SWE1_YEAST
ID SWE1_YEAST Reviewed; 819 AA.
AC P32944; D6VW03;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Mitosis inhibitor protein kinase SWE1;
DE EC=2.7.11.1;
DE AltName: Full=Wee1 homolog;
GN Name=SWE1; OrderedLocusNames=YJL187C; ORFNames=J0406;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PHOSPHORYLATION OF CDC28.
RX PubMed=8253069; DOI=10.1002/j.1460-2075.1993.tb06016.x;
RA Booher R.N., Deshaies R.J., Kirschner M.W.;
RT "Properties of Saccharomyces cerevisiae wee1 and its differential
RT regulation of p34CDC28 in response to G1 and G2 cyclins.";
RL EMBO J. 12:3417-3426(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INDUCTION.
RX PubMed=8647431; DOI=10.1101/gad.10.11.1327;
RA Ma X.-J., Lu Q., Grunstein M.;
RT "A search for proteins that interact genetically with histone H3 and H4
RT amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 10:1327-1340(1996).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=8930890; DOI=10.1091/mbc.7.11.1657;
RA Sia R.A.L., Herald H.A., Lew D.J.;
RT "Cdc28 tyrosine phosphorylation and the morphogenesis checkpoint in budding
RT yeast.";
RL Mol. Biol. Cell 7:1657-1666(1996).
RN [6]
RP FUNCTION, PHOSPHORYLATION, AND INDUCTION.
RX PubMed=9822611; DOI=10.1093/emboj/17.22.6678;
RA Sia R.A.L., Bardes E.S.G., Lew D.J.;
RT "Control of Swe1p degradation by the morphogenesis checkpoint.";
RL EMBO J. 17:6678-6688(1998).
RN [7]
RP INTERACTION WITH MET30, AND UBIQUITINATION.
RX PubMed=9716410; DOI=10.1101/gad.12.16.2587;
RA Kaiser P., Sia R.A.L., Bardes E.S.G., Lew D.J., Reed S.I.;
RT "Cdc34 and the F-box protein Met30 are required for degradation of the Cdk-
RT inhibitory kinase Swe1.";
RL Genes Dev. 12:2587-2597(1998).
RN [8]
RP FUNCTION IN MEIOSIS, AND INDUCTION.
RX PubMed=10619027; DOI=10.1016/s1097-2765(00)80390-1;
RA Leu J.-Y., Roeder G.S.;
RT "The pachytene checkpoint in S. cerevisiae depends on Swe1-mediated
RT phosphorylation of the cyclin-dependent kinase Cdc28.";
RL Mol. Cell 4:805-814(1999).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF LYS-473.
RX PubMed=10454545; DOI=10.1128/mcb.19.9.5981;
RA McMillan J.N., Sia R.A.L., Bardes E.S.G., Lew D.J.;
RT "Phosphorylation-independent inhibition of Cdc28p by the tyrosine kinase
RT Swe1p in the morphogenesis checkpoint.";
RL Mol. Cell. Biol. 19:5981-5990(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH HSL7.
RX PubMed=10490630; DOI=10.1128/mcb.19.10.6929;
RA McMillan J.N., Longtine M.S., Sia R.A.L., Theesfeld C.L., Bardes E.S.G.,
RA Pringle J.R., Lew D.J.;
RT "The morphogenesis checkpoint in Saccharomyces cerevisiae: cell cycle
RT control of Swe1p degradation by Hsl1p and Hsl7p.";
RL Mol. Cell. Biol. 19:6929-6939(1999).
RN [11]
RP FUNCTION, AND INTERACTION WITH HSL7.
RX PubMed=10490648; DOI=10.1128/mcb.19.10.7123;
RA Shulewitz M.J., Inouye C.J., Thorner J.;
RT "Hsl7 localizes to a septin ring and serves as an adapter in a regulatory
RT pathway that relieves tyrosine phosphorylation of Cdc28 protein kinase in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:7123-7137(1999).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=10805747; DOI=10.1128/mcb.20.11.4049-4061.2000;
RA Longtine M.S., Theesfeld C.L., McMillan J.N., Weaver E., Pringle J.R.,
RA Lew D.J.;
RT "Septin-dependent assembly of a cell cycle-regulatory module in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 20:4049-4061(2000).
