ID   BUB1_YEAST              Reviewed;        1021 AA.
AC   P41695; D6VUX1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=Checkpoint serine/threonine-protein kinase BUB1;
DE            EC=2.7.11.1;
GN   Name=BUB1; OrderedLocusNames=YGR188C; ORFNames=G7542;
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=7969164; DOI=10.1128/mcb.14.12.8282-8291.1994;
RA   Roberts B.T., Farr K.A., Hoyt M.A.;
RT   "The Saccharomyces cerevisiae checkpoint gene BUB1 encodes a novel protein
RT   kinase.";
RL   Mol. Cell. Biol. 14:8282-8291(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9133739;
RX   DOI=10.1002/(sici)1097-0061(19970330)13:4<357::aid-yea77>3.0.co;2-j;
RA   Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M.,
RA   Nombela C.;
RT   "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of
RT   Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 13:357-363(1997).
RN   [3]
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   [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 IN A COMPLEX WITH MAD1 AND BUB3.
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   [6]
RP   FUNCTION, AND INTERACTION WITH SKP1.
RX   PubMed=12769845; DOI=10.1016/s1097-2765(03)00145-x;
RA   Kitagawa K., Abdulle R., Bansal P.K., Cagney G., Fields S., Hieter P.;
RT   "Requirement of Skp1-Bub1 interaction for kinetochore-mediated activation
RT   of the spindle checkpoint.";
RL   Mol. Cell 11:1201-1213(2003).
RN   [7]
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   [8]
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).
CC   -!- FUNCTION: Involved in cell cycle checkpoint enforcement. The formation
CC       of a MAD1-BUB1-BUB3 complex seems to be required for the spindle
CC       checkpoint mechanism. Catalyzes the phosphorylation of BUB3 and its
CC       autophosphorylation. Associates with centromere (CEN) DNA via
CC       interaction with SKP1. The association with SKP1 is required for the
CC       mitotic delay induced by kinetochore tension defects, but not for the
CC       arrest induced by spindle depolymerization or kinetochore assembly
CC       defects. {ECO:0000269|PubMed:12769845}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SUBUNIT: Part of complex consisting of MAD1, BUB1 and BUB3 after
CC       activation of spindle checkpoint. {ECO:0000269|PubMed:10837255}.
CC   -!- INTERACTION:
CC       P41695; P41695: BUB1; NbExp=5; IntAct=EBI-3816, EBI-3816;
CC       P41695; P26449: BUB3; NbExp=12; IntAct=EBI-3816, EBI-3830;
CC       P41695; P26309: CDC20; NbExp=2; IntAct=EBI-3816, EBI-4212;
CC       P41695; P40957: MAD1; NbExp=5; IntAct=EBI-3816, EBI-10354;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Autophosphorylated.
CC   -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. BUB1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; L32027; AAA64894.1; -; Genomic_DNA.
DR   EMBL; Z72973; CAA97214.1; -; Genomic_DNA.
DR   EMBL; X99074; CAA67524.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08282.1; -; Genomic_DNA.
DR   PIR; S64506; S64506.
DR   RefSeq; NP_011704.3; NM_001181317.3.
DR   PDB; 2I3S; X-ray; 1.90 A; B/D/F=315-350.
DR   PDB; 3ESL; X-ray; 1.74 A; A/B=29-230.
DR   PDB; 4BL0; X-ray; 1.95 A; B/E=289-359.
DR   PDBsum; 2I3S; -.
DR   PDBsum; 3ESL; -.
DR   PDBsum; 4BL0; -.
DR   AlphaFoldDB; P41695; -.
DR   SMR; P41695; -.
DR   BioGRID; 33440; 728.
DR   ComplexPortal; CPX-154; Bub1-Bub3 complex.
DR   ComplexPortal; CPX-3212; Mitotic checkpoint complex, MAD1-MAD2-BUB1-BUB3 subcomplex.
DR   DIP; DIP-2236N; -.
DR   ELM; P41695; -.
DR   IntAct; P41695; 16.
DR   MINT; P41695; -.
DR   STRING; 4932.YGR188C; -.
DR   iPTMnet; P41695; -.
DR   MaxQB; P41695; -.
DR   PaxDb; 4932-YGR188C; -.
DR   PeptideAtlas; P41695; -.
DR   EnsemblFungi; YGR188C_mRNA; YGR188C; YGR188C.
DR   GeneID; 853100; -.
DR   KEGG; sce:YGR188C; -.
DR   AGR; SGD:S000003420; -.
DR   SGD; S000003420; BUB1.
DR   VEuPathDB; FungiDB:YGR188C; -.
DR   eggNOG; KOG1166; Eukaryota.
DR   GeneTree; ENSGT00940000167713; -.
DR   HOGENOM; CLU_002115_1_0_1; -.
DR   InParanoid; P41695; -.
DR   OMA; QPWMAPP; -.
DR   OrthoDB; 5479089at2759; -.
