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P47074 (MAD3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spindle assembly checkpoint component MAD3
Alternative name(s):
Mitotic MAD3 protein
Gene names
Name:MAD3
Ordered Locus Names:YJL013C
ORF Names:J1341
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3

Subunit structure

Component of the mitotic checkpoint complex (MCC) which consists of MAD2, MAD3, BUB3 and CDC20. Interacts with CDC20 and BUB3. Ref.3 Ref.4 Ref.6

Subcellular location

Nucleus.

Miscellaneous

Present with 3170 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 BUB1 N-terminal domain.

To yeast protein kinase BUB1 in its non-catalytic N-terminal domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Spindle assembly checkpoint component MAD3
PRO_0000084549

Regions

Domain67 – 228162BUB1 N-terminal

Amino acid modifications

Modified residue151Phosphoserine Ref.9
Modified residue3031Phosphoserine Ref.8
Modified residue4781Phosphothreonine Ref.7
Modified residue4881Phosphoserine Ref.9

Experimental info

Mutagenesis156 – 1594GIGS → AAAA: Abolishes interaction with CDC20. Benomyl-sensitive phenotype. Ref.3
Mutagenesis3821E → K: Abolishes interaction with BUB3. Benomyl-sensitive phenotype. Ref.3

Secondary structure

........ 515
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P47074 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 36550249D81BB6D1

FASTA51559,521
        10         20         30         40         50         60 
MKAYAKKRIS YMPSSPSQNV INFEEIETQK ENILPLKEGR SAAALSKAIH QPLVEINQVK 

        70         80         90        100        110        120 
SSFEQRLIDE LPALSDPITL YLEYIKWLNN AYPQGGNSKQ SGMLTLLERC LSHLKDLERY 

       130        140        150        160        170        180 
RNDVRFLKIW FWYIELFTRN SFMESRDIFM YMLRNGIGSE LASFYEEFTN LLIQKEKFQY 

       190        200        210        220        230        240 
AVKILQLGIK NKARPNKVLE DRLNHLLREL GENNIQLGNE ISMDSLESTV LGKTRSEFVN 

       250        260        270        280        290        300 
RLELANQNGT SSDVNLTKNN VFVDGEESDV ELFETPNRGV YRDGWENFDL KAERNKENNL 

       310        320        330        340        350        360 
RISLLEANTN LGELKQHEML SQKKRPYDEK LPIFRDSIGR SDPVYQMINT KDQKPEKIDC 

       370        380        390        400        410        420 
NFKLIYCEDE ESKGGRLEFS LEEVLAISRN VYKRVRTNRK HPREANLGQE ESANQKEAEA 

       430        440        450        460        470        480 
QSKRPKISRK ALVSKSLTPS NQGRMFSGEE YINCPMTPKG RSTETSDIIS AVKPRQLTPI 

       490        500        510 
LEMRESNSFS QSKNSEIISD DDKSSSSFIS YPPQR 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"MAD3 encodes a novel component of the spindle checkpoint which interacts with Bub3p, Cdc20p, and Mad2p."
Hardwick K.G., Johnston R.C., Smith D.L., Murray A.W.
J. Cell Biol. 148:871-882(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC20 AND BUB3, MUTAGENESIS OF 156-GLY--SER-159 AND GLU-382.
[4]"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 BUB3, IDENTIFICATION IN THE MCC COMPLEX.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"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.
[7]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478, MASS SPECTROMETRY.
Strain: YAL6B.
[8]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, MASS SPECTROMETRY.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-488, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49288 Genomic DNA. Translation: CAA89304.1.
BK006943 Genomic DNA. Translation: DAA08780.1.
PIRS56784.
RefSeqNP_012521.3. NM_001181447.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I3TX-ray2.80B/D/F/H354-400[»]
ProteinModelPortalP47074.
SMRP47074. Positions 19-227, 354-395.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1268N.
IntActP47074. 9 interactions.
MINTMINT-396546.
STRING4932.YJL013C.

Proteomic databases

PaxDbP47074.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL013C; YJL013C; YJL013C.
GeneID853439.
KEGGsce:YJL010C.
sce:YJL013C.

Organism-specific databases

CYGDYJL013c.
SGDS000003550. MAD3.

Phylogenomic databases

eggNOGNOG320292.
GeneTreeENSGT00520000055622.
KOK06680.
K14790.
OrthoDBEOG45QMPQ.

Gene expression databases

GenevestigatorP47074.
GermOnlineYJL013C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR015661. Bub1/Mad3.
IPR012572. Mad3-like.
IPR013212. Mad3_BUB1_I.
[Graphical view]
PANTHERPTHR14030. PTHR14030. 1 hit.
PfamPF08311. Mad3_BUB1_I. 1 hit.
PF08171. Mad3_BUB1_II. 1 hit.
[Graphical view]
SMARTSM00777. Mad3_BUB1_I. 1 hit.
[Graphical view]
PROSITEPS51489. BUB1_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP47074.
NextBio973988.

Entry information

Entry nameMAD3_YEAST
AccessionPrimary (citable) accession number: P47074
Secondary accession number(s): D6VWG4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families