ID CDC15_YEAST Reviewed; 974 AA. AC P27636; D6VPM6; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 27-MAR-2024, entry version 213. DE RecName: Full=Cell division control protein 15; DE EC=2.7.11.1; GN Name=CDC15; Synonyms=LYT1; OrderedLocusNames=YAR019C; 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]. RX PubMed=1495480; DOI=10.1007/bf00272358; RA Schweitzer B., Philippsen P.; RT "NPK1, a nonessential protein kinase gene in Saccharomyces cerevisiae with RT similarity to Aspergillus nidulans nimA."; RL Mol. Gen. Genet. 234:164-167(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c / GRF88; RX PubMed=1882551; DOI=10.1002/yea.320070308; RA Schweitzer B., Philippsen P.; RT "CDC15, an essential cell cycle gene in Saccharomyces cerevisiae, encodes a RT protein kinase domain."; RL Yeast 7:265-273(1991). RN [3] RP SEQUENCE REVISION TO 900-902. RA Schweitzer B.; RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX PubMed=7941740; DOI=10.1002/yea.320100413; RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.; RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 RT kbp SPO7-CENI-CDC15 region."; RL Yeast 10:535-541(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809; RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., RA Storms R.K.; RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995). RN [6] RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 316; 321 AND 900-902. 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 865-974. RX PubMed=1658741; DOI=10.1093/nar/19.20.5731; RA Davies C.J., Hutchison C.A. III; RT "A directed DNA sequencing strategy based upon Tn3 transposon mutagenesis: RT application to the ADE1 locus on Saccharomyces cerevisiae chromosome I."; RL Nucleic Acids Res. 19:5731-5738(1991). RN [8] RP FUNCTION. RX PubMed=8491189; DOI=10.1002/j.1460-2075.1993.tb05846.x; RA Surana U., Amon A., Dowzer C., McGrew J., Byers B., Nasmyth K.; RT "Destruction of the CDC28/CLB mitotic kinase is not required for the RT metaphase to anaphase transition in budding yeast."; RL EMBO J. 12:1969-1978(1993). RN [9] RP FUNCTION. RX PubMed=8407833; DOI=10.1128/jb.175.20.6562-6570.1993; RA Molero G., Yuste-Rojas M., Montesi A., Vazquez A., Nombela C., Sanchez M.; RT "A cdc-like autolytic Saccharomyces cerevisiae mutant altered in budding RT site selection is complemented by SPO12, a sporulation gene."; RL J. Bacteriol. 175:6562-6570(1993). RN [10] RP FUNCTION. RX PubMed=8175878; DOI=10.1083/jcb.125.3.517; RA Guacci V., Hogan E., Koshland D.; RT "Chromosome condensation and sister chromatid pairing in budding yeast."; RL J. Cell Biol. 125:517-530(1994). RN [11] RP FUNCTION. RX PubMed=8668128; DOI=10.1007/bf02172916; RA Shirayama M., Matsui Y., Toh-e A.; RT "Dominant mutant alleles of yeast protein kinase gene CDC15 suppress the RT lte1 defect in termination of M phase and genetically interact with RT CDC14."; RL Mol. Gen. Genet. 251:176-185(1996). RN [12] RP FUNCTION. RX PubMed=10413604; DOI=10.1006/excr.1999.4531; RA Anghileri P., Branduardi P., Sternieri F., Monti P., Visintin R., RA Bevilacqua A., Alberghina L., Martegani E., Baroni M.D.; RT "Chromosome separation and exit from mitosis in budding yeast: dependence RT on growth revealed by cAMP-mediated inhibition."; RL Exp. Cell Res. 250:510-523(1999). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=10662594; DOI=10.1006/mcbr.1999.0173; RA Cenamor R., Jimenez J., Cid V.J., Nombela C., Sanchez M.; RT "The budding yeast Cdc15 localizes to the spindle pole body in a cell- RT cycle-dependent manner."; RL Mol. Cell Biol. Res. Commun. 