ID SWE1_YEAST Reviewed; 819 AA. AC P32944; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 23-JAN-2007, entry version 57. DE Mitosis inhibitor protein kinase SWE1 (EC 2.7.11.1). GN Name=SWE1; OrderedLocusNames=YJL187C; ORFNames=J0406; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94074541; PubMed=8253069; 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 96604 / S288c / FY1679; RX MEDLINE=96208490; PubMed=8641269; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., RA Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., RA Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., RA Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., RA Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., RA Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., RA Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., RA Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., RA Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., RA Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., RA Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT X."; RL EMBO J. 15:2031-2049(1996). RN [3] RP INTERACTION WITH KCC4. RX MEDLINE=22658157; 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 RT distinct but partially-overlapping cellular functions."; RL Genes Genet. Syst. 78:113-126(2003). CC -!- FUNCTION: Protein kinase that acts both on serines and on CC tyrosines. It acts as a negative regulator of entry into mitosis CC (G2 to M transition). Phosphorylates and inhibits CDC28. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with KCC4. CC -!- INTERACTION: CC P25389:KCC4; NbExp=1; IntAct=EBI-18607, EBI-9607; CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. WEE1 CC subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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 PIR; S40400; S40400. DR DIP; DIP:2410N; -. DR IntAct; P32944; -. DR Ensembl; YJL187C; Saccharomyces cerevisiae. DR GenomeReviews; Y13136_GR; YJL187C. DR KEGG; sce:YJL187C; -. DR SGD; S000003723; SWE1. DR BioCyc; SCER-S28-01:SCER-S28-01-003271-MONOMER; -. DR LinkHub; P32944; -. DR GermOnline; YJL187C; Saccharomyces cerevisiae. DR GO; GO:0005935; C:bud neck; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004672; F:protein kinase activity; IDA:SGD. DR GO; GO:0000078; P:cell morphogenesis checkpoint; IDA:SGD. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:SGD. DR GO; GO:0008361; P:regulation of cell size; IMP:SGD. DR GO; GO:0000079; P:regulation of cyclin-dependent protein kina...; IDA:SGD. DR GO; GO:0040020; P:regulation of meiosis; IEP:SGD. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW ATP-binding; Cell cycle; Cell division; Complete proteome; Kinase; KW Mitosis; Nucleotide-binding; Transferase; Tyrosine-protein kinase. FT CHAIN 1 819 Mitosis inhibitor protein kinase SWE1. FT /FTId=PRO_0000086727. FT DOMAIN 444 794 Protein kinase. FT NP_BIND 450 458 ATP (By similarity). FT ACT_SITE 579 579 Proton acceptor (By similarity). FT BINDING 473 473 ATP (By similarity). 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 //