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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

  • bub1-bub3 complex Source: GO_Central
  • condensed nuclear chromosome kinetochore Source: SGD
  • mitotic checkpoint complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2Q → L: Abolishes checkpoint function. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi31W → G: Abolishes checkpoint function and interaction with MAD2, MAD3 and CDC20. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi120W → G: Abolishes checkpoint function and interaction with MAD2, MAD3 and CDC20. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi188E → V: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi191G → R: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi192L → E: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi193K → T: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi217R → E: Abolishes checkpoint function. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi226Q → L: Abolishes checkpoint function. No effect on interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi242R → E: Abolishes checkpoint function. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi276S → P: Abolishes checkpoint function. Lowers interaction with BUB1 and MAD3. Benomyl-sensitive phenotype. 1 Publication1
Mutagenesisi278W → R: Abolishes checkpoint function. No effect on interaction with BUB1. Lowers interaction with MAD3. Benomyl-sensitive phenotype. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000508901 – 341Cell cycle arrest protein BUB3Add BLAST341

Post-translational modificationi

Phosphorylated by BUB1.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP26449.
PRIDEiP26449.

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 interactors.
DIPiDIP-1219N.
IntActiP26449. 7 interactors.
MINTiMINT-396573.

Structurei

Secondary structure

1341
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Beta strandi14 – 20Combined sources7
Helixi21 – 23Combined sources3
Beta strandi25 – 30Combined sources6
Beta strandi33 – 41Combined sources9
Turni42 – 45Combined sources4
Beta strandi46 – 54Combined sources9
Beta strandi59 – 76Combined sources18
Beta strandi81 – 84Combined sources4
Beta strandi86 – 94Combined sources9
Beta strandi104 – 110Combined sources7
Turni111 – 113Combined sources3
Beta strandi114 – 119Combined sources6
Beta strandi122 – 127Combined sources6
Helixi129 – 132Combined sources4
Beta strandi133 – 135Combined sources3
Beta strandi137 – 142Combined sources6
Beta strandi144 – 149Combined sources6
Beta strandi153 – 158Combined sources6
Beta strandi160 – 168Combined sources9
Beta strandi171 – 178Combined sources8
Beta strandi181 – 183Combined sources3
Beta strandi186 – 189Combined sources4
Beta strandi196 – 201Combined sources6
Helixi204 – 206Combined sources3
Beta strandi208 – 213Combined sources6
Beta strandi216 – 222Combined sources7
Beta strandi236 – 239Combined sources4
Beta strandi241 – 243Combined sources3
Beta strandi249 – 251Combined sources3
Beta strandi254 – 259Combined sources6
Turni261 – 263Combined sources3
Beta strandi266 – 270Combined sources5
Beta strandi275 – 279Combined sources5
Turni280 – 283Combined sources4
Beta strandi284 – 288Combined sources5
Beta strandi293 – 302Combined sources10
Beta strandi304 – 312Combined sources9
Helixi315 – 318Combined sources4
Beta strandi320 – 322Combined sources3
Beta strandi332 – 337Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26449.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati9 – 48WD 1Add BLAST40
Repeati54 – 96WD 2Add BLAST43
Repeati97 – 137WD 3Add BLAST41
Repeati144 – 185WD 4Add BLAST42
Repeati191 – 233WD 5Add BLAST43
Repeati249 – 288WD 6Add BLAST40
Repeati292 – 329WD 7Add BLAST38

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.
OrthoDBiEOG092C4UMO.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP26449.
PRIDEiP26449.

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.
OrthoDBiEOG092C4UMO.

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...

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: November 30, 2016
This is version 148 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.