BUB1_ARATH
ID BUB1_ARATH Reviewed; 525 AA.
AC F4IVI0; Q8S8D9;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Mitotic checkpoint serine/threonine-protein kinase BUB1;
DE Short=AtBUB1;
DE EC=2.7.11.1;
DE AltName: Full=Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 1;
GN Name=BUB1; OrderedLocusNames=At2g20635; ORFNames=F23N11.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP INTERACTION WITH CDC20-1; CDC20-2 AND CDC20-5.
RX PubMed=21687678; DOI=10.1371/journal.pone.0020618;
RA Kevei Z., Baloban M., Da Ines O., Tiricz H., Kroll A., Regulski K.,
RA Mergaert P., Kondorosi E.;
RT "Conserved CDC20 cell cycle functions are carried out by two of the five
RT isoforms in Arabidopsis thaliana.";
RL PLoS ONE 6:E20618-E20618(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase that performs 2 crucial
CC functions during mitosis: it is essential for spindle-assembly
CC checkpoint signaling and for correct chromosome alignment. Has a key
CC role in the assembly of checkpoint proteins at the kinetochore. Acts as
CC a substrate for anaphase-promoting complex or cyclosome (APC/C).
CC Necessary for ensuring proper chromosome segregation. Can regulate
CC chromosome segregation in a kinetochore-independent manner. The BUB1-
CC BUB3 complex plays a role in the inhibition of APC/C when spindle-
CC assembly checkpoint is activated and inhibits the ubiquitin ligase
CC activity of APC/C by phosphorylating its activator CDC20. Kinase
CC activity is essential for inhibition of APC/CCDC20 and for chromosome
CC alignment but does not play a major role in the spindle-assembly
CC checkpoint activity (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Autophosphorylated when the cells enters mitosis.
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of the mitotic checkpoint complex (MCC); interacts with
CC CDC20-1, CDC20-2 and CDC20-5. {ECO:0000269|PubMed:21687678}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Note=Nuclear in interphase cells.
CC Accumulates gradually during G1 and S phase of the cell cycle, peaks at
CC G2/M, and drops dramatically after mitosis. Localizes to the outer
CC kinetochore. Kinetochore localization is required for normal mitotic
CC timing and checkpoint response to spindle damage and occurs very early
CC in prophase (By similarity). {ECO:0000250}.
CC -!- DOMAIN: BUB1 N-terminal domain directs kinetochore localization and
CC binding to BUB3.
CC -!- PTM: Ubiquitinated and degraded during mitotic exit. {ECO:0000250}.
CC -!- PTM: Upon spindle-assembly checkpoint activation it is
CC hyperphosphorylated and its kinase activity toward CDC20 is stimulated.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. BUB1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM15365.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007048; AAM15365.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07051.1; -; Genomic_DNA.
DR RefSeq; NP_179656.4; NM_127628.5.
DR AlphaFoldDB; F4IVI0; -.
DR SMR; F4IVI0; -.
DR STRING; 3702.AT2G20635.1; -.
DR PaxDb; F4IVI0; -.
DR PRIDE; F4IVI0; -.
DR ProteomicsDB; 240295; -.
DR EnsemblPlants; AT2G20635.1; AT2G20635.1; AT2G20635.
DR GeneID; 816591; -.
DR Gramene; AT2G20635.1; AT2G20635.1; AT2G20635.
DR KEGG; ath:AT2G20635; -.
DR Araport; AT2G20635; -.
DR TAIR; locus:2827363; AT2G20635.
DR eggNOG; KOG1166; Eukaryota.
DR HOGENOM; CLU_036448_1_0_1; -.
DR InParanoid; F4IVI0; -.
DR OMA; KSPFKRY; -.
DR OrthoDB; 1411806at2759; -.
DR PRO; PR:F4IVI0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IVI0; baseline and differential.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR14030; PTHR14030; 2.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Kinase; Kinetochore; Mitosis; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..525
FT /note="Mitotic checkpoint serine/threonine-protein kinase
FT BUB1"
FT /id="PRO_0000423378"
FT DOMAIN 1..162
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00822"
FT DOMAIN 222..520
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..138
FT /note="Necessary for kinetochore localization"
FT /evidence="ECO:0000250"
FT MOTIF 50..57
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 228..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 525 AA; 61123 MW; 3C5CD9F5675BB959 CRC64;
MTIGYRDAAG DPLFPWLMEI KNSMEDLYAG KNSGYDLDKL LFDCISTYKK DSRYRNDLRF
LKIWFLYLEG REDFERVYRE IEETEICKGH SLLYEWYAIF LEVKGLWRRA NSVYQTGLSR
KAEPFDRLKE AHSLFLQRIS KRTKASSLEK VGDDAQATDL ETGFVNPWET STVNGLIHKI
KPQLVKYDGY HVSNKVFPGK ANLSSLQNYS RNKIIEIGGR KYQMKGCAGQ GGFAQVFKAF
IDSNPDEVVA LKVQKPPFPW EFHMYRQLDC RIPDSQRSSF GLAQRVHVYS DYSILVCDYL
SHGTLQDVIN SYVVVGKSME EVLCMYYTIE MLNMLETLHS VGIIHGDFKP DNLLIRYPPE
NLTETGFHEK TGSWSKKGLC LVDWGRGIDL SLFPRTTEFT GDCRTSGFRC VEMKEDKPWK
FQVDTYGLCV IVHMMLHNVY MEIEKKQSLD GGYINMPRTS FKRYWKVDLW KELFTKLLNR
ETCEDDTETL RNLRKSMEEY ICSDPKLMKK LNELLAKQRI SLCSS