2:178-184(1999). RN [14] RP PHOSPHORYLATION, DEPHOSPHORYLATION BY CDC14, SUBCELLULAR LOCATION, AND RP FUNCTION. RX PubMed=10744974; DOI=10.1016/s0960-9822(00)00382-1; RA Xu S., Huang H.K., Kaiser P., Latterich M., Hunter T.; RT "Phosphorylation and spindle pole body localization of the Cdc15p mitotic RT regulatory protein kinase in budding yeast."; RL Curr. Biol. 10:329-332(2000). RN [15] RP PHOSPHORYLATION, DEPHOSPHORYLATION BY CDC14, SUBCELLULAR LOCATION, AND RP FUNCTION. RX PubMed=11267871; DOI=10.1016/s0960-9822(01)00095-1; RA Menssen R., Neutzner A., Seufert W.; RT "Asymmetric spindle pole localization of yeast Cdc15 kinase links mitotic RT exit and cytokinesis."; RL Curr. Biol. 11:345-350(2001). RN [16] RP PHOSPHORYLATION, DEPHOSPHORYLATION BY CDC14, AND ACTIVITY REGULATION. RX PubMed=10837230; DOI=10.1016/s0960-9822(00)00491-7; RA Jaspersen S.L., Morgan D.O.; RT "Cdc14 activates cdc15 to promote mitotic exit in budding yeast."; RL Curr. Biol. 10:615-618(2000). RN [17] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11378390; DOI=10.1016/s0960-9822(01)00228-7; RA Lee S.E., Frenz L.M., Wells N.J., Johnson A.L., Johnston L.H.; RT "Order of function of the budding-yeast mitotic exit-network proteins Tem1, RT Cdc15, Mob1, Dbf2, and Cdc5."; RL Curr. Biol. 11:784-788(2001). RN [18] RP INTERACTION WITH TEM1, AND FUNCTION. RX PubMed=11290702; DOI=10.1093/genetics/157.4.1437; RA Asakawa K., Yoshida S., Otake F., Toh-e A.; RT "A novel functional domain of Cdc15 kinase is required for its interaction RT with Tem1 GTPase in Saccharomyces cerevisiae."; RL Genetics 157:1437-1450(2001). RN [19] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=11598184; DOI=10.1091/mbc.12.10.2961; RA Visintin R., Amon A.; RT "Regulation of the mitotic exit protein kinases Cdc15 and Dbf2."; RL Mol. Biol. Cell 12:2961-2974(2001). RN [20] RP FUNCTION. RX PubMed=11404483; DOI=10.1073/pnas.141098998; RA Mah A.S., Jang J., Deshaies R.J.; RT "Protein kinase Cdc15 activates the Dbf2-Mob1 kinase complex."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7325-7330(2001). RN [21] RP FUNCTION. RX PubMed=12937277; DOI=10.1091/mbc.e03-04-0238; RA Hwa Lim H., Yeong F.M., Surana U.; RT "Inactivation of mitotic kinase triggers translocation of MEN components to RT mother-daughter neck in yeast."; RL Mol. Biol. Cell 14:4734-4743(2003). RN [22] RP FUNCTION, SUBUNIT, AND DOMAIN. RX PubMed=12832486; DOI=10.1128/mcb.23.14.5018-5030.2003; RA Bardin A.J., Boselli M.G., Amon A.; RT "Mitotic exit regulation through distinct domains within the protein kinase RT Cdc15."; RL Mol. Cell. Biol. 23:5018-5030(2003). RN [23] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [24] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [25] RP SUBCELLULAR LOCATION. RX PubMed=14718561; DOI=10.1091/mbc.e03-09-0708; RA Molk J.N., Schuyler S.C., Liu J.Y., Evans J.G., Salmon E.D., Pellman D., RA Bloom K.; RT "The differential roles of budding yeast Tem1p, Cdc15p, and Bub2p protein RT dynamics in mitotic exit."; RL Mol. Biol. Cell 15:1519-1532(2004). RN [26] RP FUNCTION. RX PubMed=17660551; DOI=10.1534/genetics.107.076133; RA Pablo-Hernando M.E., Arnaiz-Pita Y., Nakanishi H., Dawson D., del Rey F., RA Neiman A.M., Vazquez de Aldana C.R.; RT "Cdc15 is required for spore morphogenesis independently of Cdc14 in RT Saccharomyces cerevisiae."; RL Genetics 177:281-293(2007). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [28] 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 [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, 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 [30] RP FUNCTION. RX PubMed=20046099; DOI=10.4161/cc.9.2.10448; RA Schleker T., Shimada K., Sack R., Pike B.L., Gasser S.M.; RT "Cell cycle-dependent phosphorylation of Rad53 kinase by Cdc5 and Cdc28 RT modulates checkpoint adaptation."; RL Cell Cycle 9:350-363(2010). RN [31] RP SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDK1, AND FUNCTION. RX PubMed=20123997; DOI=10.1083/jcb.200911128; RA Konig C., Maekawa H., Schiebel E.; RT "Mutual regulation of cyclin-dependent kinase and the mitotic exit RT network."; RL J. Cell Biol. 188:351-368(2010). RN [32] RP FUNCTION. RX PubMed=20442249; DOI=10.1242/jcs.063891; RA Meitinger F., Petrova B., Lombardi I.M., Bertazzi D.T., Hub B., RA Zentgraf H., Pereira G.; RT "Targeted localization of Inn1, Cyk3 and Chs2 by the mitotic-exit network RT regulates cytokinesis in budding yeast."; RL J. Cell Sci. 123:1851-1861(2010). RN [33] RP FUNCTION. RX PubMed=20505077; DOI=10.1091/mbc.e09-07-0637; RA Chai C.C., Teh E.M., Yeong F.M.; RT "Unrestrained spindle elongation during recovery from spindle checkpoint RT activation in cdc15-2 cells results in mis-segregation of chromosomes."; RL Mol. Biol. Cell 21:2384-2398(2010). RN [34] RP PHOSPHORYLATION AT SER-561; SER-567 AND THR-870. RX PubMed=22031224; DOI=10.4161/cc.10.20.17790; RA Jones M.H., Keck J.M., Wong C.C., Xu T., Yates J.R. III, Winey M.; RT "Cell cycle phosphorylation of mitotic exit network (MEN) proteins."; RL Cell Cycle 10:3435-3440(2011). RN [35] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21937712; DOI=10.1101/gad.17257711; RA Rock J.M., Amon A.; RT "Cdc15 integrates Tem1 GTPase-mediated spatial signals with Polo kinase- RT mediated temporal cues to activate mitotic exit."; RL Genes Dev. 25:1943-1954(2011). RN [36] RP FUNCTION. RX PubMed=21987786; DOI=10.1073/pnas.1106448108; RA Ratsima H., Ladouceur A.M., Pascariu M., Sauve V., Salloum Z., Maddox P.S., RA D'Amours D.; RT "Independent modulation of the kinase and polo-box activities of Cdc5 RT protein unravels unique roles in the maintenance of genome stability."; RL Proc. Natl. Acad. Sci. U.S.A. 108:E914-E923(2011). RN [37] RP FUNCTION. RX PubMed=22385961; DOI=10.1016/j.cell.2012.01.041; RA Hotz M., Leisner C., Chen D., Manatschal C., Wegleiter T., Ouellet J., RA Lindstrom D., Gottschling D.E., Vogel J., Barral Y.; RT "Spindle pole bodies exploit the mitotic exit network in metaphase to drive RT their age-dependent segregation."; RL Cell 148:958-972(2012). RN [38] RP FUNCTION. RX PubMed=22718910; DOI=10.1091/mbc.e12-03-0235; RA Attner M.A., Amon A.; RT "Control of the mitotic exit network during meiosis."; RL Mol. Biol. Cell 23:3122-3132(2012). RN [39] RP INDUCTION. RX PubMed=24013422; DOI=10.4161/cc.26257; RA Ball D.A., Adames N.R., Reischmann N., Barik D., Franck C.T., Tyson J.J., RA Peccoud J.; RT "Measurement and modeling of transcriptional noise in the cell cycle RT regulatory network."; RL Cell Cycle 12:3203-3218(2013). RN [40] RP FUNCTION. RX PubMed=24039885; DOI=10.1371/journal.pone.0073194; RA Faust A.M., Wong C.C., Yates Iii J.R., Drubin D.G., Barnes G.; RT "The FEAR protein Slk19 restricts Cdc14 phosphatase to the nucleus until RT the end of anaphase, regulating its participation in mitotic exit in RT Saccharomyces cerevisiae."; RL PLoS ONE 8:E73194-E73194(2013). CC -!- FUNCTION: Protein kinase of the mitotic exit network (MEN) essential CC for late nuclear division in the mitotic cycle. Promotes mitotic exit CC by phosphorylating DBF2 and directly switching on DBF2 kinase activity. CC Involved in the localization of DBF2 and DBF20 to the neck which is CC necessary to undergo cytokinesis. Plays a role in segregation of CC chromosomes during recovery from spindle checkpoint activation. CC Required for spindle pole localization of CDK1 and inactivation of CDC2 CC kinase activity at the end of mitosis. Required for spindle