RN [13]
RP FUNCTION.
RX PubMed=11404321; DOI=10.1093/genetics/158.2.549;
RA La Valle R., Wittenberg C.;
RT "A role for the Swe1 checkpoint kinase during filamentous growth of
RT Saccharomyces cerevisiae.";
RL Genetics 158:549-562(2001).
RN [14]
RP INTERACTION WITH HSL7.
RX PubMed=11408575; DOI=10.1091/mbc.12.6.1645;
RA Cid V.J., Shulewitz M.J., McDonald K.L., Thorner J.;
RT "Dynamic localization of the Swe1 regulator Hsl7 during the Saccharomyces
RT cerevisiae cell cycle.";
RL Mol. Biol. Cell 12:1645-1669(2001).
RN [15]
RP INTERACTION WITH CDC5, AND SUBCELLULAR LOCATION.
RX PubMed=11438652; DOI=10.1128/mcb.21.15.4949-4959.2001;
RA Bartholomew C.R., Woo S.H., Chung Y.S., Jones C., Hardy C.F.;
RT "Cdc5 interacts with the Wee1 kinase in budding yeast.";
RL Mol. Cell. Biol. 21:4949-4959(2001).
RN [16]
RP FUNCTION.
RX PubMed=11283616; DOI=10.1038/35070104;
RA Harrison J.C., Bardes E.S.G., Ohya Y., Lew D.J.;
RT "A role for the Pkc1p/Mpk1p kinase cascade in the morphogenesis
RT checkpoint.";
RL Nat. Cell Biol. 3:417-420(2001).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 318-ARG--LYS-328;
RP LEU-320; LEU-324; PHE-327; LYS-328; LEU-331; TYR-332; GLU-797; ILE-806 AND
RP GLN-807.
RX PubMed=12388757; DOI=10.1091/mbc.e02-05-0283;
RA McMillan J.N., Theesfeld C.L., Harrison J.C., Bardes E.S.G., Lew D.J.;
RT "Determinants of Swe1p degradation in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 13:3560-3575(2002).
RN [18]
RP FUNCTION.
RX PubMed=12593792; DOI=10.1016/s0960-9822(03)00049-6;
RA Harvey S.L., Kellogg D.R.;
RT "Conservation of mechanisms controlling entry into mitosis: budding yeast
RT wee1 delays entry into mitosis and is required for cell size control.";
RL Curr. Biol. 13:264-275(2003).
RN [19]
RP INTERACTION WITH KCC4.
RX PubMed=12773812; DOI=10.1266/ggs.78.113;
RA Okuzaki D., Watanabe T., Tanaka S., Nojima H.;
RT "The Saccharomyces cerevisiae bud-neck proteins Kcc4 and Gin4 have distinct
RT but partially-overlapping cellular functions.";
RL Genes Genet. Syst. 78:113-126(2003).
RN [20]
RP FUNCTION.
RX PubMed=12840070; DOI=10.1242/jcs.00634;
RA Martinez-Anaya C., Dickinson J.R., Sudbery P.E.;
RT "In yeast, the pseudohyphal phenotype induced by isoamyl alcohol results
RT from the operation of the morphogenesis checkpoint.";
RL J. Cell Sci. 116:3423-3431(2003).
RN [21]
RP FUNCTION IN FILAMENTOUS GROWTH REGULATION.
RX PubMed=14565980; DOI=10.1091/mbc.e03-06-0375;
RA Jiang Y.W., Kang C.M.;
RT "Induction of S. cerevisiae filamentous differentiation by slowed DNA
RT synthesis involves Mec1, Rad53 and Swe1 checkpoint proteins.";
RL Mol. Biol. Cell 14:5116-5124(2003).
RN [22]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [23]
RP INDUCTION BY ETHANOL.
