MPS2_YEAST
ID MPS2_YEAST Reviewed; 387 AA.
AC P53159; D6VU69;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Monopolar spindle protein 2;
GN Name=MPS2; Synonyms=MMC1; OrderedLocusNames=YGL075C;
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 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
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 [4]
RP FUNCTION.
RX PubMed=1869587; DOI=10.1083/jcb.114.4.745;
RA Winey M., Goetsch L., Baum P., Byers B.;
RT "MPS1 and MPS2: novel yeast genes defining distinct steps of spindle pole
RT body duplication.";
RL J. Cell Biol. 114:745-754(1991).
RN [5]
RP FUNCTION.
RX PubMed=9060463; DOI=10.1083/jcb.136.5.969;
RA Schutz A.R., Giddings T.H. Jr., Steiner E., Winey M.;
RT "The yeast CDC37 gene interacts with MPS1 and is required for proper
RT execution of spindle pole body duplication.";
RL J. Cell Biol. 136:969-982(1997).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10397772; DOI=10.1091/mbc.10.7.2393;
RA Munoz-Centeno M.C., McBratney S., Monterrosa A., Byers B., Mann C.,
RA Winey M.;
RT "Saccharomyces cerevisiae MPS2 encodes a membrane protein localized at the
RT spindle pole body and the nuclear envelope.";
RL Mol. Biol. Cell 10:2393-2406(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH BBP1.
RX PubMed=10654940; DOI=10.1093/emboj/19.3.421;
RA Schramm C., Elliott S., Shevchenko A., Schiebel E.;
RT "The Bbp1p-Mps2p complex connects the SPB to the nuclear envelope and is
RT essential for SPB duplication.";
RL EMBO J. 19:421-433(2000).
RN [8]
RP FUNCTION.
RX PubMed=12399372; DOI=10.1093/genetics/162.2.567;
RA McBratney S., Winey M.;
RT "Mutant membrane protein of the budding yeast spindle pole body is targeted
RT to the endoplasmic reticulum degradation pathway.";
RL Genetics 162:567-578(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH SPC24.
RX PubMed=11952896; DOI=10.1046/j.1365-2958.2002.02844.x;
RA Le Masson I., Saveanu C., Chevalier A., Namane A., Gobin R.,
RA Fromont-Racine M., Jacquier A., Mann C.;
RT "Spc24 interacts with Mps2 and is required for chromosome segregation, but
RT is not implicated in spindle pole body duplication.";
RL Mol. Microbiol. 43:1431-1443(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH MPS3.
RX PubMed=16923827; DOI=10.1083/jcb.200601062;
RA Jaspersen S.L., Martin A.E., Glazko G., Giddings T.H. Jr., Morgan G.,
RA Mushegian A., Winey M.;
RT "The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the
RT spindle pole body with the nuclear envelope.";
RL J. Cell Biol. 174:665-675(2006).
RN [11]
RP FUNCTION, AND INTERACTION WITH NBP1.
RX PubMed=16436507; DOI=10.1091/mbc.e05-07-0668;
RA Araki Y., Lau C.K., Maekawa H., Jaspersen S.L., Giddings T.H. Jr.,
RA Schiebel E., Winey M.;
RT "The Saccharomyces cerevisiae spindle pole body (SPB) component Nbp1p is
RT required for SPB membrane insertion and interacts with the integral
RT membrane proteins Ndc1p and Mps2p.";
RL Mol. Biol. Cell 17:1959-1970(2006).
CC -!- FUNCTION: Component of the spindle pole body (SPB) required for
CC insertion of the nascent SPB into the nuclear envelope and for the
CC proper execution of spindle pole body (SPB) duplication.
CC {ECO:0000269|PubMed:10397772, ECO:0000269|PubMed:10654940,
CC ECO:0000269|PubMed:11952896, ECO:0000269|PubMed:12399372,
CC ECO:0000269|PubMed:16436507, ECO:0000269|PubMed:16923827,
CC ECO:0000269|PubMed:1869587, ECO:0000269|PubMed:9060463}.
