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Protein

Cell cycle arrest protein BUB3

Gene

BUB3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for cell cycle arrest in response to loss of microtubule function. Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20. The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism.1 Publication

GO - Molecular functioni

  • ubiquitin binding Source: SGD

GO - Biological processi

  • mitotic DNA integrity checkpoint Source: SGD
  • mitotic spindle assembly checkpoint Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

BioCyciYEAST:G3O-33573-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell cycle arrest protein BUB3
Gene namesi
Name:BUB3
Ordered Locus Names:YOR026W
ORF Names:OR26.16
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR026W.
SGDiS000005552. BUB3.

Subcellular locationi

GO - Cellular componenti

  • condensed nuclear chromosome kinetochore Source: SGD
  • mitotic checkpoint complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21Q → L: Abolishes checkpoint function. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi31 – 311W → G: Abolishes checkpoint function and interaction with MAD2, MAD3 and CDC20. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi120 – 1201W → G: Abolishes checkpoint function and interaction with MAD2, MAD3 and CDC20. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi188 – 1881E → V: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi191 – 1911G → R: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi192 – 1921L → E: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi193 – 1931K → T: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi217 – 2171R → E: Abolishes checkpoint function. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi226 – 2261Q → L: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi242 – 2421R → E: Abolishes checkpoint function. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi276 – 2761S → P: Abolishes checkpoint function. Lowers interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication
Mutagenesisi278 – 2781W → R: Abolishes checkpoint function. No effect on interaction with BUB1. Lowers interaction with MAD3. Benomyl-sensitive phenotype. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Cell cycle arrest protein BUB3PRO_0000050890Add
BLAST

Post-translational modificationi

Phosphorylated by BUB1.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP26449.
PeptideAtlasiP26449.

Interactioni

Subunit structurei

Component of the mitotic checkpoint complex (MCC) which consists of MAD2, MAD3, BUB3 and CDC20. Part of complex consisting of MAD1, BUB1 and BUB3 after activation of spindle checkpoint. Interacts with MAD1, MAD2 and CDC20.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BUB1P4169511EBI-3830,EBI-3816
CDC20P263098EBI-3830,EBI-4212
MAD1P409574EBI-3830,EBI-10354
MAD2P409584EBI-3830,EBI-10362
MAD3P470749EBI-3830,EBI-10369

GO - Molecular functioni

  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi34429. 415 interactions.
DIPiDIP-1219N.
IntActiP26449. 7 interactions.
MINTiMINT-396573.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi14 – 207Combined sources
Helixi21 – 233Combined sources
Beta strandi25 – 306Combined sources
Beta strandi33 – 419Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 549Combined sources
Beta strandi59 – 7618Combined sources
Beta strandi81 – 844Combined sources
Beta strandi86 – 949Combined sources
Beta strandi104 – 1107Combined sources
Turni111 – 1133Combined sources
Beta strandi114 – 1196Combined sources
Beta strandi122 – 1276Combined sources
Helixi129 – 1324Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi137 – 1426Combined sources
Beta strandi144 – 1496Combined sources
Beta strandi153 – 1586Combined sources
Beta strandi160 – 1689Combined sources
Beta strandi171 – 1788Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi196 – 2016Combined sources
Helixi204 – 2063Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi216 – 2227Combined sources
Beta strandi236 – 2394Combined sources
Beta strandi241 – 2433Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi254 – 2596Combined sources
Turni261 – 2633Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi275 – 2795Combined sources
Turni280 – 2834Combined sources
Beta strandi284 – 2885Combined sources
Beta strandi293 – 30210Combined sources
Beta strandi304 – 3129Combined sources
Helixi315 – 3184Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi332 – 3376Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U4CX-ray2.35A/B1-341[»]
1YFQX-ray1.10A1-341[»]
2I3SX-ray1.90A/C/E1-341[»]
2I3TX-ray2.80A/C/E/G1-341[»]
4BL0X-ray1.95A/D1-341[»]
ProteinModelPortaliP26449.
SMRiP26449. Positions 1-341.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26449.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati9 – 4840WD 1Add
BLAST
Repeati54 – 9643WD 2Add
BLAST
Repeati97 – 13741WD 3Add
BLAST
Repeati144 – 18542WD 4Add
BLAST
Repeati191 – 23343WD 5Add
BLAST
Repeati249 – 28840WD 6Add
BLAST
Repeati292 – 32938WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat BUB3 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

