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Protein

Spindle assembly checkpoint kinase

Gene

IPL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei133 – 1331ATPPROSITE-ProRule annotation
Active sitei227 – 2271Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi110 – 1189ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • attachment of spindle microtubules to kinetochore Source: SGD
  • chromosome segregation Source: SGD
  • homologous chromosome segregation Source: SGD
  • meiotic sister chromatid segregation Source: SGD
  • mitotic DNA integrity checkpoint Source: SGD
  • mitotic spindle disassembly Source: SGD
  • negative regulation of protein import into nucleus during spindle assembly checkpoint Source: SGD
  • peptidyl-serine phosphorylation Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of cytokinesis Source: SGD
  • regulation of mitotic cell cycle spindle assembly checkpoint Source: SGD
  • regulation of mitotic spindle assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Chromosome partition

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34100-MONOMER.
BRENDAi2.7.11.1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Spindle assembly checkpoint kinase (EC:2.7.11.1)
Alternative name(s):
Aurora kinase
Increase-in-ploidy protein 1
Gene namesi
Name:IPL1
Ordered Locus Names:YPL209C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL209C.
SGDiS000006130. IPL1.

Subcellular locationi

GO - Cellular componenti

  • chromosome passenger complex Source: SGD
  • condensed nuclear chromosome kinetochore Source: SGD
  • cytoplasm Source: UniProtKB-KW
  • kinetochore microtubule Source: SGD
  • spindle Source: SGD
  • spindle microtubule Source: SGD
  • spindle midzone Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi260 – 2601T → A in IPL1-4; causes missegregation of chromosomes at 37 degrees Celsius. 1 Publication
Mutagenesisi340 – 3401P → L in IPL1-1; causes missegregation of chromosomes at 37 degrees Celsius. 1 Publication
Mutagenesisi352 – 3521H → Y in IPL1-2; causes missegregation of chromosomes at 37 degrees Celsius. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Spindle assembly checkpoint kinasePRO_0000086029Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine; by autocatalysis1 Publication
Modified residuei76 – 761Phosphoserine1 Publication
Modified residuei260 – 2601Phosphothreonine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38991.

PTM databases

iPTMnetiP38991.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
BIR1P471344EBI-9319,EBI-3648
HIST1H3DP684312EBI-9319,EBI-79722From a different organism.
SLI15P3828310EBI-9319,EBI-20842

Protein-protein interaction databases

BioGridi35976. 168 interactions.
DIPiDIP-2771N.
IntActiP38991. 11 interactions.
MINTiMINT-1706398.

Structurei

3D structure databases

ProteinModelPortaliP38991.
SMRiP38991. Positions 58-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 355252Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00770000120530.
HOGENOMiHOG000233016.
InParanoidiP38991.
KOiK08850.
OMAiQRPMLRE.
OrthoDBiEOG793BK1.

Family and domain databases

InterProiIPR030616. Aur.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24350. PTHR24350. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38991-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRNSLVNIK LNANSPSKKT TTRPNTSRIN KPWRISHSPQ QRNPNSKIPS
60 70 80 90 100
PVREKLNRLP VNNKKFLDME SSKIPSPIRK ATSSKMIHEN KKLPKFKSLS
110 120 130 140 150
LDDFELGKKL GKGKFGKVYC VRHRSTGYIC ALKVMEKEEI IKYNLQKQFR
160 170 180 190 200
REVEIQTSLN HPNLTKSYGY FHDEKRVYLL MEYLVNGEMY KLLRLHGPFN
210 220 230 240 250
DILASDYIYQ IANALDYMHK KNIIHRDIKP ENILIGFNNV IKLTDFGWSI
260 270 280 290 300
INPPENRRKT VCGTIDYLSP EMVESREYDH TIDAWALGVL AFELLTGAPP
310 320 330 340 350
FEEEMKDTTY KRIAALDIKM PSNISQDAQD LILKLLKYDP KDRMRLGDVK
360
MHPWILRNKP FWENKRL
Length:367
Mass (Da):42,946
Last modified:February 1, 1995 - v1
Checksum:i44E3EFDDE1CDB35E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07163 Genomic DNA. Translation: AAA20496.1.
Z73565 Genomic DNA. Translation: CAA97924.1.
AY693182 Genomic DNA. Translation: AAT93201.1.
BK006949 Genomic DNA. Translation: DAA11227.1.
PIRiS47923.
RefSeqiNP_015115.1. NM_001184023.1.

Genome annotation databases

EnsemblFungiiYPL209C; YPL209C; YPL209C.
GeneIDi855892.
KEGGisce:YPL209C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07163 Genomic DNA. Translation: AAA20496.1.
Z73565 Genomic DNA. Translation: CAA97924.1.
AY693182 Genomic DNA. Translation: AAT93201.1.
BK006949 Genomic DNA. Translation: DAA11227.1.
PIRiS47923.
RefSeqiNP_015115.1. NM_001184023.1.

3D structure databases

ProteinModelPortaliP38991.
SMRiP38991. Positions 58-366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35976. 168 interactions.
DIPiDIP-2771N.
IntActiP38991. 11 interactions.
MINTiMINT-1706398.

PTM databases

iPTMnetiP38991.

Proteomic databases

MaxQBiP38991.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL209C; YPL209C; YPL209C.
GeneIDi855892.
KEGGisce:YPL209C.

Organism-specific databases

EuPathDBiFungiDB:YPL209C.
SGDiS000006130. IPL1.

Phylogenomic databases

GeneTreeiENSGT00770000120530.
HOGENOMiHOG000233016.
InParanoidiP38991.
KOiK08850.
OMAiQRPMLRE.
OrthoDBiEOG793BK1.

Enzyme and pathway databases

BioCyciYEAST:G3O-34100-MONOMER.
BRENDAi2.7.11.1. 984.

Miscellaneous databases

PROiP38991.

Family and domain databases

InterProiIPR030616. Aur.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24350. PTHR24350. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. 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.

Entry informationi

Entry nameiIPL1_YEAST
AccessioniPrimary (citable) accession number: P38991
Secondary accession number(s): D6W3G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 149 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.