MPS3_YEAST
ID MPS3_YEAST Reviewed; 682 AA.
AC P47069; D6VWG1; P47070;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Spindle pole body assembly component MPS3 {ECO:0000303|PubMed:12486115};
DE AltName: Full=98 kDa nuclear envelope protein {ECO:0000303|PubMed:12493774};
DE AltName: Full=Monopolar spindle protein 3 {ECO:0000303|PubMed:12486115};
GN Name=MPS3 {ECO:0000303|PubMed:12486115};
GN Synonyms=NEP98 {ECO:0000303|PubMed:12493774}; OrderedLocusNames=YJL019W;
GN ORFNames=J1310, J1315, YJL018W;
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], IDENTIFICATION OF FRAMESHIFT, FUNCTION,
RP SUBCELLULAR LOCATION, INTERACTION WITH CDC31, AND MUTAGENESIS OF SER-472.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=12486115; DOI=10.1083/jcb.200208169;
RA Jaspersen S.L., Giddings T.H. Jr., Winey M.;
RT "Mps3p is a novel component of the yeast spindle pole body that interacts
RT with the yeast centrin homologue Cdc31p.";
RL J. Cell Biol. 159:945-956(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF FRAMESHIFT, FUNCTION,
RP SUBCELLULAR LOCATION, INTERACTION WITH JEM1, TOPOLOGY, AND MUTAGENESIS OF
RP ASN-597.
RX PubMed=12493774; DOI=10.1074/jbc.m210934200;
RA Nishikawa S., Terazawa Y., Nakayama T., Hirata A., Makio T., Endo T.;
RT "Nep98p is a component of the yeast spindle pole body and essential for
RT nuclear division and fusion.";
RL J. Biol. Chem. 278:9938-9943(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [6]
RP IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH ECO1.
RX PubMed=15355977; DOI=10.1074/jbc.m404324200;
RA Antoniacci L.M., Kenna M.A., Uetz P., Fields S., Skibbens R.V.;
RT "The spindle pole body assembly component Mps3p/Nep98p functions in sister
RT chromatid cohesion.";
RL J. Biol. Chem. 279:49542-49550(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15282802; DOI=10.1002/yea.1133;
RA Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.;
RT "Localization of proteins that are coordinately expressed with Cln2 during
RT the cell cycle.";
RL Yeast 21:793-800(2004).
RN [9]
RP FUNCTION.
RX PubMed=16682351; DOI=10.1016/j.cub.2006.03.060;
RA Antoniacci L.M., Skibbens R.V.;
RT "Sister-chromatid telomere cohesion is nonredundant and resists both
RT spindle forces and telomere motility.";
RL Curr. Biol. 16:902-906(2006).
RN [10]
RP FUNCTION, MUTAGENESIS OF LEU-465; LEU-466; TYR-476; TRP-477; TRP-487;
RP ILE-489; PRO-494; LEU-495; TYR-496; LEU-497; THR-498; ILE-500; TYR-502;
RP HIS-504; HIS-512; ALA-517; LEU-523; ALA-540; GLN-572; GLN-573; ILE-590;
RP PHE-592; GLN-593; VAL-594; GLY-599; ILE-604; SER-605; LEU-606; ILE-611 AND
RP GLY-613, DOMAIN SUN, SUBCELLULAR LOCATION, AND INTERACTION WITH MPS2.
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 EST1.
RX PubMed=17245108; DOI=10.4161/cc.6.1.3647;
RA Antoniacci L.M., Kenna M.A., Skibbens R.V.;
RT "The nuclear envelope and spindle pole body-associated Mps3 protein bind
RT telomere regulators and function in telomere clustering.";
RL Cell Cycle 6:75-79(2007).
RN [12]
RP FUNCTION, AND INTERACTION WITH SIR4.
RX PubMed=18039933; DOI=10.1083/jcb.200706040;
RA Bupp J.M., Martin A.E., Stensrud E.S., Jaspersen S.L.;
RT "Telomere anchoring at the nuclear periphery requires the budding yeast
RT Sad1-UNC-84 domain protein Mps3.";
RL J. Cell Biol. 179:845-854(2007).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NDJ1.
