ID MAD3_YEAST Reviewed; 515 AA.
AC P47074; D6VWG4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=Spindle assembly checkpoint component MAD3;
DE AltName: Full=Mitotic MAD3 protein;
GN Name=MAD3; OrderedLocusNames=YJL013C; ORFNames=J1341;
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 [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 [2]
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 [3]
RP FUNCTION, INTERACTION WITH CDC20 AND BUB3, AND MUTAGENESIS OF
RP 156-GLY--SER-159 AND GLU-382.
RX PubMed=10704439; DOI=10.1083/jcb.148.5.871;
RA Hardwick K.G., Johnston R.C., Smith D.L., Murray A.W.;
RT "MAD3 encodes a novel component of the spindle checkpoint which interacts
RT with Bub3p, Cdc20p, and Mad2p.";
RL J. Cell Biol. 148:871-882(2000).
RN [4]
RP INTERACTION WITH BUB3, AND IDENTIFICATION IN THE MCC COMPLEX.
RX PubMed=11726501; DOI=10.1093/emboj/20.23.6648;
RA Fraschini R., Beretta A., Sironi L., Musacchio A., Lucchini G., Piatti S.;
RT "Bub3 interaction with Mad2, Mad3 and Cdc20 is mediated by WD40 repeats and
RT does not require intact kinetochores.";
RL EMBO J. 20:6648-6659(2001).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION IN THE MCC COMPLEX.
RX PubMed=15879521; DOI=10.1128/ec.4.5.867-878.2005;
RA Poddar A., Stukenberg P.T., Burke D.J.;
RT "Two complexes of spindle checkpoint proteins containing Cdc20 and Mad2
RT assemble during mitosis independently of the kinetochore in Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 4:867-878(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the spindle assembly checkpoint which is a
CC feedback control that prevents cells with incompletely assembled
CC spindles from leaving mitosis. Component of the mitotic checkpoint
CC complex (MCC) which inhibits the ubiquitin ligase activity of the
CC anaphase promoting complex/cyclosome (APC/C) by preventing its
CC activation by CDC20. {ECO:0000269|PubMed:10704439}.
CC -!- SUBUNIT: Component of the mitotic checkpoint complex (MCC) which
CC consists of MAD2, MAD3, BUB3 and CDC20. Interacts with CDC20 and BUB3.
CC {ECO:0000269|PubMed:10704439, ECO:0000269|PubMed:11726501,
CC ECO:0000269|PubMed:15879521}.
CC -!- INTERACTION:
CC P47074; P26449: BUB3; NbExp=14; IntAct=EBI-10369, EBI-3830;
CC P47074; P26309: CDC20; NbExp=9; IntAct=EBI-10369, EBI-4212;
CC P47074; P40958: MAD2; NbExp=3; IntAct=EBI-10369, EBI-10362;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 3170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To yeast protein kinase BUB1 in its non-catalytic N-
CC terminal domain. {ECO:0000305}.
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DR EMBL; Z49288; CAA89304.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08780.1; -; Genomic_DNA.
DR PIR; S56784; S56784.
DR RefSeq; NP_012521.3; NM_001181447.3.
DR PDB; 2I3T; X-ray; 2.80 A; B/D/F/H=354-400.
DR PDBsum; 2I3T; -.
DR AlphaFoldDB; P47074; -.
DR SMR; P47074; -.
DR BioGRID; 33742; 157.
DR ComplexPortal; CPX-963; Mitotic checkpoint complex, MAD2-MAD3-BUB3-CDC20.
DR DIP; DIP-1268N; -.
DR ELM; P47074; -.
DR IntAct; P47074; 9.
DR MINT; P47074; -.
DR STRING; 4932.YJL013C; -.
DR iPTMnet; P47074; -.
DR MaxQB; P47074; -.
DR PaxDb; 4932-YJL013C; -.
DR PeptideAtlas; P47074; -.
DR EnsemblFungi; YJL013C_mRNA; YJL013C; YJL013C.
DR GeneID; 853439; -.
DR KEGG; sce:YJL013C; -.
DR AGR; SGD:S000003550; -.
DR SGD; S000003550; MAD3.
DR VEuPathDB; FungiDB:YJL013C; -.
DR eggNOG; KOG1166; Eukaryota.
DR GeneTree; ENSGT00940000167713; -.
DR HOGENOM; CLU_041820_0_0_1; -.
DR InParanoid; P47074; -.
DR OMA; NSFMESR; -.
DR OrthoDB; 5479089at2759; -.
DR BioCyc; YEAST:G3O-31488-MONOMER; -.
DR Reactome; R-SCE-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR BioGRID-ORCS; 853439; 0 hits in 10 CRISPR screens.
DR EvolutionaryTrace; P47074; -.
DR PRO; PR:P47074; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47074; Protein.
DR GO; GO:0033597; C:mitotic checkpoint complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032837; P:distributive segregation; IMP:SGD.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IBA:GO_Central.
DR GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; IGI:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; IDA:SGD.
DR Gene3D; 1.20.58.2070; -; 1.
DR Gene3D; 1.25.40.930; -; 1.
DR Gene3D; 6.20.50.40; -; 1.
DR InterPro; IPR015661; Bub1/Mad3.
DR InterPro; IPR013212; Mad3/Bub1_I.
DR InterPro; IPR012572; Mad3/Bub1_II.
DR PANTHER; PTHR14030:SF4; BUB1 KINASE, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR14030; MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1; 1.
DR Pfam; PF08311; Mad3_BUB1_I; 1.
DR Pfam; PF08171; Mad3_BUB1_II; 1.
DR SMART; SM00777; Mad3_BUB1_I; 1.
DR PROSITE; PS51489; BUB1_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..515
FT /note="Spindle assembly checkpoint component MAD3"
FT /id="PRO_0000084549"
FT DOMAIN 67..228
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00822"
FT REGION 397..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 156..159
FT /note="GIGS->AAAA: Abolishes interaction with CDC20.
FT Benomyl-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:10704439"
FT MUTAGEN 382
FT /note="E->K: Abolishes interaction with BUB3. Benomyl-
FT sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:10704439"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:2I3T"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:2I3T"
FT HELIX 381..387
FT /evidence="ECO:0007829|PDB:2I3T"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:2I3T"
SQ SEQUENCE 515 AA; 59521 MW; 36550249D81BB6D1 CRC64;
MKAYAKKRIS YMPSSPSQNV INFEEIETQK ENILPLKEGR SAAALSKAIH QPLVEINQVK
SSFEQRLIDE LPALSDPITL YLEYIKWLNN AYPQGGNSKQ SGMLTLLERC LSHLKDLERY
RNDVRFLKIW FWYIELFTRN SFMESRDIFM YMLRNGIGSE LASFYEEFTN LLIQKEKFQY
AVKILQLGIK NKARPNKVLE DRLNHLLREL GENNIQLGNE ISMDSLESTV LGKTRSEFVN
RLELANQNGT SSDVNLTKNN VFVDGEESDV ELFETPNRGV YRDGWENFDL KAERNKENNL
RISLLEANTN LGELKQHEML SQKKRPYDEK LPIFRDSIGR SDPVYQMINT KDQKPEKIDC
NFKLIYCEDE ESKGGRLEFS LEEVLAISRN VYKRVRTNRK HPREANLGQE ESANQKEAEA
QSKRPKISRK ALVSKSLTPS NQGRMFSGEE YINCPMTPKG RSTETSDIIS AVKPRQLTPI
LEMRESNSFS QSKNSEIISD DDKSSSSFIS YPPQR
//
