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Spindle assembly checkpoint kinase (EC 2.7.11.1) (Aurora kinase) (Increase-in-ploidy protein 1)

 IPL1_YEAST              Reviewed;         367 AA.
P38991; D6W3G1;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
23-MAY-2018, entry version 185.
RecName: Full=Spindle assembly checkpoint kinase;
EC=2.7.11.1;
AltName: Full=Aurora kinase;
AltName: Full=Increase-in-ploidy protein 1;
Name=IPL1; OrderedLocusNames=YPL209C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-260; PRO-340
AND HIS-352.
STRAIN=ATCC 204508 / S288c;
PubMed=8007975; DOI=10.1128/MCB.14.7.4731;
Francisco L., Wang W., Chan C.S.M.;
"Type 1 protein phosphatase acts in opposition to Ipl1 protein kinase
in regulating yeast chromosome segregation.";
Mol. Cell. Biol. 14:4731-4740(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
SUBCELLULAR LOCATION.
PubMed=10385519; DOI=10.1083/jcb.145.7.1381;
Kim J.-H., Kang J.-S., Chan C.S.M.;
"Sli15 associates with the ipl1 protein kinase to promote proper
chromosome segregation in Saccharomyces cerevisiae.";
J. Cell Biol. 145:1381-1394(1999).
[6]
FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
PubMed=10975519; DOI=10.1016/S0092-8674(00)00034-9;
Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K.,
Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R.,
Smith M.M., Allis C.D.;
"Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora
kinase and Glc7/PP1 phosphatase in budding yeast and nematodes.";
Cell 102:279-291(2000).
[7]
SUBCELLULAR LOCATION.
PubMed=11724818; DOI=10.1083/jcb.200105029;
Kang J.-S., Cheeseman I.M., Kallstrom G., Velmurugan S., Barnes G.,
Chan C.S.M.;
"Functional cooperation of Dam1, Ipl1, and the inner centromere
protein (INCENP)-related protein Sli15 during chromosome
segregation.";
J. Cell Biol. 155:763-774(2001).
[8]
FUNCTION.
PubMed=11853667; DOI=10.1016/S0092-8674(02)00633-5;
Tanaka T.U., Rachidi N., Janke C., Pereira G., Galova M., Schiebel E.,
Stark M.J.R., Nasmyth K.;
"Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes
chromosome bi-orientation by altering kinetochore-spindle pole
connections.";
Cell 108:317-329(2002).
[9]
FUNCTION, AND PHOSPHORYLATION AT SER-5; SER-76 AND THR-260.
PubMed=12408861; DOI=10.1016/S0092-8674(02)00973-X;
Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,
Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.;
"Phospho-regulation of kinetochore-microtubule attachments by the
Aurora kinase Ipl1p.";
Cell 111:163-172(2002).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[12]
FUNCTION.
PubMed=23454383; DOI=10.1016/j.bbrc.2013.02.081;
Vieillemard A., Prouzet-Mauleon V., Hugues M., Lefebvre F.,
Mitteau R., Claverol S., Bonneu M., Crouzet M., Doignon F.,
Thoraval D.;
"The Saccharomyces cerevisiae RhoGAP Rgd1 is phosphorylated by the
Aurora B like kinase Ipl1.";
Biochem. Biophys. Res. Commun. 433:1-5(2013).
-!- FUNCTION: Required for high-fidelity chromosome segregation during
the later part of each cell cycle. Acts in opposition to the
phosphatase PP1. Has a role in attaching the kinetochores to the
microtubules and ensuring that sister kinetochores connect to
opposite poles. The promotion of bi-orientation is achieved by
selectively detaching kinetochore-microtubule attachments that are
not under tension. Phosphorylates histone H3 to form H3S10ph
during mitosis and meiosis. Phosphorylates RGD1 in vitro.
{ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:11853667,
ECO:0000269|PubMed:12408861, ECO:0000269|PubMed:23454383}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- INTERACTION:
P47134:BIR1; NbExp=4; IntAct=EBI-9319, EBI-3648;
P68431:HIST1H3D (xeno); NbExp=2; IntAct=EBI-9319, EBI-79722;
P38283:SLI15; NbExp=10; IntAct=EBI-9319, EBI-20842;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
Chromosome, centromere, kinetochore. Note=Associates with the
mitotic spindle and on elongated and disassembling spindles. Also
associated with the kinetochore.
-!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; U07163; AAA20496.1; -; Genomic_DNA.
EMBL; Z73565; CAA97924.1; -; Genomic_DNA.
EMBL; AY693182; AAT93201.1; -; Genomic_DNA.
EMBL; BK006949; DAA11227.1; -; Genomic_DNA.
PIR; S47923; S47923.
RefSeq; NP_015115.1; NM_001184023.1.
ProteinModelPortal; P38991; -.
SMR; P38991; -.
BioGrid; 35976; 499.
DIP; DIP-2771N; -.
IntAct; P38991; 11.
MINT; P38991; -.
STRING; 4932.YPL209C; -.
iPTMnet; P38991; -.
MaxQB; P38991; -.
PaxDb; P38991; -.
PRIDE; P38991; -.
EnsemblFungi; YPL209C; YPL209C; YPL209C.
GeneID; 855892; -.
KEGG; sce:YPL209C; -.
EuPathDB; FungiDB:YPL209C; -.
SGD; S000006130; IPL1.
GeneTree; ENSGT00910000144066; -.
HOGENOM; HOG000233016; -.
InParanoid; P38991; -.
KO; K08850; -.
OMA; QATSVPH; -.
OrthoDB; EOG092C0QJU; -.
BioCyc; YEAST:G3O-34100-MONOMER; -.
BRENDA; 2.7.11.1; 984.
Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
PRO; PR:P38991; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0032133; C:chromosome passenger complex; IDA:SGD.
GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005828; C:kinetochore microtubule; IDA:SGD.
GO; GO:0005819; C:spindle; IDA:SGD.
GO; GO:0005876; C:spindle microtubule; IDA:SGD.
GO; GO:0051233; C:spindle midzone; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; IDA:SGD.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:SGD.
GO; GO:0007059; P:chromosome segregation; IMP:SGD.
GO; GO:0045143; P:homologous chromosome segregation; IMP:SGD.
GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:SGD.
GO; GO:0044774; P:mitotic DNA integrity checkpoint; IGI:SGD.
GO; GO:0051228; P:mitotic spindle disassembly; IMP:SGD.
GO; GO:1901925; P:negative regulation of protein import into nucleus during spindle assembly checkpoint; IMP:SGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:SGD.
GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
GO; GO:0032465; P:regulation of cytokinesis; IMP:SGD.
GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:SGD.
GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:SGD.
InterPro; IPR030616; Aur.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24350; PTHR24350; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Centromere; Chromosome; Chromosome partition;
Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Kinetochore;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 367 Spindle assembly checkpoint kinase.
/FTId=PRO_0000086029.
DOMAIN 104 355 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 110 118 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 227 227 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 133 133 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 5 5 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:12408861}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000269|PubMed:12408861}.
MOD_RES 260 260 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:12408861}.
MUTAGEN 260 260 T->A: In IPL1-4; causes missegregation of
chromosomes at 37 degrees Celsius.
{ECO:0000269|PubMed:8007975}.
MUTAGEN 340 340 P->L: In IPL1-1; causes missegregation of
chromosomes at 37 degrees Celsius.
{ECO:0000269|PubMed:8007975}.
MUTAGEN 352 352 H->Y: In IPL1-2; causes missegregation of
chromosomes at 37 degrees Celsius.
{ECO:0000269|PubMed:8007975}.
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


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