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Cell cycle arrest protein BUB3

 BUB3_YEAST              Reviewed;         341 AA.
P26449; D6W292;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
02-JUN-2021, entry version 182.
RecName: Full=Cell cycle arrest protein BUB3;
Name=BUB3; OrderedLocusNames=YOR026W; ORFNames=OR26.16;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1651171; DOI=10.1016/0092-8674(81)90014-3;
Hoyt M.A., Totis L., Roberts B.T.;
"S. cerevisiae genes required for cell cycle arrest in response to loss of
microtubule function.";
Cell 66:507-517(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[4]
IDENTIFICATION IN A COMPLEX WITH MAD1 AND BUB1.
PubMed=10837255; DOI=10.1016/s0960-9822(00)00515-7;
Brady D.M., Hardwick K.G.;
"Complex formation between Mad1p, Bub1p and Bub3p is crucial for spindle
checkpoint function.";
Curr. Biol. 10:675-678(2000).
[5]
INTERACTION WITH CDC20; MAD1 AND MAD2, IDENTIFICATION IN THE MCC COMPLEX,
AND MUTAGENESIS OF TRP-31 AND TRP-120.
PubMed=11726501; DOI=10.1093/emboj/20.23.6648;
Fraschini R., Beretta A., Sironi L., Musacchio A., Lucchini G., Piatti S.;
"Bub3 interaction with Mad2, Mad3 and Cdc20 is mediated by WD40 repeats and
does not require intact kinetochores.";
EMBO J. 20:6648-6659(2001).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
IDENTIFICATION IN THE MCC COMPLEX, AND FUNCTION OF THE MCC COMPLEX.
PubMed=15879521; DOI=10.1128/ec.4.5.867-878.2005;
Poddar A., Stukenberg P.T., Burke D.J.;
"Two complexes of spindle checkpoint proteins containing Cdc20 and Mad2
assemble during mitosis independently of the kinetochore in Saccharomyces
cerevisiae.";
Eukaryot. Cell 4:867-878(2005).
[8]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
PubMed=15544799; DOI=10.1016/j.jmb.2004.09.094;
Larsen N.A., Harrison S.C.;
"Crystal structure of the spindle assembly checkpoint protein Bub3.";
J. Mol. Biol. 344:885-892(2004).
[9]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), AND MUTAGENESIS OF GLN-2; GLU-188;
GLY-191; LEU-192; LYS-193; ARG-217; GLN-226; ARG-242; SER-276 AND TRP-278.
PubMed=15644329; DOI=10.1074/jbc.m412919200;
Wilson D.K., Cerna D., Chew E.;
"The 1.1-angstrom structure of the spindle checkpoint protein Bub3p reveals
functional regions.";
J. Biol. Chem. 280:13944-13951(2005).
-!- FUNCTION: Required for cell cycle arrest in response to loss of
microtubule function. Component of the spindle assembly checkpoint
which is a feedback control that prevents cells with incompletely
assembled spindles from leaving mitosis. Component of the mitotic
checkpoint complex (MCC) which inhibits the ubiquitin ligase activity
of the anaphase promoting complex/cyclosome (APC/C) by preventing its
activation by CDC20. The formation of a MAD1-BUB1-BUB3 complex seems to
be required for the spindle checkpoint mechanism.
{ECO:0000269|PubMed:15879521}.
-!- SUBUNIT: Component of the mitotic checkpoint complex (MCC) which
consists of MAD2, MAD3, BUB3 and CDC20. Part of complex consisting of
MAD1, BUB1 and BUB3 after activation of spindle checkpoint. Interacts
with MAD1, MAD2 and CDC20. {ECO:0000269|PubMed:10837255,
ECO:0000269|PubMed:11726501, ECO:0000269|PubMed:15879521}.
-!- INTERACTION:
P26449; P41695: BUB1; NbExp=12; IntAct=EBI-3830, EBI-3816;
P26449; P26309: CDC20; NbExp=8; IntAct=EBI-3830, EBI-4212;
P26449; P40957: MAD1; NbExp=4; IntAct=EBI-3830, EBI-10354;
P26449; P40958: MAD2; NbExp=4; IntAct=EBI-3830, EBI-10362;
P26449; P47074: MAD3; NbExp=14; IntAct=EBI-3830, EBI-10369;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- PTM: Phosphorylated by BUB1.
-!- MISCELLANEOUS: Present with 1430 molecules/cell in log phase SD medium.
{ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the WD repeat BUB3 family. {ECO:0000305}.
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EMBL; M64707; AAA34459.1; -; Genomic_DNA.
EMBL; X87331; CAA60742.1; -; Genomic_DNA.
EMBL; Z74934; CAA99216.1; -; Genomic_DNA.
