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P54199

- MPS1_YEAST

UniProt

P54199 - MPS1_YEAST

Protein

Serine/threonine-protein kinase MPS1

Gene

MPS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. Implicated in spindle pole body (SPD) duplication. Dual specificity kinase that can phosphorylate serine, threonine and tyrosine residues. Phosphorylates the SPC29 and SPC110 spindle pole body components.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei468 – 4681ATPPROSITE-ProRule annotation
    Active sitei563 – 5631Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi446 – 4549ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein serine/threonine/tyrosine kinase activity Source: SGD
    4. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. mitotic spindle assembly checkpoint Source: SGD
    2. protein phosphorylation Source: SGD
    3. regulation of attachment of spindle microtubules to kinetochore Source: SGD
    4. sister chromatid biorientation Source: SGD
    5. spindle assembly Source: SGD
    6. spindle pole body duplication Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29454-MONOMER.
    BRENDAi2.7.12.1. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase MPS1 (EC:2.7.12.2)
    Alternative name(s):
    Monopolar spindle protein 1
    Regulatory cell proliferation kinase 1
    Gene namesi
    Name:MPS1
    Synonyms:RPK1
    Ordered Locus Names:YDL028C
    ORF Names:D2785
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL028c.
    SGDiS000002186. MPS1.

    Subcellular locationi

    GO - Cellular componenti

    1. condensed nuclear chromosome kinetochore Source: SGD
    2. spindle pole body Source: SGD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi580 – 5801D → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 764764Serine/threonine-protein kinase MPS1PRO_0000086391Add
    BLAST

    Post-translational modificationi

    Autophosphorylated.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP54199.
    PaxDbiP54199.

    Expressioni

    Gene expression databases

    GenevestigatoriP54199.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BEM1P293663EBI-11224,EBI-3508
    SLA1P327902EBI-11224,EBI-17313
    TID3P404604EBI-11224,EBI-25247

    Protein-protein interaction databases

    BioGridi32028. 159 interactions.
    DIPiDIP-5897N.
    IntActiP54199. 37 interactions.
    MINTiMINT-597563.
    STRINGi4932.YDL028C.

    Structurei

    3D structure databases

    ProteinModelPortaliP54199.
    SMRiP54199. Positions 405-734.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini440 – 720281Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi273 – 28210Poly-Ser
    Compositional biasi309 – 3157Poly-Ser

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00620000087848.
    HOGENOMiHOG000248654.
    KOiK08866.
    OMAiCVKVVHD.
    OrthoDBiEOG71GB3B.

    Family and domain databases

    InterProiIPR011009. 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]
    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.

    P54199-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNSFHDYV DLKSRTNTRQ FSDDEEFTTP PKLSNFGSAL LSHTEKTSAS    50
    EILSSHNNDK IANRLEEMDR SSSRSHPPPS MGNLTSGHTS TSSHSTLFGR 100
    YLRNNHQTSM TTMNTSDIEI NVGNSLDKSF ERIRNLRQNM KEDITAKYAE 150
    RRSKRFLISN RTTKLGPAKR AMTLTNIFDE DVPNSPNQPI NARETVELPL 200
    EDSHQTNFKE TKRNTDYDSI DFGDLNPIQY IKKHNLPTSD LPLISQIYFD 250
    KQREENRQAA LRKHSSRELL YKSRSSSSSL SSNNLLANKD NSITSNNGSQ 300
    PRRKVSTGSS SSKSSIEIRR ALKENIDTSN NSNFNSPIHK IYKGISRNKD 350
    SDSEKREVLR NISINANHAD NLLQQENKRL KRSLDDAITN ENINSKNLEV 400
    FYHRPAPKPP VTKKVEIVEP AKSASLSNNR NIITVNDSQY EKIELLGRGG 450
    SSRVYKVKGS GNRVYALKRV SFDAFDDSSI DGFKGEIELL EKLKDQKRVI 500
    QLLDYEMGDG LLYLIMECGD HDLSQILNQR SGMPLDFNFV RFYTKEMLLC 550
    IKVVHDAGIV HSDLKPANFV LVKGILKIID FGIANAVPEH TVNIYRETQI 600
    GTPNYMAPEA LVAMNYTQNS ENQHEGNKWK VGRPSDMWSC GCIIYQMIYG 650
    KPPYGSFQGQ NRLLAIMNPD VKIPFPEHTS NNEKIPKSAI ELMKACLYRN 700
    PDKRWTVDKV LSSTFLQPFM ISGSIMEDLI RNAVRYGSEK PHISQDDLND 750
    VVDTVLRKFA DYKI 764
    Length:764
    Mass (Da):86,772
    Last modified:July 27, 2011 - v2
    Checksum:i5A404F4F83A9D548
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461A → S in AAA88731. (PubMed:8028580)Curated
    Sequence conflicti211 – 2133TKR → RRE in CAA96461. (PubMed:9046088)Curated
    Sequence conflicti211 – 2133TKR → RRE in CAA98587. (PubMed:9169867)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08909 Genomic DNA. Translation: AAA88731.1.
    Z71781 Genomic DNA. Translation: CAA96461.1.
    Z74076 Genomic DNA. Translation: CAA98587.1.
    BK006938 Genomic DNA. Translation: DAA11824.2.
    PIRiS67561.
    RefSeqiNP_010256.2. NM_001180087.2.

