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UniProtKB/Swiss-Prot entry P38991


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IPL1_YEAST
Primary accession number P38991
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Spindle assembly checkpoint kinase
Synonyms EC 2.7.11.1
Aurora kinase
Increase-in-ploidy protein 1
Gene name
Name: IPL1
OrderedLocusNames: YPL209C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF THR-260; PRO-340 AND HIS-352.
STRAIN=ATCC 204508 / S288c;
PubMed=8007975 [NCBI, ExPASy, EBI, Israel, Japan]
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 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
FUNCTION.
DOI=10.1016/S0092-8674(02)00633-5; PubMed=11853667 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
SUBCELLULAR LOCATION.
DOI=10.1083/jcb.145.7.1381; PubMed=10385519 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/S0092-8674(00)00034-9; PubMed=10975519 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1083/jcb.200105029; PubMed=11724818 [NCBI, ExPASy, EBI, Israel, Japan]
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, AND PHOSPHORYLATION AT SER-5; SER-76 AND THR-260.
DOI=10.1016/S0092-8674(02)00973-X; PubMed=12408861 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-38, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-76, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U07163; AAA20496.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73565; CAA97924.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY693182; AAT93201.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S47923; S47923.
RefSeq NP_015115.1; -.
3D structure databases
HSSP P31751; 1GZK. [HSSP ENTRY / PDB]
ModBase P38991.
Protein-protein interaction databases
DIP DIP:2771N; -.
IntAct P38991; 10.
Enzyme and pathway databases
BRENDA 2.7.11.1; 250.
Organism-specific databases
CYGD YPL209c; -.
SGD S000006130; IPL1.
Yeast-GFP YPL209C.
Gene expression databases
ArrayExpress P38991; -.
GermOnline YPL209C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0032133; Cellular component: chromosome passenger complex (inferred from direct assay from SGD).
GO:0000778; Cellular component: condensed nuclear chromosome kinetochore (inferred from direct assay from SGD).
GO:0005828; Cellular component: kinetochore microtubule (inferred from direct assay from SGD).
GO:0051233; Cellular component: spindle midzone (inferred from direct assay from SGD).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008608; Biological process: attachment of spindle microtubules to kinetochore (inferred from mutant phenotype from SGD).
GO:0045144; Biological process: meiotic sister chromatid segregation (inferred from mutant phenotype from SGD).
GO:0051228; Biological process: mitotic spindle disassembly (inferred from mutant phenotype from SGD).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from SGD).
GO:0032465; Biological process: regulation of cytokinesis (inferred from mutant phenotype from SGD).
GO:0031577; Biological process: spindle checkpoint (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl YPL209C; Saccharomyces cerevisiae. [Contig view]
GeneID 855892; -.
GenomeReviews U00094_GR; YPL209C.
KEGG sce:YPL209C; -.
NMPDR fig|4932.3.peg.6243; -.
Phylogenomic databases
HOGENOM P38991; -.
OMA P38991; FEASTYQ.
Other
NextBio 980568; -.
ProtoNet P38991.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell cycle; Chromosome partition; Complete proteome; Kinase; Kinetochore; Nucleotide-binding; Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   367  367     Spindle assembly checkpoint kinase. PRO_0000086029
DOMAIN   104   355  252     Protein kinase. 
NP_BIND   110   118  9     ATP (By similarity). 
ACT_SITE   227   227        Proton acceptor (By similarity). 
BINDING   133   133        ATP (By similarity). 
MOD_RES   5     5        Phosphoserine; by autocatalysis. 
MOD_RES   36    36        Phosphoserine. 
MOD_RES   38    38        Phosphoserine. 
MOD_RES   50    50        Phosphoserine. 
MOD_RES   76    76        Phosphoserine. 
MOD_RES   260   260        Phosphothreonine; by autocatalysis. 
MUTAGEN   260   260        T->A: In IPL1-4; causes missegregation of chromosomes at 37 degrees Celsius. 
MUTAGEN   340   340        P->L: In IPL1-1; causes missegregation of chromosomes at 37 degrees Celsius. 
MUTAGEN   352   352        H->Y: In IPL1-2; causes missegregation of chromosomes at 37 degrees Celsius. 
Sequence information
Length: 367 AA [This is the length of the unprocessed precursor] Molecular weight: 42946 Da [This is the MW of the unprocessed precursor] CRC64: 44E3EFDDE1CDB35E [This is a checksum on the sequence]
        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 

P38991 in FASTA format

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