EMBL; BK006948; DAA10808.1; -; Genomic_DNA.
PIR; B39654; B39654.
RefSeq; NP_014669.1; NM_001183445.1.
PDB; 1U4C; X-ray; 2.35 A; A/B=1-341.
PDB; 1YFQ; X-ray; 1.10 A; A=1-341.
PDB; 2I3S; X-ray; 1.90 A; A/C/E=1-341.
PDB; 2I3T; X-ray; 2.80 A; A/C/E/G=1-341.
PDB; 4BL0; X-ray; 1.95 A; A/D=1-341.
PDBsum; 1U4C; -.
PDBsum; 1YFQ; -.
PDBsum; 2I3S; -.
PDBsum; 2I3T; -.
PDBsum; 4BL0; -.
SMR; P26449; -.
BioGRID; 34429; 709.
ComplexPortal; CPX-154; Bub1-Bub3 complex.
ComplexPortal; CPX-3212; Mitotic checkpoint complex, MAD1-MAD2-BUB1-BUB3 subcomplex.
ComplexPortal; CPX-963; Mitotic checkpoint complex, MAD2-MAD3-BUB3-CDC20.
DIP; DIP-1219N; -.
IntAct; P26449; 10.
MINT; P26449; -.
STRING; 4932.YOR026W; -.
iPTMnet; P26449; -.
MaxQB; P26449; -.
PaxDb; P26449; -.
PRIDE; P26449; -.
EnsemblFungi; YOR026W_mRNA; YOR026W; YOR026W.
GeneID; 854191; -.
KEGG; sce:YOR026W; -.
SGD; S000005552; BUB3.
VEuPathDB; FungiDB:YOR026W; -.
eggNOG; KOG1036; Eukaryota.
GeneTree; ENSGT00950000183091; -.
HOGENOM; CLU_038526_2_0_1; -.
InParanoid; P26449; -.
OMA; ENECKPK; -.
Reactome; R-SCE-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
EvolutionaryTrace; P26449; -.
PRO; PR:P26449; -.
Proteomes; UP000002311; Chromosome XV.
RNAct; P26449; protein.
GO; GO:1990298; C:bub1-bub3 complex; IBA:GO_Central.
GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IDA:SGD.
GO; GO:0000776; C:kinetochore; IBA:GO_Central.
GO; GO:0033597; C:mitotic checkpoint complex; IDA:SGD.
GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
GO; GO:0044774; P:mitotic DNA integrity checkpoint; IGI:SGD.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IBA:GO_Central.
GO; GO:1902499; P:positive regulation of protein autoubiquitination; IDA:SGD.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 4.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Nucleus; Phosphoprotein; Reference proteome;
Repeat; WD repeat.
CHAIN 1..341
/note="Cell cycle arrest protein BUB3"
/id="PRO_0000050890"
REPEAT 9..48
/note="WD 1"
REPEAT 54..96
/note="WD 2"
REPEAT 97..137
/note="WD 3"
REPEAT 144..185
/note="WD 4"
REPEAT 191..233
/note="WD 5"
REPEAT 249..288
/note="WD 6"
REPEAT 292..329
/note="WD 7"
MUTAGEN 2
/note="Q->L: Abolishes checkpoint function. Benomyl-
sensitive phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 31
/note="W->G: Abolishes checkpoint function and interaction
with MAD2, MAD3 and CDC20. Benomyl-sensitive phenotype."
/evidence="ECO:0000269|PubMed:11726501"
MUTAGEN 120
/note="W->G: Abolishes checkpoint function and interaction
with MAD2, MAD3 and CDC20. Benomyl-sensitive phenotype."
/evidence="ECO:0000269|PubMed:11726501"
MUTAGEN 188
/note="E->V: Abolishes checkpoint function. No effect on
interaction with BUB1 and MAD3. Benomyl-sensitive
phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 191
/note="G->R: Abolishes checkpoint function. No effect on
interaction with BUB1 and MAD3. Benomyl-sensitive
phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 192
/note="L->E: Abolishes checkpoint function. No effect on
interaction with BUB1 and MAD3. Benomyl-sensitive
phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 193
/note="K->T: Abolishes checkpoint function. No effect on
interaction with BUB1 and MAD3. Benomyl-sensitive
phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 217
/note="R->E: Abolishes checkpoint function. Benomyl-
sensitive phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 226
/note="Q->L: Abolishes checkpoint function. No effect on
interaction with BUB1 and MAD3. Benomyl-sensitive
phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 242
/note="R->E: Abolishes checkpoint function. Benomyl-
sensitive phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 276
/note="S->P: Abolishes checkpoint function. Lowers
interaction with BUB1 and MAD3. Benomyl-sensitive
phenotype."