RX PubMed=17495028; DOI=10.1073/pnas.0606165104;
RA Conrad M.N., Lee C.Y., Wilkerson J.L., Dresser M.E.;
RT "MPS3 mediates meiotic bouquet formation in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8863-8868(2007).
RN [14]
RP FUNCTION, AND INTERACTION WITH CSM4 AND NDJ1.
RX PubMed=18585352; DOI=10.1016/j.cell.2008.04.047;
RA Conrad M.N., Lee C.Y., Chao G., Shinohara M., Kosaka H., Shinohara A.,
RA Conchello J.A., Dresser M.E.;
RT "Rapid telomere movement in meiotic prophase is promoted by NDJ1, MPS3, and
RT CSM4 and is modulated by recombination.";
RL Cell 133:1175-1187(2008).
RN [15]
RP FUNCTION.
RX PubMed=19390086; DOI=10.1101/gad.1782209;
RA Oza P., Jaspersen S.L., Miele A., Dekker J., Peterson C.L.;
RT "Mechanisms that regulate localization of a DNA double-strand break to the
RT nuclear periphery.";
RL Genes Dev. 23:912-927(2009).
RN [16]
RP FUNCTION.
RX PubMed=19390087; DOI=10.1101/gad.1787509;
RA Schober H., Ferreira H., Kalck V., Gehlen L.R., Gasser S.M.;
RT "Yeast telomerase and the SUN domain protein Mps3 anchor telomeres and
RT repress subtelomeric recombination.";
RL Genes Dev. 23:928-938(2009).
RN [17]
RP FUNCTION.
RX PubMed=19217407; DOI=10.1016/j.molcel.2009.01.016;
RA Kalocsay M., Hiller N.J., Jentsch S.;
RT "Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome
RT fixation in response to a persistent DNA double-strand break.";
RL Mol. Cell 33:335-343(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [19]
RP FUNCTION.
RX PubMed=20016273; DOI=10.4161/cc.9.1.10317;
RA Oza P., Peterson C.L.;
RT "Opening the DNA repair toolbox: localization of DNA double strand breaks
RT to the nuclear periphery.";
RL Cell Cycle 9:43-49(2010).
RN [20]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=22017544; DOI=10.1111/j.1365-2443.2011.01554.x;
RA Rao H.B., Shinohara M., Shinohara A.;
RT "Mps3 SUN domain is important for chromosome motion and juxtaposition of
RT homologous chromosomes during meiosis.";
RL Genes Cells 16:1081-1096(2011).
RN [21]
RP INTERACTION WITH HTZ1, AND SUBCELLULAR LOCATION.
RX PubMed=21518795; DOI=10.1083/jcb.201011017;
RA Gardner J.M., Smoyer C.J., Stensrud E.S., Alexander R., Gogol M.,
RA Wiegraebe W., Jaspersen S.L.;
RT "Targeting of the SUN protein Mps3 to the inner nuclear membrane by the
RT histone variant H2A.Z.";
RL J. Cell Biol. 193:489-507(2011).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=30141044; DOI=10.1007/978-1-4939-8691-0_12;
RA Unruh J.R., Slaughter B.D., Jaspersen S.L.;
RT "Functional analysis of the yeast LINC complex using fluctuation
RT spectroscopy and super-resolution imaging.";
RL Methods Mol. Biol. 1840:137-161(2018).
RN [23]
RP INTERACTION WITH REC8, AND SUBCELLULAR LOCATION.
RX PubMed=30417519; DOI=10.1111/gtc.12653;
RA Bommi J.R., Rao H.B.D.P., Challa K., Higashide M., Shinmyozu K.,
RA Nakayama J.I., Shinohara M., Shinohara A.;
RT "Meiosis-specific cohesin component, Rec8, promotes the localization of
RT Mps3 SUN domain protein on the nuclear envelope.";
RL Genes Cells 24:94-106(2019).
RN [24]
RP FUNCTION, IDENTIFICATION WITHIN THE LINC COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=32967926; DOI=10.26508/lsa.202000824;
RA Fan J., Jin H., Koch B.A., Yu H.G.;
RT "Mps2 links Csm4 and Mps3 to form a telomere-associated LINC complex in
RT budding yeast.";
RL Life. Sci Alliance 3:0-0(2020).
RN [25]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-189 AND SER-190, AND
RP MUTAGENESIS OF 188-THR--SER-190.
