BUB3_YEAST
ID BUB3_YEAST Reviewed; 341 AA.
AC P26449; D6W292;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Cell cycle arrest protein BUB3;
GN Name=BUB3; OrderedLocusNames=YOR026W; ORFNames=OR26.16;
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=1651171; DOI=10.1016/0092-8674(81)90014-3;
RA Hoyt M.A., Totis L., Roberts B.T.;
RT "S. cerevisiae genes required for cell cycle arrest in response to loss of
RT microtubule function.";
RL Cell 66:507-517(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 IDENTIFICATION IN A COMPLEX WITH MAD1 AND BUB1.
RX PubMed=10837255; DOI=10.1016/s0960-9822(00)00515-7;
RA Brady D.M., Hardwick K.G.;
RT "Complex formation between Mad1p, Bub1p and Bub3p is crucial for spindle
RT checkpoint function.";
RL Curr. Biol. 10:675-678(2000).
RN [5]
RP INTERACTION WITH CDC20; MAD1 AND MAD2, IDENTIFICATION IN THE MCC COMPLEX,
RP AND MUTAGENESIS OF TRP-31 AND TRP-120.
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 [6]
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 [7]
RP IDENTIFICATION IN THE MCC COMPLEX, AND FUNCTION OF 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX PubMed=15544799; DOI=10.1016/j.jmb.2004.09.094;
RA Larsen N.A., Harrison S.C.;
RT "Crystal structure of the spindle assembly checkpoint protein Bub3.";
RL J. Mol. Biol. 344:885-892(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), AND MUTAGENESIS OF GLN-2; GLU-188;
RP GLY-191; LEU-192; LYS-193; ARG-217; GLN-226; ARG-242; SER-276 AND TRP-278.
RX PubMed=15644329; DOI=10.1074/jbc.m412919200;
RA Wilson D.K., Cerna D., Chew E.;
RT "The 1.1-angstrom structure of the spindle checkpoint protein Bub3p reveals
RT functional regions.";
RL J. Biol. Chem. 280:13944-13951(2005).
CC -!- FUNCTION: Required for cell cycle arrest in response to loss of
CC microtubule function. Component of the spindle assembly checkpoint
CC which is a feedback control that prevents cells with incompletely
CC assembled spindles from leaving mitosis. Component of the mitotic
CC checkpoint complex (MCC) which inhibits the ubiquitin ligase activity
CC of the anaphase promoting complex/cyclosome (APC/C) by preventing its
CC activation by CDC20. The formation of a MAD1-BUB1-BUB3 complex seems to
CC be required for the spindle checkpoint mechanism.
CC {ECO:0000269|PubMed:15879521}.
CC -!- SUBUNIT: Component of the mitotic checkpoint complex (MCC) which
CC consists of MAD2, MAD3, BUB3 and CDC20. Part of complex consisting of
CC MAD1, BUB1 and BUB3 after activation of spindle checkpoint. Interacts
CC with MAD1, MAD2 and CDC20. {ECO:0000269|PubMed:10837255,
CC ECO:0000269|PubMed:11726501, ECO:0000269|PubMed:15879521}.
CC -!- INTERACTION:
CC P26449; P41695: BUB1; NbExp=12; IntAct=EBI-3830, EBI-3816;
CC P26449; P26309: CDC20; NbExp=8; IntAct=EBI-3830, EBI-4212;
CC P26449; P40957: MAD1; NbExp=4; IntAct=EBI-3830, EBI-10354;
CC P26449; P40958: MAD2; NbExp=4; IntAct=EBI-3830, EBI-10362;
CC P26449; P47074: MAD3; NbExp=14; IntAct=EBI-3830, EBI-10369;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Phosphorylated by BUB1.
CC -!- MISCELLANEOUS: Present with 1430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat BUB3 family. {ECO:0000305}.
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DR EMBL; M64707; AAA34459.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60742.1; -; Genomic_DNA.
DR EMBL; Z74934; CAA99216.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10808.1; -; Genomic_DNA.
DR PIR; B39654; B39654.
DR RefSeq; NP_014669.1; NM_001183445.1.
DR PDB; 1U4C; X-ray; 2.35 A; A/B=1-341.
DR PDB; 1YFQ; X-ray; 1.10 A; A=1-341.
DR PDB; 2I3S; X-ray; 1.90 A; A/C/E=1-341.
DR PDB; 2I3T; X-ray; 2.80 A; A/C/E/G=1-341.
DR PDB; 4BL0; X-ray; 1.95 A; A/D=1-341.
DR PDBsum; 1U4C; -.
DR PDBsum; 1YFQ; -.
DR PDBsum; 2I3S; -.
DR PDBsum; 2I3T; -.
DR PDBsum; 4BL0; -.
DR AlphaFoldDB; P26449; -.
DR SMR; P26449; -.
DR BioGRID; 34429; 710.
DR ComplexPortal; CPX-154; Bub1-Bub3 complex.