RX PubMed=15118337; DOI=10.1271/bbb.68.968;
RA Kubota S., Takeo I., Kume K., Kanai M., Shitamukai A., Mizunuma M.,
RA Miyakawa T., Shimoi H., Iefuji H., Hirata D.;
RT "Effect of ethanol on cell growth of budding yeast: genes that are
RT important for cell growth in the presence of ethanol.";
RL Biosci. Biotechnol. Biochem. 68:968-972(2004).
RN [24]
RP PHOSPHORYLATION AT SER-36; SER-102; SER-111; SER-118; THR-131; SER-136;
RP SER-156; SER-169; SER-225; SER-254; THR-280; SER-312; SER-379; SER-395;
RP SER-438; SER-610; THR-629 AND THR-688.
RX PubMed=15037762; DOI=10.1073/pnas.0400641101;
RA Sakchaisri K., Asano S., Yu L.-R., Shulewitz M.J., Park C.J., Park J.-E.,
RA Cho Y.-W., Veenstra T.D., Thorner J., Lee K.S.;
RT "Coupling morphogenesis to mitotic entry.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4124-4129(2004).
RN [25]
RP SUBCELLULAR LOCATION.
RX PubMed=15282802; DOI=10.1002/yea.1133;
RA Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.;
RT "Localization of proteins that are coordinately expressed with Cln2 during
RT the cell cycle.";
RL Yeast 21:793-800(2004).
RN [26]
RP FUNCTION, PHOSPHORYLATION AT SER-36; THR-45; SER-56; SER-63; SER-70;
RP THR-74; SER-105; SER-111; SER-118; THR-121; THR-124; SER-127; SER-133;
RP SER-136; THR-196; SER-201; SER-262; SER-263; SER-266; SER-284; SER-294;
RP SER-345; THR-367; THR-373; SER-379; THR-384; SER-610 AND THR-692, AND
RP INTERACTION WITH CLB2-CDC28.
RX PubMed=16096060; DOI=10.1016/j.cell.2005.05.029;
RA Harvey S.L., Charlet A., Haas W., Gygi S.P., Kellogg D.R.;
RT "Cdk1-dependent regulation of the mitotic inhibitor Wee1.";
RL Cell 122:407-420(2005).
RN [27]
RP FUNCTION.
RX PubMed=16360682; DOI=10.1016/j.cub.2005.11.039;
RA McNulty J.J., Lew D.J.;
RT "Swe1p responds to cytoskeletal perturbation, not bud size, in S.
RT cerevisiae.";
RL Curr. Biol. 15:2190-2198(2005).
RN [28]
RP FUNCTION, AND PHOSPHORYLATION BY CLB2-CDC28.
RX PubMed=15920482; DOI=10.1038/sj.emboj.7600683;
RA Asano S., Park J.-E., Sakchaisri K., Yu L.-R., Song S., Supavilai P.,
RA Veenstra T.D., Lee K.S.;
RT "Concerted mechanism of Swe1/Wee1 regulation by multiple kinases in budding
RT yeast.";
RL EMBO J. 24:2194-2204(2005).
RN [29]
RP FUNCTION.
RX PubMed=15956196; DOI=10.1073/pnas.0406987102;
RA Hu F., Aparicio O.M.;
RT "Swe1 regulation and transcriptional control restrict the activity of
RT mitotic cyclins toward replication proteins in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8910-8915(2005).
RN [30]
RP FUNCTION.
RX PubMed=16571676; DOI=10.1091/mbc.e05-11-1093;
RA Liu H., Wang Y.;
RT "The function and regulation of budding yeast Swe1 in response to
RT interrupted DNA synthesis.";
RL Mol. Biol. Cell 17:2746-2756(2006).
RN [31]
RP PHOSPHORYLATION BY CLB-CDC28.