RX PubMed=34586062; DOI=10.7554/elife.63119;
RA Prasada Rao H.B., Sato T., Challa K., Fujita Y., Shinohara M.,
RA Shinohara A.;
RT "Phosphorylation of luminal region of the SUN-domain protein Mps3 promotes
RT nuclear envelope localization during meiosis.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Component of the linker nucleocytoskeleton and cytoskeleton
CC (LINC) complex that regulates telomere movement and meiotic
CC recombination during meiosis (PubMed:17245108, PubMed:18585352,
CC PubMed:32967926). Connects the spindle pole body with the nuclear
CC envelope through its interaction with MPS2 and mediates meiotic bouquet
CC formation and rapid chromosome movements in meiotic prophase
CC (PubMed:16923827, PubMed:17495028, PubMed:22017544). Functions as an
CC integral membrane anchor for telomeres and is a nuclear receptor for
CC the SIR4 pathway of telomere tethering and gene inactivation
CC (PubMed:18039933, PubMed:19390087). Essential for nuclear division and
CC fusion and required for the first step of spindle pole body duplication
CC in G1 (PubMed:12486115, PubMed:12493774). Functions in sister chromatid
CC cohesion establishment (PubMed:15355977, PubMed:16682351). Recruits
CC double-strand breaks (DSBs) to the nuclear periphery for chromosome
CC healing (PubMed:19390086, PubMed:19217407, PubMed:20016273).
CC {ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:12493774,
CC ECO:0000269|PubMed:15355977, ECO:0000269|PubMed:16682351,
CC ECO:0000269|PubMed:16923827, ECO:0000269|PubMed:17245108,
CC ECO:0000269|PubMed:17495028, ECO:0000269|PubMed:18039933,
CC ECO:0000269|PubMed:18585352, ECO:0000269|PubMed:19217407,
CC ECO:0000269|PubMed:19390086, ECO:0000269|PubMed:19390087,
CC ECO:0000269|PubMed:20016273, ECO:0000269|PubMed:22017544,
CC ECO:0000269|PubMed:32967926}.
CC -!- SUBUNIT: Component of the linker nucleocytoskeleton and cytoskeleton
CC (LINC) complex composed of at least MPS2, MPS3 and CSM4
CC (PubMed:32967926). Interacts with HTZ1 (PubMed:21518795). Interacts
CC with REC8 (PubMed:30417519). Interacts with CSM4; ECO1, EST1, JEM1,
CC CDC31, NDJ1, MPS2 and SIR4 (PubMed:12486115, PubMed:12493774,
CC PubMed:15355977, PubMed:16923827, PubMed:17245108, PubMed:17495028,
CC PubMed:18039933, PubMed:18585352). {ECO:0000269|PubMed:12486115,
CC ECO:0000269|PubMed:12493774, ECO:0000269|PubMed:15355977,
CC ECO:0000269|PubMed:16923827, ECO:0000269|PubMed:17245108,
CC ECO:0000269|PubMed:17495028, ECO:0000269|PubMed:18039933,
CC ECO:0000269|PubMed:18585352, ECO:0000269|PubMed:21518795,
CC ECO:0000269|PubMed:30417519, ECO:0000269|PubMed:32967926}.
