GeneTreeiENSGT00530000063230.
HOGENOMiHOG000057137.
InParanoidiP32944.
KOiK03114.
OMAiWVPKFLI.
OrthoDBiEOG092C38EF.

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]
SMARTiSM00220. S_TKc. 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.
PIRiS40400.
RefSeqiNP_012348.1. NM_001181620.1.

3D structure databases

ProteinModelPortaliP32944.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33575. 309 interactors.
DIPiDIP-2410N.
IntActiP32944. 31 interactors.
MINTiMINT-532694.

PTM databases

iPTMnetiP32944.

Proteomic databases

MaxQBiP32944.
PRIDEiP32944.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YJL187C.
SGDiS000003723. SWE1.

Phylogenomic databases

GeneTreeiENSGT00530000063230.
HOGENOMiHOG000057137.
InParanoidiP32944.
KOiK03114.
OMAiWVPKFLI.
OrthoDBiEOG092C38EF.

Enzyme and pathway databases

BioCyciYEAST:G3O-31620-MONOMER.
ReactomeiR-SCE-156711. Polo-like kinase mediated events.
R-SCE-69202. Cyclin E associated events during G1/S transition.
R-SCE-69273. Cyclin A/B1 associated events during G2/M transition.
R-SCE-69478. G2/M DNA replication checkpoint.
R-SCE-69656. Cyclin A:Cdk2-associated events at S phase entry.
R-SCE-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Miscellaneous databases

PROiP32944.

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]
SMARTiSM00220. S_TKc. 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]
ProtoNetiSearch...

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 2, 2016
This is version 159 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.