MPS1_YEAST
ID MPS1_YEAST Reviewed; 764 AA.
AC P54199; D6VRW4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Serine/threonine-protein kinase MPS1;
DE EC=2.7.12.2;
DE AltName: Full=Monopolar spindle protein 1;
DE AltName: Full=Regulatory cell proliferation kinase 1;
GN Name=MPS1; Synonyms=RPK1; OrderedLocusNames=YDL028C; ORFNames=D2785;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=8028580; DOI=10.1007/bf00279573;
RA Poch O., Schwob E., de Fraipont F., Camasses A., Bordonne R., Martin R.P.;
RT "RPK1, an essential yeast protein kinase involved in the regulation of the
RT onset of mitosis, shows homology to mammalian dual-specificity kinases.";
RL Mol. Gen. Genet. 243:641-653(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046088;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<65::aid-yea50>3.0.co;2-t;
RA Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.;
RT "The sequence of a 36.7 kb segment on the left arm of chromosome IV from
RT Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames
RT (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1
RT and 11 new ORFs.";
RL Yeast 13:65-71(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 211-213.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP CHARACTERIZATION, AND MUTAGENESIS OF ASP-580.
RX PubMed=7737118; DOI=10.1002/j.1460-2075.1995.tb07154.x;
RA Lauze E., Stoelcker B., Luca F.C., Weiss E., Schutz A.R., Winey M.;
RT "Yeast spindle pole body duplication gene MPS1 encodes an essential dual
RT specificity protein kinase.";
RL EMBO J. 14:1655-1663(1995).
RN [6]
RP FUNCTION.
RX PubMed=11278681; DOI=10.1074/jbc.m010461200;
RA Friedman D.B., Kern J.W., Huneycutt B.J., Vinh D.B., Crawford D.K.,
RA Steiner E., Scheiltz D., Yates J. III, Resing K.A., Ahn N.G., Winey M.,
RA Davis T.N.;
RT "Yeast Mps1p phosphorylates the spindle pole component Spc110p in the N-
RT terminal domain.";
RL J. Biol. Chem. 276:17958-17967(2001).
RN [7]
RP FUNCTION.
RX PubMed=19269975; DOI=10.1074/jbc.m900088200;
RA Holinger E.P., Old W.M., Giddings T.H. Jr., Wong C., Yates J.R. III,
RA Winey M.;
RT "Budding yeast centrosome duplication requires stabilization of Spc29 via
RT Mps1-mediated phosphorylation.";
RL J. Biol. Chem. 284:12949-12955(2009).
CC -!- FUNCTION: Involved in the regulation of the onset of mitosis. Involved
CC in a pathway that coordinates cell proliferation and differentiation.
CC Implicated in spindle pole body (SPD) duplication. Dual specificity
CC kinase that can phosphorylate serine, threonine and tyrosine residues.
CC Phosphorylates the SPC29 and SPC110 spindle pole body components.
CC {ECO:0000269|PubMed:11278681, ECO:0000269|PubMed:19269975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- INTERACTION:
CC P54199; P29366: BEM1; NbExp=3; IntAct=EBI-11224, EBI-3508;
CC P54199; P40460: NDC80; NbExp=4; IntAct=EBI-11224, EBI-25247;
CC P54199; P32790: SLA1; NbExp=2; IntAct=EBI-11224, EBI-17313;
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; L08909; AAA88731.1; -; Genomic_DNA.
DR EMBL; Z71781; CAA96461.1; -; Genomic_DNA.
DR EMBL; Z74076; CAA98587.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11824.2; -; Genomic_DNA.
DR PIR; S67561; S67561.
DR RefSeq; NP_010256.2; NM_001180087.2.
DR AlphaFoldDB; P54199; -.
DR SMR; P54199; -.
DR BioGRID; 32028; 628.
DR DIP; DIP-5897N; -.
DR IntAct; P54199; 38.
DR MINT; P54199; -.
DR STRING; 4932.YDL028C; -.
DR iPTMnet; P54199; -.
DR MaxQB; P54199; -.
DR PaxDb; P54199; -.
DR PRIDE; P54199; -.
DR EnsemblFungi; YDL028C_mRNA; YDL028C; YDL028C.
DR GeneID; 851533; -.
DR KEGG; sce:YDL028C; -.
DR SGD; S000002186; MPS1.
DR VEuPathDB; FungiDB:YDL028C; -.
DR eggNOG; KOG0596; Eukaryota.
DR GeneTree; ENSGT00950000182984; -.
DR HOGENOM; CLU_019372_0_0_1; -.
DR InParanoid; P54199; -.
DR OMA; DLNPYQY; -.
DR BioCyc; YEAST:G3O-29454-MON; -.
DR BRENDA; 2.7.12.1; 984.
DR PRO; PR:P54199; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P54199; protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043515; F:kinetochore binding; IDA:SGD.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:SGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051304; P:chromosome separation; IEA:InterPro.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034501; P:protein localization to kinetochore; IGI:SGD.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:SGD.
DR GO; GO:0031134; P:sister chromatid biorientation; IMP:SGD.
DR GO; GO:0051225; P:spindle assembly; IMP:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR016242; Mps1.
DR InterPro; IPR027084; Prot_kin_Mps1_fam.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22974:SF21; PTHR22974:SF21; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000611; Ser/Thr_PK_MPS1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..764
FT /note="Serine/threonine-protein kinase MPS1"
FT /id="PRO_0000086391"
FT DOMAIN 440..720
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 66..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 563
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 446..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 580
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7737118"
FT CONFLICT 146
FT /note="A -> S (in Ref. 1; AAA88731)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..213
FT /note="TKR -> RRE (in Ref. 2; CAA96461 and 3; CAA98587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 764 AA; 86772 MW; 5A404F4F83A9D548 CRC64;
MSTNSFHDYV DLKSRTNTRQ FSDDEEFTTP PKLSNFGSAL LSHTEKTSAS EILSSHNNDK
IANRLEEMDR SSSRSHPPPS MGNLTSGHTS TSSHSTLFGR YLRNNHQTSM TTMNTSDIEI
NVGNSLDKSF ERIRNLRQNM KEDITAKYAE RRSKRFLISN RTTKLGPAKR AMTLTNIFDE
DVPNSPNQPI NARETVELPL EDSHQTNFKE TKRNTDYDSI DFGDLNPIQY IKKHNLPTSD
LPLISQIYFD KQREENRQAA LRKHSSRELL YKSRSSSSSL SSNNLLANKD NSITSNNGSQ
PRRKVSTGSS SSKSSIEIRR ALKENIDTSN NSNFNSPIHK IYKGISRNKD SDSEKREVLR
NISINANHAD NLLQQENKRL KRSLDDAITN ENINSKNLEV FYHRPAPKPP VTKKVEIVEP
AKSASLSNNR NIITVNDSQY EKIELLGRGG SSRVYKVKGS GNRVYALKRV SFDAFDDSSI
DGFKGEIELL EKLKDQKRVI QLLDYEMGDG LLYLIMECGD HDLSQILNQR SGMPLDFNFV
RFYTKEMLLC IKVVHDAGIV HSDLKPANFV LVKGILKIID FGIANAVPEH TVNIYRETQI
GTPNYMAPEA LVAMNYTQNS ENQHEGNKWK VGRPSDMWSC GCIIYQMIYG KPPYGSFQGQ
NRLLAIMNPD VKIPFPEHTS NNEKIPKSAI ELMKACLYRN PDKRWTVDKV LSSTFLQPFM
ISGSIMEDLI RNAVRYGSEK PHISQDDLND VVDTVLRKFA DYKI
