ID IPL1_YEAST Reviewed; 367 AA. AC P38991; D6W3G1; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=Spindle assembly checkpoint kinase; DE EC=2.7.11.1; DE AltName: Full=Aurora kinase; DE AltName: Full=Increase-in-ploidy protein 1; GN Name=IPL1; OrderedLocusNames=YPL209C; 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], AND MUTAGENESIS OF THR-260; PRO-340 AND RP HIS-352. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8007975; DOI=10.1128/mcb.14.7.4731-4740.1994; RA Francisco L., Wang W., Chan C.S.M.; RT "Type 1 protein phosphatase acts in opposition to Ipl1 protein kinase in RT regulating yeast chromosome segregation."; RL Mol. Cell. Biol. 14:4731-4740(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP SUBCELLULAR LOCATION. RX PubMed=10385519; DOI=10.1083/jcb.145.7.1381; RA Kim J.-H., Kang J.-S., Chan C.S.M.; RT "Sli15 associates with the ipl1 protein kinase to promote proper chromosome RT segregation in Saccharomyces cerevisiae."; RL J. Cell Biol. 145:1381-1394(1999). RN [6] RP FUNCTION IN PHOSPHORYLATION OF HISTONE H3. RX PubMed=10975519; DOI=10.1016/s0092-8674(00)00034-9; RA Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., RA Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., RA Allis C.D.; RT "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase RT and Glc7/PP1 phosphatase in budding yeast and nematodes."; RL Cell 102:279-291(2000). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=11724818; DOI=10.1083/jcb.200105029; RA Kang J.-S., Cheeseman I.M., Kallstrom G., Velmurugan S., Barnes G., RA Chan C.S.M.; RT "Functional cooperation of Dam1, Ipl1, and the inner centromere protein RT (INCENP)-related protein Sli15 during chromosome segregation."; RL J. Cell Biol. 155:763-774(2001). RN [8] RP FUNCTION. RX PubMed=11853667; DOI=10.1016/s0092-8674(02)00633-5; RA Tanaka T.U., Rachidi N., Janke C., Pereira G., Galova M., Schiebel E., RA Stark M.J.R., Nasmyth K.; RT "Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes RT chromosome bi-orientation by altering kinetochore-spindle pole RT connections."; RL Cell 108:317-329(2002). RN [9] RP FUNCTION, AND PHOSPHORYLATION AT SER-5; SER-76 AND THR-260. RX PubMed=12408861; DOI=10.1016/s0092-8674(02)00973-x; RA Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S., RA Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.; RT "Phospho-regulation of kinetochore-microtubule attachments by the Aurora RT kinase Ipl1p."; RL Cell 111:163-172(2002). RN [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [12] RP FUNCTION. RX PubMed=23454383; DOI=10.1016/j.bbrc.2013.02.081; RA Vieillemard A., Prouzet-Mauleon V., Hugues M., Lefebvre F., Mitteau R., RA Claverol S., Bonneu M., Crouzet M., Doignon F., Thoraval D.; RT "The Saccharomyces cerevisiae RhoGAP Rgd1 is phosphorylated by the Aurora B RT like kinase Ipl1."; RL Biochem. Biophys. Res. Commun. 433:1-5(2013). CC -!- FUNCTION: Required for high-fidelity chromosome segregation during the CC later part of each cell cycle. Acts in opposition to the phosphatase CC PP1. Has a role in attaching the kinetochores to the microtubules and CC ensuring that sister kinetochores connect to opposite poles. The CC promotion of bi-orientation is achieved by selectively detaching CC kinetochore-microtubule attachments that are not under tension. CC Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis. CC Phosphorylates RGD1 in vitro. {ECO:0000269|PubMed:10975519, CC ECO:0000269|PubMed:11853667, ECO:0000269|PubMed:12408861, CC ECO:0000269|PubMed:23454383}. 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 -!- INTERACTION: CC P38991; P47134: BIR1; NbExp=4; IntAct=EBI-9319, EBI-3648; CC P38991; P38283: SLI15; NbExp=10; IntAct=EBI-9319, EBI-20842; CC P38991; P68431: H3C12; Xeno; NbExp=2; IntAct=EBI-9319, EBI-79722; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. CC Chromosome, centromere, kinetochore. Note=Associates with the mitotic CC spindle and on elongated and disassembling spindles. Also associated CC with the kinetochore. CC -!- MISCELLANEOUS: Present with 149 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. Aurora subfamily. {ECO:0000255|PROSITE- CC 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; U07163; AAA20496.1; -; Genomic_DNA. DR EMBL; Z73565; CAA97924.1; -; Genomic_DNA. DR EMBL; AY693182; AAT93201.