IPL1_YEAST
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 03-AUG-2022, entry version 211.
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}.
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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; 508.
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; P38991; -.
DR PRIDE; P38991; -.
DR EnsemblFungi; YPL209C_mRNA; YPL209C; YPL209C.
DR GeneID; 855892; -.
DR KEGG; sce:YPL209C; -.
DR SGD; S000006130; IPL1.
DR VEuPathDB; FungiDB:YPL209C; -.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_6_1; -.
DR InParanoid; P38991; -.
DR OMA; PHTKNVD; -.
DR BioCyc; YEAST:G3O-34100-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
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:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:SGD.
DR GO; GO:0051316; P:attachment of spindle microtubules to kinetochore involved in meiotic chromosome segregation; IC:ComplexPortal.
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; IC: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; IC:ComplexPortal.
DR InterPro; IPR030616; Aur.
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; PTHR24350; 1.
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; 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
