BUB3_MOUSE
ID BUB3_MOUSE Reviewed; 326 AA.
AC Q9WVA3; P97397; Q6ZWM5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Mitotic checkpoint protein BUB3;
DE AltName: Full=WD repeat type I transmembrane protein A72.5;
GN Name=Bub3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=10411903; DOI=10.1073/pnas.96.15.8493;
RA Martinez-Exposito M.J., Kaplan K.B., Copeland J., Sorger P.K.;
RT "Retention of the BUB3 checkpoint protein on lagging chromosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8493-8498(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X 129/Sv; TISSUE=Bone marrow;
RA Downs A., Xie X., Yan W., Li J., Palacios R.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP POLY-ADP-RIBOSYLATION BY PARP1.
RX PubMed=12011073; DOI=10.1074/jbc.m200620200;
RA Saxena A., Saffery R., Wong L.H., Kalitsis P., Choo K.H.;
RT "Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose)
RT polymerase-1 protein and are poly(ADP-ribosyl)ated.";
RL J. Biol. Chem. 277:26921-26926(2002).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19888327; DOI=10.1371/journal.pone.0007701;
RA Li M., Li S., Yuan J., Wang Z.B., Sun S.C., Schatten H., Sun Q.Y.;
RT "Bub3 is a spindle assembly checkpoint protein regulating chromosome
RT segregation during mouse oocyte meiosis.";
RL PLoS ONE 4:E7701-E7701(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has a dual function in spindle-assembly checkpoint signaling
CC and in promoting the establishment of correct kinetochore-microtubule
CC (K-MT) attachments. Promotes the formation of stable end-on bipolar
CC attachments. Necessary for kinetochore localization of BUB1. The
CC BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting
CC complex or cyclosome (APC/C) when spindle-assembly checkpoint is
CC activated and inhibits the ubiquitin ligase activity of APC/C by
CC phosphorylating its activator CDC20. This complex can also
CC phosphorylate MAD1L1 (By similarity). Regulates chromosome segregation
CC during oocyte meiosis. {ECO:0000250, ECO:0000269|PubMed:19888327}.
CC -!- SUBUNIT: Interacts with BUB1 and BUBR1. The BUB1/BUB3 complex interacts
CC with MAD1L1. Interacts with ZNF207/BuGZ; leading to promote stability
CC and kinetochore loading of BUB3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000269|PubMed:19888327}. Note=Starts to localize at
CC kinetochores in prometaphase I (Pro-MI) stage and maintains the
CC localization until the metaphase I-anaphase I (MI-AI) transition.
CC {ECO:0000250}.
CC -!- PTM: Poly-ADP-ribosylated by PARP1.
CC -!- SIMILARITY: Belongs to the WD repeat BUB3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB39606.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF149822; AAD38038.1; -; mRNA.
DR EMBL; U67327; AAB39606.1; ALT_FRAME; mRNA.
DR EMBL; AK088534; BAC40409.1; -; mRNA.
DR EMBL; BC025089; AAH25089.1; -; mRNA.
DR CCDS; CCDS40160.1; -.
DR RefSeq; NP_001304279.1; NM_001317350.1.
DR RefSeq; NP_033904.2; NM_009774.4.
DR AlphaFoldDB; Q9WVA3; -.
DR SMR; Q9WVA3; -.
DR BioGRID; 198406; 9.
DR ComplexPortal; CPX-3968; Mitotic Checkpoint Complex.
DR IntAct; Q9WVA3; 3.
DR MINT; Q9WVA3; -.
DR STRING; 10090.ENSMUSP00000081547; -.
DR iPTMnet; Q9WVA3; -.
DR PhosphoSitePlus; Q9WVA3; -.
DR SwissPalm; Q9WVA3; -.
DR REPRODUCTION-2DPAGE; Q9WVA3; -.
DR EPD; Q9WVA3; -.
DR MaxQB; Q9WVA3; -.
DR PaxDb; Q9WVA3; -.
DR PeptideAtlas; Q9WVA3; -.
DR PRIDE; Q9WVA3; -.
DR ProteomicsDB; 265393; -.
DR Antibodypedia; 1213; 388 antibodies from 41 providers.
DR DNASU; 12237; -.
DR Ensembl; ENSMUST00000084502; ENSMUSP00000081547; ENSMUSG00000066979.
DR GeneID; 12237; -.
DR KEGG; mmu:12237; -.
DR UCSC; uc009kbq.1; mouse.
DR CTD; 9184; -.
DR MGI; MGI:1343463; Bub3.
DR VEuPathDB; HostDB:ENSMUSG00000066979; -.
DR eggNOG; KOG1036; Eukaryota.
DR GeneTree; ENSGT00950000183091; -.
DR HOGENOM; CLU_038526_0_0_1; -.
DR InParanoid; Q9WVA3; -.
DR OMA; WDPFNRK; -.
DR OrthoDB; 1048963at2759; -.
DR PhylomeDB; Q9WVA3; -.
DR TreeFam; TF105454; -.
DR Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 12237; 25 hits in 70 CRISPR screens.
DR ChiTaRS; Bub3; mouse.
DR PRO; PR:Q9WVA3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9WVA3; protein.
DR Bgee; ENSMUSG00000066979; Expressed in vestibular epithelium and 267 other tissues.
DR ExpressionAtlas; Q9WVA3; baseline and differential.
DR Genevisible; Q9WVA3; MM.
DR GO; GO:1990298; C:bub1-bub3 complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0033597; C:mitotic checkpoint complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:MGI.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0034501; P:protein localization to kinetochore; ISO:MGI.
DR GO; GO:0051983; P:regulation of chromosome segregation; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Isopeptide bond; Kinetochore; Meiosis;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; WD repeat.
FT CHAIN 1..326
FT /note="Mitotic checkpoint protein BUB3"
FT /id="PRO_0000050892"
FT REPEAT 5..43
FT /note="WD 1"
FT REPEAT 46..83
FT /note="WD 2"
FT REPEAT 86..124
FT /note="WD 3"
FT REPEAT 128..163
FT /note="WD 4"
FT REPEAT 223..262
FT /note="WD 5"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43684"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43684"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O43684"
FT CONFLICT 62
FT /note="C -> W (in Ref. 2; AAB39606)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="G -> A (in Ref. 2; AAB39606)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="R -> W (in Ref. 1; AAD38038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 36955 MW; F1EA57368E5A6345 CRC64;
MTGSNEFKLN QPPEDGISSV KFSPNTSQFL LVSSWDTSVR LYDVPANSMR LKYQHTGAVL
DCAFYDPTHA WSGGLDHQLK MHDLNTDQEN LVGTHDAPIR CVEYCPEVNV MVTGSWDQTV
KLWDPRTPCN AGTFSQPEKV YTLSVSGDRL IVGTAGRRVL VWDLRNMGYV QQRRESSLKY
QTRCIRAFPN KQGYVLSSIE GRVAVEYLDP SPEVQKKKYA FKCHRLKENN IEQIYPVNAI
SFHNIHNTFA TGGSDGFVNI WDPFNKKRLC QFHRYPTSIA SLAFSNDGTT LAIASSYMYE
MDDTEHPEDG IFIRQVTDAE TKPKST