CC -!- INTERACTION:
CC P47069; P06704: CDC31; NbExp=2; IntAct=EBI-25811, EBI-4259;
CC P47069; Q08955: CSM4; NbExp=2; IntAct=EBI-25811, EBI-31728;
CC P47069; P36049: EBP2; NbExp=4; IntAct=EBI-25811, EBI-6289;
CC P47069; P43605: ECO1; NbExp=5; IntAct=EBI-25811, EBI-22988;
CC P47069; P17214: EST1; NbExp=3; IntAct=EBI-25811, EBI-6684;
CC P47069; Q12692: HTZ1; NbExp=3; IntAct=EBI-25811, EBI-8080;
CC P47069; P40358: JEM1; NbExp=2; IntAct=EBI-25811, EBI-25940;
CC P47069; P53159: MPS2; NbExp=4; IntAct=EBI-25811, EBI-23834;
CC P47069; Q12366: NDJ1; NbExp=2; IntAct=EBI-25811, EBI-34568;
CC P47069; Q08746: RRS1; NbExp=4; IntAct=EBI-25811, EBI-16026;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:21518795,
CC ECO:0000269|PubMed:22017544, ECO:0000269|PubMed:30141044,
CC ECO:0000269|PubMed:30417519, ECO:0000269|PubMed:34586062}; Single-pass
CC type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, spindle pole body
CC {ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:12493774,
CC ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:22017544,
CC ECO:0000269|PubMed:30141044}. Chromosome, telomere
CC {ECO:0000269|PubMed:32967926}. Note=Localizes to the spindle pole body
CC half bridge throughout the cell cycle (PubMed:15282802). Relocalizes
CC from the spindle pole body to the nuclear envelope in meiosis, via the
CC interaction with HTZ1 (PubMed:22017544, PubMed:21518795). The cohesin
CC component REC8 promotes localization on nuclear envelope in mitotic
CC cells (PubMed:30417519). {ECO:0000269|PubMed:15282802,
CC ECO:0000269|PubMed:21518795, ECO:0000269|PubMed:22017544,
CC ECO:0000269|PubMed:30417519}.
CC -!- DOMAIN: The SUN domain is involved in the binding to MPS2 and is
CC important for modulating chromosome motion events that act in meiotic
CC chromosome juxtaposition and by extension, promoting proper
CC morphogenesis of the synaptonemal complex.
CC {ECO:0000269|PubMed:16923827, ECO:0000269|PubMed:22017544}.
CC -!- PTM: Phosphorylation at Ser-189 and Ser-190 by CDC7 and CDC28 during
CC meiosis regulates of the localization on nuclear envelope for meiotic
CC chromosome motion and nuclear envelope remodeling.
CC {ECO:0000269|PubMed:34586062}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA89309.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA89310.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z49294; CAA89309.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z49294; CAA89310.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006943; DAA08777.1; -; Genomic_DNA.
DR PIR; S56789; S56789.
DR PIR; S56790; S56790.
DR RefSeq; NP_012515.4; NM_001181453.3.
DR AlphaFoldDB; P47069; -.
DR BioGRID; 33739; 501.
DR DIP; DIP-1311N; -.
DR IntAct; P47069; 25.
DR MINT; P47069; -.
DR STRING; 4932.YJL019W; -.
DR iPTMnet; P47069; -.
DR MaxQB; P47069; -.
DR PaxDb; P47069; -.
DR PRIDE; P47069; -.
DR EnsemblFungi; YJL019W_mRNA; YJL019W; YJL019W.
DR GeneID; 853434; -.
DR KEGG; sce:YJL019W; -.
DR SGD; S000003556; MPS3.
DR VEuPathDB; FungiDB:YJL019W; -.
DR eggNOG; ENOG502QSZA; Eukaryota.
DR HOGENOM; CLU_025282_0_0_1; -.
DR InParanoid; P47069; -.
DR OMA; IYNANQH; -.
DR BioCyc; YEAST:G3O-31491-MON; -.
DR PRO; PR:P47069; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47069; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005825; C:half bridge of spindle pole body; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:SGD.
DR GO; GO:0000741; P:karyogamy; IMP:SGD.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Signal-anchor; Telomere; Transmembrane; Transmembrane helix.
FT CHAIN 1..682
FT /note="Spindle pole body assembly component MPS3"
FT /id="PRO_0000076266"
FT TOPO_DOM 1..154
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..682
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 427..616
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..682
FT /note="Interaction with CDC31"
FT /evidence="ECO:0000269|PubMed:12486115"
FT REGION 431..650
FT /note="Interaction with JEM1"
FT /evidence="ECO:0000269|PubMed:12493774"
FT REGION 641..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..273
FT /evidence="ECO:0000255"
FT COMPBIAS 85..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:34586062"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:34586062"
FT MUTAGEN 188..190
FT /note="TSS->AAA: Impairs the localization to the nuclear
FT inner membrane."
FT /evidence="ECO:0000269|PubMed:34586062"
FT MUTAGEN 188..190
FT /note="TSS->DDD: Mimics constitutive phosphorylation and
FT blocks the regulation of the localization to nuclear inner
FT membrane."