disassembly CC after meiosis II and plays a role in spore morphogenesis. CC {ECO:0000269|PubMed:10413604, ECO:0000269|PubMed:10744974, CC ECO:0000269|PubMed:11267871, ECO:0000269|PubMed:11290702, CC ECO:0000269|PubMed:11378390, ECO:0000269|PubMed:11404483, CC ECO:0000269|PubMed:11598184, ECO:0000269|PubMed:12832486, CC ECO:0000269|PubMed:12937277, ECO:0000269|PubMed:17660551, CC ECO:0000269|PubMed:20046099, ECO:0000269|PubMed:20123997, CC ECO:0000269|PubMed:20442249, ECO:0000269|PubMed:20505077, CC ECO:0000269|PubMed:21937712, ECO:0000269|PubMed:21987786, CC ECO:0000269|PubMed:22385961, ECO:0000269|PubMed:22718910, CC ECO:0000269|PubMed:24039885, ECO:0000269|PubMed:8175878, CC ECO:0000269|PubMed:8407833, ECO:0000269|PubMed:8491189, CC ECO:0000269|PubMed:8668128}. 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 -!- ACTIVITY REGULATION: Kinase activity is inhibited by phosphorylation CC and activated by dephosphorylation by CDC14. CC {ECO:0000269|PubMed:10837230}. CC -!- SUBUNIT: Homodimer. Interacts with TEM1. {ECO:0000269|PubMed:11290702, CC ECO:0000269|PubMed:12832486}. CC -!- INTERACTION: CC P27636; P38987: TEM1; NbExp=6; IntAct=EBI-4200, EBI-19113; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole. Bud neck. CC Note=Localizes to the spindle pole bodies at late anaphase and CC translocates to the cytoplasm upon DNA replication stress. Localization CC to SPBs depends on CDC5 and TEM1 and is inhibited by BUB2. Accumulates CC at the daughter SPB after anaphase onset when the daughter SPB begins CC to penetrate the bud neck. Not found in the mother SPD during early CC anaphase. As anaphase proceeds, continues to accumulate on the daughter CC SPB and also localizes to the mother SPB. At the end of telophase, a CC portion of CDC15 localizes at the mother-bud neck. CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:24013422}. CC -!- DOMAIN: The region between residues 360 and 702 is essential for CC function and is required for self-association and for binding to CC spindle pole bodies. {ECO:0000269|PubMed:12832486}. CC -!- DOMAIN: The region between residues 751 and 974 is an auto-inhibitory CC domain which inhibits MEN signaling. {ECO:0000269|PubMed:12832486}. CC -!- PTM: Phosphorylation by CDK1 reduces the binding to the mother spindle CC pole body. The extent of phosphorylation gradually increases during CC cell-cycle progression until some point during late anaphase/telophase CC when it is rapidly dephosphorylated by CDC14. Phosphorylation inhibits CC kinase activity and dephosphorylation by CDC14 activates CDC15. CC {ECO:0000269|PubMed:10744974, ECO:0000269|PubMed:10837230, CC ECO:0000269|PubMed:11267871, ECO:0000269|PubMed:20123997, CC ECO:0000269|PubMed:22031224}. CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator. CC {ECO:0000305}. 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; X60549; CAA43041.1; -; Genomic_DNA. DR EMBL; X52683; CAA36906.1; -; Genomic_DNA. DR EMBL; L22015; AAC04965.1; -; Genomic_DNA. DR EMBL; M67445; AAA34400.1; -; Genomic_DNA. DR EMBL; BK006935; DAA06996.2; -; Genomic_DNA. DR PIR; S15038; S15038. DR RefSeq; NP_009411.2; NM_001178218.2. DR AlphaFoldDB; P27636; -. DR SMR; P27636; -. DR BioGRID; 31801; 419. DR DIP; DIP-5728N; -. DR IntAct; P27636; 16. DR MINT; P27636; -. DR STRING; 4932.YAR019C; -. DR iPTMnet; P27636; -. DR MaxQB; P27636; -. DR PaxDb; 4932-YAR019C; -. DR PeptideAtlas; P27636; -. DR TopDownProteomics; P27636; -. DR EnsemblFungi; YAR019C_mRNA; YAR019C; YAR019C. DR GeneID; 851274; -. DR KEGG; sce:YAR019C; -. DR AGR; SGD:S000000072; -. DR SGD; S000000072; CDC15. DR VEuPathDB; FungiDB:YAR019C; -. DR eggNOG; KOG0198; Eukaryota. DR