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11227.1; -; Genomic_DNA. DR PIR; S47923; S47923. DR RefSeq; NP_015115.1; NM_001184023.1. DR AlphaFoldDB; P38991; -. DR SMR; P38991; -. DR BioGRID; 35976; 513. DR ComplexPortal; CPX-1900; Chromosomal passenger complex. DR DIP; DIP-2771N; -. DR IntAct; P38991; 11. DR MINT; P38991; -. DR STRING; 4932.YPL209C; -. DR iPTMnet; P38991; -. DR MaxQB; P38991; -. DR PaxDb; 4932-YPL209C; -. DR PeptideAtlas; P38991; -. DR EnsemblFungi; YPL209C_mRNA; YPL209C; YPL209C. DR GeneID; 855892; -. DR KEGG; sce:YPL209C; -. DR AGR; SGD:S000006130; -. DR SGD; S000006130; IPL1. DR VEuPathDB; FungiDB:YPL209C; -. DR eggNOG; KOG0580; Eukaryota. DR HOGENOM; CLU_000288_63_6_1; -. DR InParanoid; P38991; -. DR OMA; WIVKHCK; -. DR OrthoDB; 117459at2759; -. DR BioCyc; YEAST:G3O-34100-MONOMER; -. DR BRENDA; 2.7.11.1; 984. DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR BioGRID-ORCS; 855892; 3 hits in 13 CRISPR screens. DR PRO; PR:P38991; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; P38991; Protein. DR GO; GO:0032133; C:chromosome passenger complex; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0000776; C:kinetochore; IDA:SGD. DR GO; GO:0005828; C:kinetochore microtubule; IDA:SGD. DR GO; GO:0005874; C:microtubule; HDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0005819; C:spindle; IDA:SGD. DR GO; GO:0005876; C:spindle microtubule; IDA:SGD. DR GO; GO:0051233; C:spindle midzone; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IDA: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:0051316; P:attachment of meiotic spindle microtubules to kinetochore; NAS:ComplexPortal. DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:SGD. DR GO; GO:0007059; P:chromosome segregation; IMP:SGD. DR GO; GO:0045143; P:homologous chromosome segregation; IMP:SGD. DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:SGD. DR GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; IGI:SGD. DR GO; GO:0051228; P:mitotic spindle disassembly; IMP:SGD. DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central. DR GO; GO:1901925; P:negative regulation of protein import into nucleus during spindle assembly checkpoint; IMP:SGD. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:CACAO. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:CACAO. DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; NAS:ComplexPortal. DR GO; GO:0032465; P:regulation of cytokinesis; IMP:SGD. DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:SGD. DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:SGD. DR GO; GO:0031134; P:sister chromatid biorientation; NAS:ComplexPortal. DR CDD; cd14007; STKc_Aurora; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR030616; Aur-like. 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; PTHR24350:SF0; AURORA KINASE; 1. DR PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-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; Centromere; Chromosome; Chromosome partition; KW Cytoplasm; Cytoskeleton; Kinase; Kinetochore; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1..367 FT /note="Spindle assembly checkpoint kinase" FT /id="PRO_0000086029" FT DOMAIN 104..355 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..50 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 227 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 110..118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 133 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 5 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:12408861" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12408861" FT MOD_RES 260 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:12408861" FT MUTAGEN 260 FT /note="T->A: In IPL1-4; causes missegregation of FT chromosomes at 37 degrees Celsius." FT /evidence="ECO:0000269|PubMed:8007975" FT MUTAGEN 340 FT /note="P->L: In IPL1-1; causes missegregation of FT chromosomes at 37 degrees Celsius." FT /evidence="ECO:0000269|PubMed:8007975" FT MUTAGEN 352 FT /note="H->Y: In IPL1-2; causes missegregation of FT chromosomes at 37 degrees Celsius." FT /evidence="ECO:0000269|PubMed:8007975" SQ SEQUENCE 367 AA; 42946 MW; 44E3EFDDE1CDB35E CRC64; MQRNSLVNIK LNANSPSKKT TTRPNTSRIN KPWRISHSPQ QRNPNSKIPS PVREKLNRLP VNNKKFLDME SSKIPSPIRK ATSSKMIHEN KKLPKFKSLS LDDFELGKKL GKGKFGKVYC VRHRSTGYIC ALKVMEKEEI IKYNLQKQFR REVEIQTSLN HPNLTKSYGY FHDEKRVYLL MEYLVNGEMY KLLRLHGPFN DILASDYIYQ IANALDYMHK KNIIHRDIKP ENILIGFNNV IKLTDFGWSI INPPENRRKT VCGTIDYLSP EMVESREYDH TIDAWALGVL AFELLTGAPP FEEEMKDTTY KRIAALDIKM PSNISQDAQD LILKLLKYDP KDRMRLGDVK MHPWILRNKP FWENKRL //