RX PubMed=17614281; DOI=10.1016/j.cub.2007.05.075;
RA Keaton M.A., Bardes E.S.G., Marquitz A.R., Freel C.D., Zyla T.R.,
RA Rudolph J., Lew D.J.;
RT "Differential susceptibility of yeast S and M phase CDK complexes to
RT inhibitory tyrosine phosphorylation.";
RL Curr. Biol. 17:1181-1189(2007).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [34]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-741, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Protein kinase that acts as a negative regulator of entry
CC into mitosis (G2 to M transition) by phosphorylating and inhibiting the
CC mitosis-promoting cyclin B-bound CDC28 at 'Tyr-19'. SWE1-mediated
CC inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to
CC delay mitosis in response to defects in growth, actin organization or
CC bud formation. Inhibits the activity of B-type cyclins in replication
CC initiation strongly for CLB2, moderately for CLB3 and CLB4, and there
CC is no apparent inhibition for CLB5 and CLB6, correlating with the
CC normal expression timing of those cyclins. Hyperphosphorylation and
CC degradation of SWE1 when all checkpoint requirement are met releases
CC CLB2-CDC28 from inhibition and allows for progression through the cell
CC cycle. SWE1-dependent CDC28 phosphorylation is also required for
CC pachytene arrest upon activation of the recombination checkpoint during
CC meiosis. Also involved in the regulation of nitrogen starvation- and
CC short chain alcohol-induced filamentous growth, or filamentous
CC differentiation in response to slowed DNA synthesis. Can act both on
CC serines and on tyrosines. {ECO:0000269|PubMed:10454545,
CC ECO:0000269|PubMed:10490630, ECO:0000269|PubMed:10490648,
CC ECO:0000269|PubMed:10619027, ECO:0000269|PubMed:11283616,
CC ECO:0000269|PubMed:11404321, ECO:0000269|PubMed:12388757,
CC ECO:0000269|PubMed:12593792, ECO:0000269|PubMed:12840070,
CC ECO:0000269|PubMed:14565980, ECO:0000269|PubMed:15920482,
CC ECO:0000269|PubMed:15956196, ECO:0000269|PubMed:16096060,
CC ECO:0000269|PubMed:16360682, ECO:0000269|PubMed:16571676,
CC ECO:0000269|PubMed:8253069, ECO:0000269|PubMed:8930890,
CC ECO:0000269|PubMed:9822611}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with CLB2-CDC28. Partial hyperphosphorylation of
CC SWE1 by CLB2-CDC28 stabilizes the ternary complex of SWE1 and CLB2-
CC CDC28 and stimulates kinase activity of SWE1 in a positive feedback
CC loop, maintaining CLB2-CDC28 in the tyrosine-phosphorylated state.
CC Fully hyperphosphorylated SWE1 dissociates from CLB2-CDC28. Interacts
CC with HSL7, KCC4 and MET30. {ECO:0000269|PubMed:10490630,
CC ECO:0000269|PubMed:10490648, ECO:0000269|PubMed:11408575,
CC ECO:0000269|PubMed:11438652, ECO:0000269|PubMed:12773812,
CC ECO:0000269|PubMed:16096060, ECO:0000269|PubMed:9716410}.
CC -!- INTERACTION:
CC P32944; Q00684: CDC14; NbExp=3; IntAct=EBI-18607, EBI-4192;
CC P32944; P32562: CDC5; NbExp=4; IntAct=EBI-18607, EBI-4440;
CC P32944; P38274: HSL7; NbExp=4; IntAct=EBI-18607, EBI-21618;
CC P32944; P13185: KIN1; NbExp=3; IntAct=EBI-18607, EBI-9716;
CC -!- SUBCELLULAR LOCATION: Bud neck. Nucleus. Note=When SWE1 first
CC accumulates in G1, it is localized to the nucleus. After bud emergence,
CC a subpopulation is recruited to the daughter side of the mother-bud
CC neck through HSL1 and its adapter HSL7, where it is susceptible to
CC hyperphosphorylation and degradation.
CC -!- INDUCTION: Expressed periodically during the cell cycle, with a peak in
CC late G1. Transcriptional repression requires ZDS1. Protein accumulation
CC is also periodic, peaking during S/G2 and declining prior to and during
CC nuclear division of the unperturbed cell cycle. Stabilized during a
CC checkpoint response in G2. Induced during meiosis. Induced by ethanol
CC (at protein level). {ECO:0000269|PubMed:10619027,
CC ECO:0000269|PubMed:15118337, ECO:0000269|PubMed:8647431,
CC ECO:0000269|PubMed:8930890, ECO:0000269|PubMed:9822611}.
