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 27-MAR-2024, entry version 202. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 466. 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; 4932-YJL187C; -. DR PeptideAtlas; P32944; -. DR EnsemblFungi; YJL187C_mRNA; YJL187C; YJL187C. DR GeneID; 853252; -. DR KEGG; sce:YJL187C; -. DR AGR; SGD:S000003723; -. 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 OrthoDB; 928649at2759; -. DR BioCyc; YEAST:G3O-31620-MONOMER; -. DR Reactome; R-SCE-156711; Polo-like kinase mediated events. DR BioGRID-ORCS; 853252; 0 hits in 13 CRISPR screens. 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:0005737; C:cytoplasm; IBA:GO_Central. 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; IEA:UniProtKB-KW. 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; IEA:UniProtKB-KW. DR GO; GO:0044879; P:mitotic morphogenesis checkpoint signaling; IDA:SGD. DR GO; GO:0110031; P:negative regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central. DR GO; GO:0010697; P:negative regulation of mitotic spindle pole body separation; IMP:SGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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:0040020; P:regulation of meiotic nuclear division; IMP:SGD. DR CDD; cd14052; PTKc_Wee1_fungi; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1. DR PANTHER; PTHR11042:SF185; WEE1-LIKE PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //