BUB1_SCHPO
ID BUB1_SCHPO Reviewed; 1044 AA.
AC O94751;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Checkpoint serine/threonine-protein kinase bub1;
DE EC=2.7.11.1;
GN Name=bub1 {ECO:0000303|PubMed:9864354};
GN ORFNames=SPCC1322.12c {ECO:0000312|PomBase:SPCC1322.12c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SP011;
RX PubMed=9864354; DOI=10.1083/jcb.143.7.1775;
RA Bernard P., Hardwick K.G., Javerzat J.-P.;
RT "Fission yeast Bub1 is a mitotic centromere protein essential for the
RT spindle checkpoint and the preservation of correct ploidy through
RT mitosis.";
RL J. Cell Biol. 143:1775-1787(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, INTERACTION WITH BUB3 AND MAD3, AND SUBCELLULAR LOCATION.
RX PubMed=15509783; DOI=10.1128/mcb.24.22.9786-9801.2004;
RA Vanoosthuyse V., Valsdottir R., Javerzat J.-P., Hardwick K.G.;
RT "Kinetochore targeting of fission yeast Mad and Bub proteins is essential
RT for spindle checkpoint function but not for all chromosome segregation
RT roles of Bub1p.";
RL Mol. Cell. Biol. 24:9786-9801(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-78.
RX PubMed=15525673; DOI=10.1091/mbc.e04-07-0558;
RA Kadura S., He X., Vanoosthuyse V., Hardwick K.G., Sazer S.;
RT "The A78V mutation in the Mad3-like domain of Schizosaccharomyces pombe
RT Bub1p perturbs nuclear accumulation and kinetochore targeting of Bub1p,
RT Bub3p, and Mad3p and spindle assembly checkpoint function.";
RL Mol. Biol. Cell 16:385-395(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=28974540; DOI=10.1083/jcb.201612194;
RA Salas-Pino S., Gallardo P., Barrales R.R., Braun S., Daga R.R.;
RT "The fission yeast nucleoporin Alm1 is required for proteasomal degradation
RT of kinetochore components.";
RL J. Cell Biol. 216:3591-3608(2017).
CC -!- FUNCTION: Involved in cell cycle checkpoint enforcement. Acts to
CC stabilize the spindle during mitosis. Required for the correct
CC localization of bub3 and mad3 to the kinetochore. Appears to have a
CC role in chromosome segregation. Catalyzes the phosphorylation of bub3.
CC {ECO:0000269|PubMed:15509783, ECO:0000269|PubMed:15525673,
CC ECO:0000269|PubMed:9864354}.
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: Interacts with bub3 and mad3. {ECO:0000269|PubMed:15509783}.
CC -!- INTERACTION:
CC O94751; O94751: bub1; NbExp=2; IntAct=EBI-1002539, EBI-1002539;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Chromosome, centromere. Note=Associates with kinetochores and
CC centromeres during the early stages of mitosis.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous disruption of nucleoporin alm1
CC results in a growth defect. {ECO:0000269|PubMed:28974540}.
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; AF064796; AAC98348.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA22865.1; -; Genomic_DNA.
DR PIR; T43800; T43800.
DR RefSeq; NP_588140.1; NM_001023130.2.
DR AlphaFoldDB; O94751; -.
DR BioGRID; 275320; 47.
DR DIP; DIP-37961N; -.
DR IntAct; O94751; 6.
DR STRING; 4896.SPCC1322.12c.1; -.
DR iPTMnet; O94751; -.
DR MaxQB; O94751; -.
DR PaxDb; O94751; -.
DR PRIDE; O94751; -.
DR EnsemblFungi; SPCC1322.12c.1; SPCC1322.12c.1:pep; SPCC1322.12c.
DR GeneID; 2538736; -.
DR KEGG; spo:SPCC1322.12c; -.
DR PomBase; SPCC1322.12c; bub1.
DR VEuPathDB; FungiDB:SPCC1322.12c; -.
DR eggNOG; KOG1166; Eukaryota.