CC -!- PTM: Ubiquitinated by the SCF(MET30) complex, leading to its
CC degradation by the proteasome. {ECO:0000269|PubMed:9716410}.
CC -!- PTM: Phosphorylated progressively by CLA4, CLB2-CDC28 and CDC5. CLA4-
CC dependent phosphorylation occurs in late S phase, followed by
CC phosphorylation by CLB2-CDC28 in early G2, when the levels of mitotic
CC CLB2 increases. This phosphorylation is critical for triggering
CC subsequent SWE1-CDC5 interaction and CDC5-dependent phosphorylation.
CC The resulting cumulative hyperphosphorylation down-regulates SWE1 by
CC targeting it for ubiquitin-mediated degradation. This stepwise
CC phosphorylation is thought to be a mechanism to integrate the different
CC checkpoint requirements before entry into mitosis.
CC {ECO:0000269|PubMed:14574415, ECO:0000269|PubMed:15037762,
CC ECO:0000269|PubMed:15920482, ECO:0000269|PubMed:16096060,
CC ECO:0000269|PubMed:17614281, ECO:0000269|PubMed:8253069,
CC ECO:0000269|PubMed:9822611}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X73966; CAA52150.1; -; Genomic_DNA.
DR EMBL; Z49462; CAA89482.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08619.1; -; Genomic_DNA.
DR PIR; S40400; S40400.
DR RefSeq; NP_012348.1; NM_001181620.1.
DR AlphaFoldDB; P32944; -.
DR SMR; P32944; -.
DR BioGRID; 33575; 464.
DR DIP; DIP-2410N; -.
DR ELM; P32944; -.
DR IntAct; P32944; 35.
DR MINT; P32944; -.
DR STRING; 4932.YJL187C; -.
DR iPTMnet; P32944; -.
DR MaxQB; P32944; -.
DR PaxDb; P32944; -.
DR PRIDE; P32944; -.
DR EnsemblFungi; YJL187C_mRNA; YJL187C; YJL187C.
DR GeneID; 853252; -.
DR KEGG; sce:YJL187C; -.
DR SGD; S000003723; SWE1.
DR VEuPathDB; FungiDB:YJL187C; -.
DR eggNOG; KOG0601; Eukaryota.
DR GeneTree; ENSGT00940000159427; -.
DR HOGENOM; CLU_007696_0_0_1; -.
DR InParanoid; P32944; -.
DR OMA; RFIHDSC; -.
DR BioCyc; YEAST:G3O-31620-MON; -.
DR Reactome; R-SCE-156711; Polo-like kinase mediated events.
DR PRO; PR:P32944; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32944; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0044879; P:mitotic morphogenesis checkpoint signaling; IDA:SGD.
DR GO; GO:0010697; P:negative regulation of mitotic spindle pole body separation; IMP:SGD.
DR GO; GO:0090154; P:positive regulation of sphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0000320; P:re-entry into mitotic cell cycle; IGI:SGD.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Isopeptide bond; Kinase; Magnesium;
KW Meiosis; Metal-binding; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tyrosine-protein kinase; Ubl conjugation.