GeneTree; ENSGT00940000176374; -. DR HOGENOM; CLU_006413_0_0_1; -. DR InParanoid; P27636; -. DR OMA; KYHGFIQ; -. DR OrthoDB; 5481100at2759; -. DR BioCyc; YEAST:G3O-28875-MONOMER; -. DR BRENDA; 2.7.11.1; 984. DR Reactome; R-SCE-2871796; FCERI mediated MAPK activation. DR Reactome; R-SCE-383280; Nuclear Receptor transcription pathway. DR BioGRID-ORCS; 851274; 1 hit in 13 CRISPR screens. DR PRO; PR:P27636; -. DR Proteomes; UP000002311; Chromosome I. DR RNAct; P27636; Protein. DR GO; GO:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0005816; C:spindle pole body; IDA:SGD. DR GO; GO:0005524; F:ATP 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; IDA:SGD. DR GO; GO:0051229; P:meiotic spindle disassembly; IMP:SGD. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:SGD. DR GO; GO:1904750; P:negative regulation of protein localization to nucleolus; IMP:SGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:1903024; P:positive regulation of ascospore-type prospore membrane formation; IMP:SGD. DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:SGD. 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; PTHR48012:SF26; SERINE_THREONINE-PROTEIN KINASE DDB_G0283821; 1. DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 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; Cytoplasm; Cytoskeleton; Kinase; KW Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..974 FT /note="Cell division control protein 15" FT /id="PRO_0000085717" FT DOMAIN 25..272 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 360..702 FT /note="Self association domain" FT REGION 554..592 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 751..974 FT /note="Auto-inhibitory domain" FT REGION 941..974 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 960..974 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 31..39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 54 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 561 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22031224" FT MOD_RES 567 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22031224, FT ECO:0007744|PubMed:19779198" FT MOD_RES 870 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:22031224" FT CONFLICT 316 FT /note="A -> R (in Ref. 1; CAA43041, 2; CAA36906, 4 and 5; FT AAC04965)" FT /evidence="ECO:0000305" FT CONFLICT 321 FT /note="A -> P (in Ref. 1; CAA43041, 2; CAA36906, 4 and 5; FT AAC04965)" FT /evidence="ECO:0000305" FT CONFLICT 900..902 FT /note="KDV -> NGC (in Ref. 4; no nucleotide entry and 5; FT AAC04965)" FT /evidence="ECO:0000305" SQ SEQUENCE 974 AA; 110242 MW; 99383BD871A4A726 CRC64; MNSMADTDRV NLTPIQRASE KSVQYHLKQV IGRGSYGVVY KAINKHTDQV VAIKEVVYEN DEELNDIMAE ISLLKNLNHN NIVKYHGFIR KSYELYILLE YCANGSLRRL ISRSSTGLSE NESKTYVTQT LLGLKYLHGE GVIHRDIKAA NILLSADNTV KLADFGVSTI VNSSALTLAG TLNWMAPEIL GNRGASTLSD IWSLGATVVE MLTKNPPYHN LTDANIYYAV ENDTYYPPSS FSEPLKDFLS KCFVKNMYKR PTADQLLKHV WINSTENVKV DKLNKFKEDF TDADYHWDAD FQEEKLNISP SKFSLAAAPA AWAENNQELD LMPPTESQLL SQLKSSSKPL TDLHVLFSVC SLENIADTII ECLSRTTVDK RLITAFGSIF VYDTQHNHSR LRLKFIAMGG IPLIIKFEHL AKEFVIDYPQ TLIECGIMYP PNFASLKTPK YILELVYRFY DLTSTAFWCR WCFKHLDISL LLNNIHERRA QSILLKLSSY APWSFEKILP SLIDSKLKKK ILISPQITYV VFKSINYMIT TNDDKIHKSA IPSSSSLPLS SSPTRNSPVN SVQSPSRSPV HSLMATRPSS PMRHKSISNF PHLTISSKSR LLIELPEGFF TWLTSFFVDM AQIKDLSVLK YFTKLCYLTV HINSTFLNDL LDNDAFFAFI RNIDTIIPFI DDAKTAAFIW KQITAICVEM SLDMDQMSAS LFSTAMNFIR KKNNTSISGL EIILNCLHFT LRNVNDDVAP TVGSSESHSV FLIKVNNDAA IELPIDQLVD LFYALNDDDV NLSKLISIFT KICSLPGFEN LTINIIFHPN FYEKIVSFFD TYFNSLLIQI DLLKFIKLIF SKSLLKLYDY TGQPDPIKQT EPNRRNKATV FKLRAILVQI TEFLNNNWNK DVPKRNSNQV GGDSVLICQL CEDIRSLSKK GSLQKVSSVT AAIGSSPTKD ERSNLRSSKD KSDGFSVPIT TFQT //