DR HOGENOM; CLU_002115_1_0_1; -.
DR InParanoid; O94751; -.
DR PhylomeDB; O94751; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR PRO; PR:O94751; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:1990298; C:bub1-bub3 complex; IMP:PomBase.
DR GO; GO:0034506; C:chromosome, centromeric core domain; IDA:PomBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0071957; C:old mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0072371; F:histone kinase activity (H2A-S121 specific); IDA:PomBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:PomBase.
DR GO; GO:1905318; P:meiosis I spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:1990813; P:meiotic centromeric cohesion protection; IMP:PomBase.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IBA:GO_Central.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:0060629; P:regulation of homologous chromosome segregation; IMP:PomBase.
DR InterPro; IPR015661; Bub1/Mad3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR013212; Mad3/Bub1_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR14030; PTHR14030; 1.
DR Pfam; PF08311; Mad3_BUB1_I; 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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Kinase; Kinetochore; Mitosis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1044
FT /note="Checkpoint serine/threonine-protein kinase bub1"
FT /id="PRO_0000085675"
FT DOMAIN 36..204
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00822"
FT DOMAIN 718..1044
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 209..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 861
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 724..732
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 78
FT /note="A->V: Defect in activating the spindle assembly
FT checkpoint. No localization of bub1, bub3 or mad3 to the
FT kinetochore."
FT /evidence="ECO:0000269|PubMed:15525673"
SQ SEQUENCE 1044 AA; 118353 MW; 32CE71E471BC1BF6 CRC64;
MSDWRLTENV LDQNIPETKP RESKTRLEEI QRLALFQEEL DIIEELDDPV DVWYRCIEWL
LETRFLGMET VNKMLDDAIQ YLERCRFALN DVRHLLIQLA KIKQSYETPD ELQQAAKQFY
QLASKGIGLE LALFYEEYGS LLIRMQRWKE ASEVFHAAVS REARPLVRLL RNAAEFSRAY
DLHNAHPSIH DAPYSSPFPP PRIVLGSKPV SSSTLPSKPK SFQVFSDASS SRDSQNASDL
PQAKSLESEA NTPNLPLLYD KSSGKRVEYS AFNFLALYEN GEERSMEECR AQRYLSSIQP
NTAASFPKVV PKNEISVHHD SSSSNVSPIY KNPVAEQSDT PTRSLPKNYA YVAKSTSPEL
KVFDTVMPVA LSPKPAQKPP SPTIHTKAAL ADILDIFNQP LRSESLEKSS KSPISAQSSY
LGTPLKNDEN SSNSGATSLT GRSQEEHLDF IPSLTPSKNY PSKIYSPNKN LDFSHTASKA
ETYKNSNELE NVKREQPFSE LLPSTLQEET ATGTTSTTFA NAKRRPEDSN ISPTNPKKLH
TLPRSPQYST VDSNSVLSPA MPKGYMFVNE NQSMKHESSV SNPVATIPHE NGKHDFGQLS
PIEHKPFFPK NDDELPGPSG YLTMPYEEAM ASLSNLPTLI NPLDQSLRDL LFQVLRPSLL
RDKDYHEHET SFALVEHIES FVSKIKPKAG GPGRRRSSNR HSLDGPEFHL FYPPNTNLSV
ISKLGQGAFA PVYLVKSKIE TENGDVSQGG AENNESKLFA LKIETPPSCF EFYLTRQAMT
RLKGLRETNS ILPVHQLHMF HDTSHLLMDY RPQGSILDLV NSMHNSTFSS SGMDEILVVF
FSIEFLRIIE ALHTHKIIHG DLKADNALLR LETVADSEWS PIYSPEGLYG WSFKGIYLID
FGRGIDLSLF EEKVKFIADW DTDLQDCIEM REGRPWTYQI DYHGLAAIIY TMLFGQYIET
RIEVINGQRR QVLTQRMKRY WNQDLWHRLF DLLLNPTLHV SEENLPMTEE LSKIRIEMEE
WLVNHSTGGS GLKGLLKSIE KRKI
