P38991 (IPL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spindle assembly checkpoint kinase
EC=2.7.11.1

Alternative name(s):
Aurora kinase
Increase-in-ploidy protein 1

Gene names

Name:	IPL1
Ordered Locus Names:	YPL209C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5 Ref.7 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
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. Ref.6 Ref.8
Miscellaneous	Present with 149 molecules/cell in log phase SD medium. Ref.10
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Chromosome partition
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	attachment of spindle microtubules to kinetochore Inferred from mutant phenotype. Source: SGD homologous chromosome segregation Inferred from mutant phenotype. Source: SGD meiotic sister chromatid segregation Inferred from mutant phenotype. Source: SGD mitotic cell cycle G2/M transition decatenation checkpoint Inferred from genetic interaction. Source: SGD mitotic spindle disassembly Inferred from mutant phenotype. Source: SGD regulation of cytokinesis Inferred from mutant phenotype. Source: SGD spindle checkpoint Inferred from mutant phenotype. Source: SGD
Cellular component	chromosome passenger complex Inferred from direct assay. Source: SGD condensed nuclear chromosome kinetochore Inferred from direct assay. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW kinetochore microtubule Inferred from direct assay Ref.8. Source: SGD spindle midzone Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.9. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HIST1H3A	P68431	2	EBI-9319,EBI-79722	From a different organism.
SLI15	P38283	3	EBI-9319,EBI-20842

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 367	367	Spindle assembly checkpoint kinase		PRO_0000086029
Regions
	Domain	104 – 355	252	Protein kinase
	Nucleotide binding	110 – 118	9	ATP By similarity
Sites
	Active site	227	1	Proton acceptor By similarity
	Binding site	133	1	ATP By similarity
Amino acid modifications
	Modified residue	5	1	Phosphoserine; by autocatalysis Ref.9
	Modified residue	36	1	Phosphoserine Ref.11
	Modified residue	38	1	Phosphoserine Ref.11 Ref.12
	Modified residue	50	1	Phosphoserine Ref.13
	Modified residue	76	1	Phosphoserine Ref.9 Ref.13
	Modified residue	260	1	Phosphothreonine; by autocatalysis Ref.9
Experimental info
	Mutagenesis	260	1	T → A in IPL1-4; causes missegregation of chromosomes at 37 degrees Celsius. Ref.1
	Mutagenesis	340	1	P → L in IPL1-1; causes missegregation of chromosomes at 37 degrees Celsius. Ref.1
	Mutagenesis	352	1	H → Y in IPL1-2; causes missegregation of chromosomes at 37 degrees Celsius. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38991 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 44E3EFDDE1CDB35E	FASTA	367	42,946
	10 20 30 40 50 60 MQRNSLVNIK LNANSPSKKT TTRPNTSRIN KPWRISHSPQ QRNPNSKIPS PVREKLNRLP 70 80 90 100 110 120 VNNKKFLDME SSKIPSPIRK ATSSKMIHEN KKLPKFKSLS LDDFELGKKL GKGKFGKVYC 130 140 150 160 170 180 VRHRSTGYIC ALKVMEKEEI IKYNLQKQFR REVEIQTSLN HPNLTKSYGY FHDEKRVYLL 190 200 210 220 230 240 MEYLVNGEMY KLLRLHGPFN DILASDYIYQ IANALDYMHK KNIIHRDIKP ENILIGFNNV 250 260 270 280 290 300 IKLTDFGWSI INPPENRRKT VCGTIDYLSP EMVESREYDH TIDAWALGVL AFELLTGAPP 310 320 330 340 350 360 FEEEMKDTTY KRIAALDIKM PSNISQDAQD LILKLLKYDP KDRMRLGDVK MHPWILRNKP FWENKRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Type 1 protein phosphatase acts in opposition to Ipl1 protein kinase in regulating yeast chromosome segregation." Francisco L., Wang W., Chan C.S.M. Mol. Cell. Biol. 14:4731-4740(1994) [PubMed: 8007975] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF THR-260; PRO-340 AND HIS-352. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." 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. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections." Tanaka T.U., Rachidi N., Janke C., Pereira G., Galova M., Schiebel E., Stark M.J.R., Nasmyth K. Cell 108:317-329(2002) [PubMed: 11853667] [Abstract] Cited for: FUNCTION.
[6]	"Sli15 associates with the ipl1 protein kinase to promote proper chromosome segregation in Saccharomyces cerevisiae." Kim J.-H., Kang J.-S., Chan C.S.M. J. Cell Biol. 145:1381-1394(1999) [PubMed: 10385519] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes." 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. Cell 102:279-291(2000) [PubMed: 10975519] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[8]	"Functional cooperation of Dam1, Ipl1, and the inner centromere protein (INCENP)-related protein Sli15 during chromosome segregation." Kang J.-S., Cheeseman I.M., Kallstrom G., Velmurugan S., Barnes G., Chan C.S.M. J. Cell Biol. 155:763-774(2001) [PubMed: 11724818] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p." 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. Cell 111:163-172(2002) [PubMed: 12408861] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-5; SER-76 AND THR-260.
[10]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." 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. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-38, MASS SPECTROMETRY.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-76, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U07163 Genomic DNA. Translation: AAA20496.1. Z73565 Genomic DNA. Translation: CAA97924.1. AY693182 Genomic DNA. Translation: AAT93201.1. BK006949 Genomic DNA. Translation: DAA11227.1.
PIR	S47923.
RefSeq	NP_015115.1. NM_001184023.1.
3D structure databases
ProteinModelPortal	P38991.
SMR	P38991. Positions 98-365.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2771N.
IntAct	P38991. 11 interactions.
MINT	MINT-1706398.
STRING	P38991.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPL209C; YPL209C; YPL209C.
GeneID	855892.
KEGG	sce:YPL209C.
NMPDR	fig|4932.3.peg.6243.
Organism-specific databases
CYGD	YPL209c.
SGD	S000006130. IPL1.
Phylogenomic databases
eggNOG	fuNOG07092.
GeneTree	EFGT00070000008711.
HOGENOM	HBG755340.
OMA	RSKENCI.
OrthoDB	EOG4T7CC4.
Enzyme and pathway databases
BRENDA	2.7.11.1. 984.
Gene expression databases
ArrayExpress	P38991.
Genevestigator	P38991.
GermOnline	YPL209C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08850.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980568.

Entry information

Entry name

IPL1_YEAST

Accession

Primary (citable) accession number: P38991
Secondary accession number(s): D6W3G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program