FT CHAIN 1..819
FT /note="Mitosis inhibitor protein kinase SWE1"
FT /id="PRO_0000086727"
FT DOMAIN 444..794
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 86..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 579
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 450..458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 584
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762,
FT ECO:0000269|PubMed:16096060"
FT MOD_RES 45
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 56
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 63
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 74
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 102
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 105
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 111
FT /note="Phosphoserine; by CDC5, CDC28 and CLA4"
FT /evidence="ECO:0000269|PubMed:15037762,
FT ECO:0000269|PubMed:16096060"
FT MOD_RES 118
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762,
FT ECO:0000269|PubMed:16096060"
FT MOD_RES 121
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 124
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 127
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 131
FT /note="Phosphothreonine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 133
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 136
FT /note="Phosphoserine; by CDC28 and CLA4"
FT /evidence="ECO:0000269|PubMed:15037762,
FT ECO:0000269|PubMed:16096060"
FT MOD_RES 156
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 169
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 196
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 201
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 225
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 254
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 263
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 266
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 280
FT /note="Phosphothreonine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 312
FT /note="Phosphoserine; by CLA4"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 367
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 373
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 379
FT /note="Phosphoserine; by CDC5 and CLA4"
FT /evidence="ECO:0000269|PubMed:15037762,
FT ECO:0000269|PubMed:16096060, ECO:0007744|PubMed:19779198"
FT MOD_RES 384
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:16096060"
FT MOD_RES 395
FT /note="Phosphoserine; by CDC5 and CLA4"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 438
FT /note="Phosphoserine; by CDC5 and CLA4"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 610
FT /note="Phosphoserine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762,
FT ECO:0000269|PubMed:16096060"
FT MOD_RES 629
FT /note="Phosphothreonine; by CDC5"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 688
FT /note="Phosphothreonine; by CDC5 and CLA4"
FT /evidence="ECO:0000269|PubMed:15037762"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16096060"
FT CROSSLNK 741
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 318..328
FT /note="Missing: Impairs interaction with HSL7 and prevents
FT bud neck localization and degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 320
FT /note="L->P,Q: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 324
FT /note="L->S: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 327
FT /note="F->S: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 328
FT /note="K->E: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 331
FT /note="L->I: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 332
FT /note="Y->C: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 473
FT /note="K->A,P: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:10454545"
FT MUTAGEN 797
FT /note="E->K,V,G: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 806
FT /note="I->T,A,N: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
FT MUTAGEN 807
FT /note="Q->R,E: Prevents degradation."
FT /evidence="ECO:0000269|PubMed:12388757"
SQ SEQUENCE 819 AA; 92468 MW; F49FE73937958A02 CRC64;
MSSLDEDEED FEMLDTENLQ FMGKKMFGKQ AGEDESDDFA IGGSTPTNKL KFYPYSNNKL
TRSTGTLNLS LSNTALSEAN SKFLGKIEEE EEEEEEGKDE ESVDSRIKRW SPFHENESVT
TPITKRSAEK TNSPISLKQW NQRWFPKNDA RTENTSSSSS YSVAKPNQSA FTSSGLVSKM
SMDTSLYPAK LRIPETPVKK SPLVEGRDHK HVHLSSSKNA SSSLSVSPLN FVEDNNLQED
LLFSDSPSSK ALPSIHVPTI DSSPLSEAKY HAHDRHNNQT NILSPTNSLV TNSSPQTLHS
NKFKKIKRAR NSVILKNREL TNSLQQFKDD LYGTDENFPP PIIISSHHST RKNPQPYQFR
GRYDNDTDEE ISTPTRRKSI IGATSQTHRE SRPLSLSSAI VTNTTSAETH SISSTDSSPL
NSKRRLISSN KLSANPDSHL FEKFTNVHSI GKGQFSTVYQ VTFAQTNKKY AIKAIKPNKY
NSLKRILLEI KILNEVTNQI TMDQEGKEYI IDYISSWKFQ NSYYIMTELC ENGNLDGFLQ
EQVIAKKKRL EDWRIWKIIV ELSLALRFIH DSCHIVHLDL KPANVMITFE GNLKLGDFGM
ATHLPLEDKS FENEGDREYI APEIISDCTY DYKADIFSLG LMIVEIAANV VLPDNGNAWH
KLRSGDLSDA GRLSSTDIHS ESLFSDITKV DTNDLFDFER DNISGNSNNA GTSTVHNNSN
INNPNMNNGN DNNNVNTAAT KNRLILHKSS KIPAWVPKFL IDGESLERIV RWMIEPNYER
RPTANQILQT EECLYVEMTR NAGAIIQEDD FGPKPKFFI