    Genome annotation databases

    EnsemblFungiiYDL028C; YDL028C; YDL028C.
    GeneIDi851533.
    KEGGisce:YDL028C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08909 Genomic DNA. Translation: AAA88731.1 .
    Z71781 Genomic DNA. Translation: CAA96461.1 .
    Z74076 Genomic DNA. Translation: CAA98587.1 .
    BK006938 Genomic DNA. Translation: DAA11824.2 .
    PIRi S67561.
    RefSeqi NP_010256.2. NM_001180087.2.

    3D structure databases

    ProteinModelPortali P54199.
    SMRi P54199. Positions 405-734.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32028. 159 interactions.
    DIPi DIP-5897N.
    IntActi P54199. 37 interactions.
    MINTi MINT-597563.
    STRINGi 4932.YDL028C.

    Proteomic databases

    MaxQBi P54199.
    PaxDbi P54199.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL028C ; YDL028C ; YDL028C .
    GeneIDi 851533.
    KEGGi sce:YDL028C.

    Organism-specific databases

    CYGDi YDL028c.
    SGDi S000002186. MPS1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00620000087848.
    HOGENOMi HOG000248654.
    KOi K08866.
    OMAi CVKVVHD.
    OrthoDBi EOG71GB3B.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29454-MONOMER.
    BRENDAi 2.7.12.1. 984.

    Miscellaneous databases

    NextBioi 968929.
    PROi P54199.

    Gene expression databases

    Genevestigatori P54199.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RPK1, an essential yeast protein kinase involved in the regulation of the onset of mitosis, shows homology to mammalian dual-specificity kinases."
      Poch O., Schwob E., de Fraipont F., Camasses A., Bordonne R., Martin R.P.
      Mol. Gen. Genet. 243:641-653(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 28383 / FL100 / VTT C-80102.
    2. "The sequence of a 36.7 kb segment on the left arm of chromosome IV from Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1 and 11 new ORFs."
      Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.
      Yeast 13:65-71(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 211-213.
      Strain: ATCC 204508 / S288c.
    5. "Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase."
      Lauze E., Stoelcker B., Luca F.C., Weiss E., Schutz A.R., Winey M.
      EMBO J. 14:1655-1663(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-580.
    6. Cited for: FUNCTION.
    7. "Budding yeast centrosome duplication requires stabilization of Spc29 via Mps1-mediated phosphorylation."
      Holinger E.P., Old W.M., Giddings T.H. Jr., Wong C., Yates J.R. III, Winey M.
      J. Biol. Chem. 284:12949-12955(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMPS1_YEAST
    AccessioniPrimary (citable) accession number: P54199
    Secondary accession number(s): D6VRW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

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

    External Data

    Dasty 3