/evidence="ECO:0000269|PubMed:15644329"
MUTAGEN 278
/note="W->R: Abolishes checkpoint function. No effect on
interaction with BUB1. Lowers interaction with MAD3.
Benomyl-sensitive phenotype."
/evidence="ECO:0000269|PubMed:15644329"
STRAND 2..5
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 14..20
/evidence="ECO:0007829|PDB:1YFQ"
HELIX 21..23
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 25..30
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 33..41
/evidence="ECO:0007829|PDB:1YFQ"
TURN 42..45
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 46..54
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 59..76
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 81..84
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 86..94
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 104..110
/evidence="ECO:0007829|PDB:1YFQ"
TURN 111..113
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 114..119
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 122..127
/evidence="ECO:0007829|PDB:1YFQ"
HELIX 129..132
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 133..135
/evidence="ECO:0007829|PDB:2I3S"
STRAND 137..142
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 144..149
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 153..158
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 160..168
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 171..178
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 181..183
/evidence="ECO:0007829|PDB:2I3T"
STRAND 186..189
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 196..201
/evidence="ECO:0007829|PDB:1YFQ"
HELIX 204..206
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 208..213
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 216..222
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 236..239
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 241..243
/evidence="ECO:0007829|PDB:2I3S"
STRAND 249..251
/evidence="ECO:0007829|PDB:2I3S"
STRAND 254..259
/evidence="ECO:0007829|PDB:1YFQ"
TURN 261..263
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 266..270
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 275..279
/evidence="ECO:0007829|PDB:1YFQ"
TURN 280..283
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 284..288
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 293..302
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 304..312
/evidence="ECO:0007829|PDB:1YFQ"
HELIX 315..318
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 320..322
/evidence="ECO:0007829|PDB:1YFQ"
STRAND 332..337
/evidence="ECO:0007829|PDB:1YFQ"
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


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[BUB3] Mitotic checkpoint protein BUB3
[BUB3.1 At3g19590 MMB12.5] Mitotic checkpoint protein BUB3.1 (Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 3.1)
[bub3 SPAC23H3.08c] Mitotic checkpoint protein bub3
[Bub3] Mitotic checkpoint protein BUB3 (WD repeat type I transmembrane protein A72.5)
[ZNF207 BUGZ] BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (hBuGZ) (Zinc finger protein 207)
[bub-3 Y54G9A.6] Mitotic checkpoint protein bub-3 (Budding uninhibited by benzimidazole 3)
[Znf207 Bugz Zep Zfp207] BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (49 kDa zinc finger protein) (Zinc finger protein 207)
[znf207 bugz] BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (xBuGZ) (Zinc finger protein 207)
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[ZNF207 BUGZ] BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (Zinc finger protein 207)
[CDC20 YGL116W] APC/C activator protein CDC20 (Cell division control protein 20)
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)
[Bub1b Mad3l] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (BubR1) (Mitotic checkpoint kinase MAD3L)
[BUB1 YGR188C G7542] Checkpoint serine/threonine-protein kinase BUB1 (EC 2.7.11.1)
[SIW14 OCA3 YNL032W N2746] Inositol phosphatase SIW14 (EC 3.6.1.52) (5-PP-InsP phosphatase) (Inositol pyrophosphate phosphatase SIW14) (Oxidant-induced cell-cycle arrest protein 3) (Synthetic interaction with WHI2 protein 14)
[TBRG4 CPR2 FASTKD4 KIAA0948] FAST kinase domain-containing protein 4 (Cell cycle progression restoration protein 2) (Cell cycle progression protein 2) (Protein TBRG4) (Transforming growth factor beta regulator 4)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)

Bibliography :
[33384373] CDC20 assists its catalytic incorporation in the mitotic checkpoint complex.
[32479259] The copy-number and varied strengths of MELT motifs in Spc105 balance the strength and responsiveness of the spindle assembly checkpoint.
[32284991] The cohesin release factor Wapl interacts with Bub3 to govern SAC activity in female meiosis I.
[31257143] The Bub1-TPR Domain Interacts Directly with Mad3 to Generate Robust Spindle Checkpoint Arrest.
[30553276] C-Src confers resistance to mitotic stress through inhibition DMAP1/Bub3 complex formation in pancreatic cancer.
[30250048] Analysis of the role of GSK3 in the mitotic checkpoint.
[30205061] Bub1 is not essential for the checkpoint response to unattached kinetochores in diploid human cells.
[29978915] Mechanism of cytokinesis failure in ovarian cystadenomas with defective BRCA1 and P53 pathways.
[29895228] The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores.
[29804664] Assays for the spindle assembly checkpoint in cell culture.