Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54199

- MPS1_YEAST

UniProt

P54199 - MPS1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 serine/threonine/tyrosine kinase activity Source: SGD
  3. 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
Complete GO annotation...

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
Complete GO annotation...

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

Structurei

3D structure databases

ProteinModelPortaliP54199.
SMRiP54199. Positions 433-763.
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.
InParanoidiP54199.
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.
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

        10         20         30         40         50
MSTNSFHDYV DLKSRTNTRQ FSDDEEFTTP PKLSNFGSAL LSHTEKTSAS
60 70 80 90 100
EILSSHNNDK IANRLEEMDR SSSRSHPPPS MGNLTSGHTS TSSHSTLFGR
110 120 130 140 150
YLRNNHQTSM TTMNTSDIEI NVGNSLDKSF ERIRNLRQNM KEDITAKYAE
160 170 180 190 200
RRSKRFLISN RTTKLGPAKR AMTLTNIFDE DVPNSPNQPI NARETVELPL
210 220 230 240 250
EDSHQTNFKE TKRNTDYDSI DFGDLNPIQY IKKHNLPTSD LPLISQIYFD
260 270 280 290 300
KQREENRQAA LRKHSSRELL YKSRSSSSSL SSNNLLANKD NSITSNNGSQ
310 320 330 340 350
PRRKVSTGSS SSKSSIEIRR ALKENIDTSN NSNFNSPIHK IYKGISRNKD
360 370 380 390 400
SDSEKREVLR NISINANHAD NLLQQENKRL KRSLDDAITN ENINSKNLEV
410 420 430 440 450
FYHRPAPKPP VTKKVEIVEP AKSASLSNNR NIITVNDSQY EKIELLGRGG
460 470 480 490 500
SSRVYKVKGS GNRVYALKRV SFDAFDDSSI DGFKGEIELL EKLKDQKRVI
510 520 530 540 550
QLLDYEMGDG LLYLIMECGD HDLSQILNQR SGMPLDFNFV RFYTKEMLLC
560 570 580 590 600
IKVVHDAGIV HSDLKPANFV LVKGILKIID FGIANAVPEH TVNIYRETQI
610 620 630 640 650
GTPNYMAPEA LVAMNYTQNS ENQHEGNKWK VGRPSDMWSC GCIIYQMIYG
660 670 680 690 700
KPPYGSFQGQ NRLLAIMNPD VKIPFPEHTS NNEKIPKSAI ELMKACLYRN
710 720 730 740 750
PDKRWTVDKV LSSTFLQPFM ISGSIMEDLI RNAVRYGSEK PHISQDDLND
760
VVDTVLRKFA DYKI
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 433-763.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32028. 160 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.
InParanoidi P54199.
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.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 129 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