DR ComplexPortal; CPX-3212; Mitotic checkpoint complex, MAD1-MAD2-BUB1-BUB3 subcomplex.
DR ComplexPortal; CPX-963; Mitotic checkpoint complex, MAD2-MAD3-BUB3-CDC20.
DR DIP; DIP-1219N; -.
DR IntAct; P26449; 10.
DR MINT; P26449; -.
DR STRING; 4932.YOR026W; -.
DR iPTMnet; P26449; -.
DR MaxQB; P26449; -.
DR PaxDb; P26449; -.
DR PRIDE; P26449; -.
DR EnsemblFungi; YOR026W_mRNA; YOR026W; YOR026W.
DR GeneID; 854191; -.
DR KEGG; sce:YOR026W; -.
DR SGD; S000005552; BUB3.
DR VEuPathDB; FungiDB:YOR026W; -.
DR eggNOG; KOG1036; Eukaryota.
DR GeneTree; ENSGT00950000183091; -.
DR HOGENOM; CLU_038526_2_0_1; -.
DR InParanoid; P26449; -.
DR OMA; ENECKPK; -.
DR BioCyc; YEAST:G3O-33573-MON; -.
DR Reactome; R-SCE-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR EvolutionaryTrace; P26449; -.
DR PRO; PR:P26449; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P26449; protein.
DR GO; GO:1990298; C:bub1-bub3 complex; IPI:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0033597; C:mitotic checkpoint complex; IDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; IGI:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:ComplexPortal.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IC:ComplexPortal.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; IDA:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..341
FT /note="Cell cycle arrest protein BUB3"
FT /id="PRO_0000050890"
FT REPEAT 9..48
FT /note="WD 1"
FT REPEAT 54..96
FT /note="WD 2"
FT REPEAT 97..137
FT /note="WD 3"
FT REPEAT 144..185
FT /note="WD 4"
FT REPEAT 191..233
FT /note="WD 5"
FT REPEAT 249..288
FT /note="WD 6"
FT REPEAT 292..329
FT /note="WD 7"
FT MUTAGEN 2
FT /note="Q->L: Abolishes checkpoint function. Benomyl-
FT sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 31
FT /note="W->G: Abolishes checkpoint function and interaction
FT with MAD2, MAD3 and CDC20. Benomyl-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:11726501"
FT MUTAGEN 120
FT /note="W->G: Abolishes checkpoint function and interaction
FT with MAD2, MAD3 and CDC20. Benomyl-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:11726501"
FT MUTAGEN 188
FT /note="E->V: Abolishes checkpoint function. No effect on
FT interaction with BUB1 and MAD3. Benomyl-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 191
FT /note="G->R: Abolishes checkpoint function. No effect on
FT interaction with BUB1 and MAD3. Benomyl-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 192
FT /note="L->E: Abolishes checkpoint function. No effect on
FT interaction with BUB1 and MAD3. Benomyl-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 193
FT /note="K->T: Abolishes checkpoint function. No effect on
FT interaction with BUB1 and MAD3. Benomyl-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 217
FT /note="R->E: Abolishes checkpoint function. Benomyl-
FT sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 226
FT /note="Q->L: Abolishes checkpoint function. No effect on
FT interaction with BUB1 and MAD3. Benomyl-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 242
FT /note="R->E: Abolishes checkpoint function. Benomyl-
FT sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 276
FT /note="S->P: Abolishes checkpoint function. Lowers
FT interaction with BUB1 and MAD3. Benomyl-sensitive
FT phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT MUTAGEN 278
FT /note="W->R: Abolishes checkpoint function. No effect on
FT interaction with BUB1. Lowers interaction with MAD3.
FT Benomyl-sensitive phenotype."
FT /evidence="ECO:0000269|PubMed:15644329"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1YFQ"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1YFQ"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 59..76
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1YFQ"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1YFQ"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2I3S"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2I3T"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1YFQ"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2I3S"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:2I3S"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:1YFQ"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1YFQ"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:1YFQ"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1YFQ"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:1YFQ"
SQ SEQUENCE 341 AA; 38445 MW; 0BDFB8697935BCEB CRC64;
MQIVQIEQAP KDYISDIKII PSKSLLLITS WDGSLTVYKF DIQAKNVDLL QSLRYKHPLL
CCNFIDNTDL QIYVGTVQGE ILKVDLIGSP SFQALTNNEA NLGICRICKY GDDKLIAASW
DGLIEVIDPR NYGDGVIAVK NLNSNNTKVK NKIFTMDTNS SRLIVGMNNS QVQWFRLPLC
EDDNGTIEES GLKYQIRDVA LLPKEQEGYA CSSIDGRVAV EFFDDQGDDY NSSKRFAFRC
HRLNLKDTNL AYPVNSIEFS PRHKFLYTAG SDGIISCWNL QTRKKIKNFA KFNEDSVVKI
ACSDNILCLA TSDDTFKTNA AIDQTIELNA SSIYIIFDYE N
