BUB1_YEAST
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 03-AUG-2022, entry version 198.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 724.
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; P41695; -.
DR PRIDE; P41695; -.
DR EnsemblFungi; YGR188C_mRNA; YGR188C; YGR188C.
DR GeneID; 853100; -.
DR KEGG; sce:YGR188C; -.
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; CAKETSL; -.
DR BioCyc; YEAST:G3O-30878-MON; -.
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 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: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:0034501; P:protein localization to kinetochore; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0031134; P:sister chromatid biorientation; IMP:SGD.
DR DisProt; DP01294; -.
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; PTHR14030; 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; SSF56112; 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