CC -!- SUBUNIT: Interacts with BBP1, MPS3, and SPC24.
CC {ECO:0000269|PubMed:10654940, ECO:0000269|PubMed:11952896,
CC ECO:0000269|PubMed:16436507, ECO:0000269|PubMed:16923827}.
CC -!- INTERACTION:
CC P53159; Q12365: BBP1; NbExp=6; IntAct=EBI-23834, EBI-3448;
CC P53159; P47069: MPS3; NbExp=4; IntAct=EBI-23834, EBI-25811;
CC P53159; P52919: NBP1; NbExp=2; IntAct=EBI-23834, EBI-11886;
CC P53159; Q04477: SPC24; NbExp=8; IntAct=EBI-23834, EBI-27228;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:10397772};
CC Single-pass membrane protein {ECO:0000269|PubMed:10397772}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, spindle pole body
CC {ECO:0000269|PubMed:10397772}.
CC -!- SIMILARITY: Belongs to the MPS2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z72597; CAA96780.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08030.1; -; Genomic_DNA.
DR PIR; S64082; S64082.
DR RefSeq; NP_011440.1; NM_001180940.1.
DR AlphaFoldDB; P53159; -.
DR SMR; P53159; -.
DR BioGRID; 33175; 101.
DR ComplexPortal; CPX-1287; MPS2-BBP1 spindle pole body anchor complex.
DR DIP; DIP-2989N; -.
DR IntAct; P53159; 12.
DR MINT; P53159; -.
DR STRING; 4932.YGL075C; -.
DR iPTMnet; P53159; -.
DR MaxQB; P53159; -.
DR PaxDb; P53159; -.
DR PRIDE; P53159; -.
DR EnsemblFungi; YGL075C_mRNA; YGL075C; YGL075C.
DR GeneID; 852805; -.
DR KEGG; sce:YGL075C; -.
DR SGD; S000003043; MPS2.
DR VEuPathDB; FungiDB:YGL075C; -.
DR eggNOG; ENOG502RYE7; Eukaryota.
DR HOGENOM; CLU_069890_0_0_1; -.
DR InParanoid; P53159; -.
DR OMA; FIYAKDF; -.
DR BioCyc; YEAST:G3O-30576-MON; -.
DR PRO; PR:P53159; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53159; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IMP:SGD.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0106084; C:mitotic nuclear membrane microtubule tethering complex; IPI:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0140444; F:cytoskeleton-nuclear membrane anchor activity; IMP:SGD.
DR GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR GO; GO:0000741; P:karyogamy; IMP:SGD.
DR GO; GO:1990608; P:mitotic spindle pole body localization; IDA:ComplexPortal.
DR GO; GO:0071988; P:protein localization to spindle pole body; IMP:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR InterPro; IPR031433; Mps2.
DR Pfam; PF17060; MPS2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..387
FT /note="Monopolar spindle protein 2"
FT /id="PRO_0000202760"
FT TRANSMEM 311..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 216..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..232
FT /evidence="ECO:0000255"
FT COMPBIAS 216..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 44585 MW; CF8AFA86EDEA834C CRC64;
MSNGAFDAIF EYAWGQIDKP ISGDFIYGKD LPKLIEIIEN IFQKAQKSGS YELRLPLFSE
INKDLFRTFS NTKTFFKIHK EEFDDIFFNL VNHPLREILE NAFIGVDSIP SDFIVSMNLN
SPSKFLVENK NKNTEGAGIS TPRKKLTESP IKLLSRNNIG KALEVQVEEL KRELTAKQSL
LQENERQVSE LKIRLETYQE KYASIQQRFS DLQKARQVED NQNSSRTSDP GSPLVTGIDQ
KAILEEFRRR LQRQTDTISF LKDQIRRERG LNCSNDKVSH SKRKHATTDG DGTFKNFISA
VPSNIWVKAT IRIIVCFALL AGVLPYIRKY VYAHDTPSQN SRLQLSWWEN SGILSKIVWF
FEDQTDLETE YRSNANVDDA YSRVFGI