HOGENOMiHOG000247885.
InParanoidiP26449.
KOiK02180.
OMAiRFAFRCH.
OrthoDBiEOG76QFSQ.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26449-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIVQIEQAP KDYISDIKII PSKSLLLITS WDGSLTVYKF DIQAKNVDLL
60 70 80 90 100
QSLRYKHPLL CCNFIDNTDL QIYVGTVQGE ILKVDLIGSP SFQALTNNEA
110 120 130 140 150
NLGICRICKY GDDKLIAASW DGLIEVIDPR NYGDGVIAVK NLNSNNTKVK
160 170 180 190 200
NKIFTMDTNS SRLIVGMNNS QVQWFRLPLC EDDNGTIEES GLKYQIRDVA
210 220 230 240 250
LLPKEQEGYA CSSIDGRVAV EFFDDQGDDY NSSKRFAFRC HRLNLKDTNL
260 270 280 290 300
AYPVNSIEFS PRHKFLYTAG SDGIISCWNL QTRKKIKNFA KFNEDSVVKI
310 320 330 340
ACSDNILCLA TSDDTFKTNA AIDQTIELNA SSIYIIFDYE N
Length:341
Mass (Da):38,445
Last modified:August 1, 1992 - v1
Checksum:i0BDFB8697935BCEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64707 Genomic DNA. Translation: AAA34459.1.
X87331 Genomic DNA. Translation: CAA60742.1.
Z74934 Genomic DNA. Translation: CAA99216.1.
BK006948 Genomic DNA. Translation: DAA10808.1.
PIRiB39654.
RefSeqiNP_014669.1. NM_001183445.1.

Genome annotation databases

EnsemblFungiiYOR026W; YOR026W; YOR026W.
GeneIDi854191.
KEGGisce:YOR026W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64707 Genomic DNA. Translation: AAA34459.1.
X87331 Genomic DNA. Translation: CAA60742.1.
Z74934 Genomic DNA. Translation: CAA99216.1.
BK006948 Genomic DNA. Translation: DAA10808.1.
PIRiB39654.
RefSeqiNP_014669.1. NM_001183445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U4CX-ray2.35A/B1-341[»]
1YFQX-ray1.10A1-341[»]
2I3SX-ray1.90A/C/E1-341[»]
2I3TX-ray2.80A/C/E/G1-341[»]
4BL0X-ray1.95A/D1-341[»]
ProteinModelPortaliP26449.
SMRiP26449. Positions 1-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34429. 415 interactions.
DIPiDIP-1219N.
IntActiP26449. 7 interactions.
MINTiMINT-396573.

Proteomic databases

MaxQBiP26449.
PeptideAtlasiP26449.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR026W; YOR026W; YOR026W.
GeneIDi854191.
KEGGisce:YOR026W.

Organism-specific databases

EuPathDBiFungiDB:YOR026W.
SGDiS000005552. BUB3.

Phylogenomic databases

HOGENOMiHOG000247885.
InParanoidiP26449.
KOiK02180.
OMAiRFAFRCH.
OrthoDBiEOG76QFSQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-33573-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP26449.
PROiP26449.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "S. cerevisiae genes required for cell cycle arrest in response to loss of microtubule function."
    Hoyt M.A., Totis L., Roberts B.T.
    Cell 66:507-517(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Complex formation between Mad1p, Bub1p and Bub3p is crucial for spindle checkpoint function."
    Brady D.M., Hardwick K.G.
    Curr. Biol. 10:675-678(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH MAD1 AND BUB1.
  5. "Bub3 interaction with Mad2, Mad3 and Cdc20 is mediated by WD40 repeats and does not require intact kinetochores."
    Fraschini R., Beretta A., Sironi L., Musacchio A., Lucchini G., Piatti S.
    EMBO J. 20:6648-6659(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC20; MAD1 AND MAD2, IDENTIFICATION IN THE MCC COMPLEX, MUTAGENESIS OF TRP-31 AND TRP-120.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Two complexes of spindle checkpoint proteins containing Cdc20 and Mad2 assemble during mitosis independently of the kinetochore in Saccharomyces cerevisiae."
    Poddar A., Stukenberg P.T., Burke D.J.
    Eukaryot. Cell 4:867-878(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCC COMPLEX, FUNCTION OF THE MCC COMPLEX.
  8. "Crystal structure of the spindle assembly checkpoint protein Bub3."
    Larsen N.A., Harrison S.C.
    J. Mol. Biol. 344:885-892(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
  9. "The 1.1-angstrom structure of the spindle checkpoint protein Bub3p reveals functional regions."
    Wilson D.K., Cerna D., Chew E.
    J. Biol. Chem. 280:13944-13951(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), MUTAGENESIS OF GLN-2; GLU-188; GLY-191; LEU-192; LYS-193; ARG-217; GLN-226; ARG-242; SER-276 AND TRP-278.

Entry informationi

Entry nameiBUB3_YEAST
AccessioniPrimary (citable) accession number: P26449
Secondary accession number(s): D6W292
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 8, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1430 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.