FT /evidence="ECO:0000269|PubMed:34586062"
FT MUTAGEN 465
FT /note="L->E: Lethal; when associated with E-466."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 466
FT /note="L->E: Lethal; when associated with E-465."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 472
FT /note="S->N: In mps3-1; defective in spindle pole body
FT assembly and duplication."
FT /evidence="ECO:0000269|PubMed:12486115"
FT MUTAGEN 476
FT /note="Y->C: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 477
FT /note="W->A: Defective in spindle pole body duplication at
FT 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 487
FT /note="W->A: Defective in spindle pole body duplication at
FT 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 489
FT /note="I->H: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 494
FT /note="P->A: Lethal; when associated with A-495; A-496; A-
FT 497 and A-498."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 495
FT /note="L->A: Lethal; when associated with A-494; A-496; A-
FT 497 and A-498."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 496
FT /note="Y->A: Lethal; when associated with A-494; A-495; A-
FT 497 and A-498."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 497
FT /note="L->A: Lethal; when associated with A-494; A-495; A-
FT 496 and A-498."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 498
FT /note="T->A: Lethal; when associated with A-494; A-495; A-
FT 496 and A-497."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 500
FT /note="I->D: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 502
FT /note="Y->H: Defective in spindle pole body duplication at
FT 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 504
FT /note="H->A: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 512
FT /note="H->P: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 517
FT /note="A->P: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 523
FT /note="L->K: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 540
FT /note="A->D: Defective in spindle pole body duplication at
FT 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 572
FT /note="Q->L: Defective in spindle pole body duplication at
FT 37 degrees Celsius; when associated with L-573."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 573
FT /note="Q->L: Defective in spindle pole body duplication at
FT 37 degrees Celsius; when associated with L-572."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 590
FT /note="I->D: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 592
FT /note="F->S: Defective in spindle pole body duplication at
FT 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 593
FT /note="Q->A: Lethal; when associated with D-594."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 594
FT /note="V->D: Lethal; when associated with A-593."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 597
FT /note="N->K: In nep98-7; defective in spindle organization
FT during nuclear division and in G2/M progression."
FT /evidence="ECO:0000269|PubMed:12493774"
FT MUTAGEN 599
FT /note="G->A: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 604
FT /note="I->W: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 605
FT /note="S->C: Lethal; when associated with Q-606."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 606
FT /note="L->Q: Lethal; when associated with C-605."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 611
FT /note="I->R: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
FT MUTAGEN 613
FT /note="G->D: Lethal."
FT /evidence="ECO:0000269|PubMed:16923827"
SQ SEQUENCE 682 AA; 79175 MW; 71B54CEB2B876815 CRC64;
MNNSNEHRRE EAGAANEQMP YNKAVKSAYA DVLKDKMNRE QEISLRAIKK GIYTDGGETD
NYDMDKENDS AYEMFKKNLD FPLDQHNDDD DDDPYIEDNG QETDGYSDED YTDEADKSFI
EDSDSDSYDL ESNSDFEENL ESSGEAKKLK WRTYIFYGGL FFVFYFFGSF LMTTVKNNDL
ESHSSGATSS PGKSFSNLQK QVNHLYSELS KRDEKHSSEL DKTVKIIVSQ FEKNIKRLLP
SNLVNFENDI NSLTKQVETI STSMSELQRR NHKFTVENVT QWQDQLVKQL DTHLPQEIPV
VINNSSSLLI IPELHNYLSA LISDVIESPG IGTAGSAESR WEYDLNRYVK EILSNELQYI
DKDYFIQEMN RRLQSNKQEI WEEITNRLET QQQQQQQQVQ QDYSNVPQQY SSILMKRLIH
QIYNSNQHQW EDDLDFATYV QGTKLLNHLT SPTWRQGSGV QPIELLTDSK QSSSTYWQCE
NEPGCSWAIR FKTPLYLTKI SYMHGRFTNN LHIMNSAPRL ISLYVKLSQT KEIKALQTLA
NQYGFGQHHK RDRNYIKIAK FEYRLTDSRI RQQMYLPPWF IQLKPLVRSI VFQVDENYGN
KKFISLRKFI INGVTPQDLQ IIENNEFPVL LGDTPEYGVT QNTDEGKRKV LLSKPPYASS
STSTKFHPAS NVPSFGQDEL DQ