DR   BioCyc; YEAST:G3O-30878-MONOMER; -.
DR   BRENDA; 2.7.11.1; 984.
DR   Reactome; R-SCE-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   BioGRID-ORCS; 853100; 2 hits in 13 CRISPR screens.
DR   EvolutionaryTrace; P41695; -.
DR   PRO; PR:P41695; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P41695; Protein.
DR   GO; GO:1990298; C:bub1-bub3 complex; IPI:ComplexPortal.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR   GO; GO:0000776; C:kinetochore; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034508; P:centromere complex assembly; IMP:SGD.
DR   GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR   GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IBA:GO_Central.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:ComplexPortal.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0034501; P:protein localization to kinetochore; IMP:SGD.
DR   GO; GO:0031134; P:sister chromatid biorientation; IMP:SGD.
DR   CDD; cd13981; STKc_Bub1_BubR1; 1.
DR   DisProt; DP01294; -.
DR   Gene3D; 1.20.58.2070; -; 1.
DR   Gene3D; 1.25.40.930; -; 1.
DR   Gene3D; 6.10.20.170; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR015661; Bub1/Mad3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR013212; Mad3/Bub1_I.
DR   InterPro; IPR012572; Mad3/Bub1_II.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00777; Mad3_BUB1_I; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51489; BUB1_N; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell cycle; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..1021
FT                   /note="Checkpoint serine/threonine-protein kinase BUB1"
FT                   /id="PRO_0000085676"
FT   DOMAIN          47..212
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00822"
FT   DOMAIN          705..1021
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        833
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         711..719
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         733
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   MUTAGEN         733
FT                   /note="K->R: Loss of activity."
FT   CONFLICT        531
FT                   /note="D -> V (in Ref. 1; AAA64894)"
FT                   /evidence="ECO:0000305"
FT   STRAND          307..309
FT                   /evidence="ECO:0007829|PDB:4BL0"
FT   STRAND          317..321
FT                   /evidence="ECO:0007829|PDB:2I3S"
FT   HELIX           323..326
FT                   /evidence="ECO:0007829|PDB:2I3S"
FT   STRAND          330..332
FT                   /evidence="ECO:0007829|PDB:4BL0"
FT   HELIX           336..343
FT                   /evidence="ECO:0007829|PDB:2I3S"
SQ   SEQUENCE   1021 AA;  117868 MW;  6D76FC980775D3F9 CRC64;
     MNLDLGSTVR GYESDKDTFP QSKGVSSSQK EQHSQLNQTK IAYEQRLLND LEDMDDPLDL
     FLDYMIWIST SYIEVDSESG QEVLRSTMER CLIYIQDMET YRNDPRFLKI WIWYINLFLS
     NNFHESENTF KYMFNKGIGT KLSLFYEEFS KLLENAQFFL EAKVLLELGA ENNCRPYNRL
     LRSLSNYEDR LREMNIVENQ NSVPDSRERL KGRLIYRTAP FFIRKFLTSS LMTDDKENRA
     NLNSNVGVGK SAPNVYQDSI VVADFKSETE RLNLNSSKQP SNQRLKNGNK KTSIYADQKQ
     SNNPVYKLIN TPGRKPERIV FNFNLIYPEN DEEFNTEEIL AMIKGLYKVQ RRGKKHTEDY
     TSDKNRKKRK LDVLVERRQD LPSSQPPVVP KSTRIEVFKD DDNPSQSTHH KNTQVQVQTT
     TSILPLKPVV DGNLAHETPV KPSLTSNASR SPTVTAFSKD AINEVFSMFN QHYSTPGALL
     DGDDTTTSKF NVFENFTQEF TAKNIEDLTE VKDPKQETVS QQTTSTNETN DRYERLSNSS
     TRPEKADYMT PIKETTETDV VPIIQTPKEQ IRTEDKKSGD NTETQTQLTS TTIQSSPFLT
     QPEPQAEKLL QTAEHSEKSK EHYPTIIPPF TKIKNQPPVI IENPLSNNLR AKFLSEISPP
     LFQYNTFYNY NQELKMSSLL KKIHRVSRNE NKNPIVDFKK TGDLYCIRGE LGEGGYATVY
     LAESSQGHLR ALKVEKPASV WEYYIMSQVE FRLRKSTILK SIINASALHL FLDESYLVLN
     YASQGTVLDL INLQREKAID GNGIMDEYLC MFITVELMKV LEKIHEVGII HGDLKPDNCM
     IRLEKPGEPL GAHYMRNGED GWENKGIYLI DFGRSFDMTL LPPGTKFKSN WKADQQDCWE
     MRAGKPWSYE ADYYGLAGVI HSMLFGKFIE TIQLQNGRCK LKNPFKRYWK KEIWGVIFDL
     LLNSGQASNQ ALPMTEKIVE IRNLIESHLE QHAENHLRNV ILSIEEELSH FQYKGKPSRR
     F
//