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P38991 (IPL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Phosphorylates RGD1 in vitro. Ref.6 Ref.8 Ref.9 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Nucleus. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore. Note: Associates with the mitotic spindle and on elongated and disassembling spindles. Also associated with the kinetochore. Ref.5 Ref.7

Miscellaneous

Present with 149 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Chromosome partition
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processattachment of spindle microtubules to kinetochore

Inferred from mutant phenotype PubMed 10072382. Source: SGD

chromosome segregation

Inferred from mutant phenotype PubMed 8293973. Source: SGD

homologous chromosome segregation

Inferred from mutant phenotype PubMed 17289568. Source: SGD

meiotic sister chromatid segregation

Inferred from mutant phenotype PubMed 17289568PubMed 17371833. Source: SGD

mitotic DNA integrity checkpoint

Inferred from genetic interaction PubMed 16651657. Source: SGD

mitotic spindle disassembly

Inferred from mutant phenotype PubMed 12566427. Source: SGD

negative regulation of protein import into nucleus during spindle assembly checkpoint

Inferred from mutant phenotype PubMed 23177738. Source: SGD

positive regulation of spindle checkpoint

Inferred from mutant phenotype PubMed 16327780. Source: SGD

protein phosphorylation

Inferred from direct assay PubMed 17504936PubMed 23142046. Source: SGD

regulation of cytokinesis

Inferred from mutant phenotype PubMed 16615892. Source: SGD

   Cellular_componentchromosome passenger complex

Inferred from direct assay PubMed 19158380. Source: SGD

condensed nuclear chromosome kinetochore

Inferred from direct assay PubMed 11511347PubMed 12566427. Source: SGD

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

kinetochore microtubule

Inferred from direct assay Ref.7. Source: SGD

spindle

Inferred from direct assay PubMed 12566427. Source: SGD

spindle microtubule

Inferred from direct assay PubMed 11511347Ref.7. Source: SGD

spindle midzone

Inferred from direct assay PubMed 12566427. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Inferred from direct assay PubMed 10072382PubMed 16143104PubMed 23142046. Source: SGD

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIST1H3DP684312EBI-9319,EBI-79722From a different organism.
SLI15P382833EBI-9319,EBI-20842

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Spindle assembly checkpoint kinase
PRO_0000086029

Regions

Domain104 – 355252Protein kinase
Nucleotide binding110 – 1189ATP By similarity

Sites

Active site2271Proton acceptor By similarity
Binding site1331ATP By similarity

Amino acid modifications

Modified residue51Phosphoserine; by autocatalysis Ref.9
Modified residue761Phosphoserine Ref.9
Modified residue2601Phosphothreonine; by autocatalysis Ref.9

Experimental info

Mutagenesis2601T → A in IPL1-4; causes missegregation of chromosomes at 37 degrees Celsius. Ref.1
Mutagenesis3401P → L in IPL1-1; causes missegregation of chromosomes at 37 degrees Celsius. Ref.1
Mutagenesis3521H → Y in IPL1-2; causes missegregation of chromosomes at 37 degrees Celsius. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P38991 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 44E3EFDDE1CDB35E

FASTA36742,946
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[7]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"The Saccharomyces cerevisiae RhoGAP Rgd1 is phosphorylated by the Aurora B like kinase Ipl1."
Vieillemard A., Prouzet-Mauleon V., Hugues M., Lefebvre F., Mitteau R., Claverol S., Bonneu M., Crouzet M., Doignon F., Thoraval D.
Biochem. Biophys. Res. Commun. 433:1-5(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+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.
PIRS47923.
RefSeqNP_015115.1. NM_001184023.1.

3D structure databases

ProteinModelPortalP38991.
SMRP38991. Positions 58-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35976. 163 interactions.
DIPDIP-2771N.
IntActP38991. 10 interactions.
MINTMINT-1706398.
STRING4932.YPL209C.

Proteomic databases

PaxDbP38991.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL209C; YPL209C; YPL209C.
GeneID855892.
KEGGsce:YPL209C.

Organism-specific databases

CYGDYPL209c.
SGDS000006130. IPL1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074590.
HOGENOMHOG000233016.
KOK08850.
OMACISGPVK.
OrthoDBEOG793BK1.

Enzyme and pathway databases

BioCycYEAST:G3O-34100-MONOMER.
BRENDA2.7.11.1. 984.

Gene expression databases

GenevestigatorP38991.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980568.
PROP38991.

Entry information

Entry nameIPL1_YEAST
AccessionPrimary (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: April 16, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families