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CDC15_YEAST
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   03-AUG-2022, entry version 206.
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}.
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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; 415.
DR   DIP; DIP-5728N; -.
DR   IntAct; P27636; 16.
DR   MINT; P27636; -.
DR   STRING; 4932.YAR019C; -.
DR   iPTMnet; P27636; -.
DR   MaxQB; P27636; -.
DR   PaxDb; P27636; -.
DR   PRIDE; P27636; -.
DR   TopDownProteomics; P27636; -.
DR   EnsemblFungi; YAR019C_mRNA; YAR019C; YAR019C.
DR   GeneID; 851274; -.
DR   KEGG; sce:YAR019C; -.
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   BioCyc; YEAST:G3O-28875-MON; -.
DR   BRENDA; 2.7.11.1; 984.
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:1903024; P:positive regulation of ascospore-type prospore membrane formation; IMP:SGD.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007096; P:regulation of exit from mitosis; 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; 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
 
 
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