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UniProtKB/Swiss-Prot entry P25300


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BUD5_YEAST
Primary accession number P25300
Secondary accession number Q06729
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on March 15, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name Bud site selection protein 5
Synonyms None
Gene name
Name: BUD5
OrderedLocusNames: YCR038C
ORFNames: YCR38C, YCR526
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=1789011 [NCBI, ExPASy, EBI, Israel, Japan]
Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C., Soustelle C.;
"The MAT locus revisited within a 9.8 kb fragment of chromosome III containing BUD5 and two new open reading frames.";
Yeast 7:881-888(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(91)90017-S; PubMed=1905982 [NCBI, ExPASy, EBI, Israel, Japan]
Powers S., Gonzales E., Christensen T., Cubert J., Broek D.;
"Functional cloning of BUD5, a CDC25-related gene from S. cerevisiae that can suppress a dominant-negative RAS2 mutant.";
Cell 65:1225-1231(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1038/357038a0; PubMed=1574125 [NCBI, ExPASy, EBI, Israel, Japan]
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[4]
SEQUENCE REVISION TO 110; 401; 481 AND N-TERMINUS.
Valles G., Volckaerts G.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-642.
STRAIN=SP1;
DOI=10.1016/0092-8674(91)90016-R; PubMed=1905981 [NCBI, ExPASy, EBI, Israel, Japan]
Chant J., Corrado K., Pringle J.R., Herskowitz I.;
"Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for bud site selection and interacts with bud formation gene BEM1.";
Cell 65:1213-1224(1991).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-642.
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=1964349 [NCBI, ExPASy, EBI, Israel, Japan]
Thierry A., Fairhead C., Dujon B.;
"The complete sequence of the 8.2 kb segment left of MAT on chromosome III reveals five ORFs, including a gene for a yeast ribokinase.";
Yeast 6:521-534(1990).
[7]
FUNCTION.
PubMed=8234337 [NCBI, ExPASy, EBI, Israel, Japan]
Bender A.;
"Genetic evidence for the roles of the bud-site-selection genes BUD5 and BUD2 in control of the Rsr1p (Bud1p) GTPase in yeast.";
Proc. Natl. Acad. Sci. U.S.A. 90:9926-9929(1993).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1016/S0960-9822(01)00230-5; PubMed=11378394 [NCBI, ExPASy, EBI, Israel, Japan]
Marston A.L., Chen T., Yang M.C., Belhumeur P., Chant J.;
"A localized GTPase exchange factor, Bud5, determines the orientation of division axes in yeast.";
Curr. Biol. 11:803-807(2001).
[9]
FUNCTION, AND INTERACTION WITH GSP1.
DOI=10.1007/s004380100511; PubMed=11589573 [NCBI, ExPASy, EBI, Israel, Japan]
Clement M., Lavallee F., Barbes-Morin G., de Repentigny L., Belhumeur P.;
"Overexpression of Bud5p can suppress mutations in the Gsp1p guanine nucleotide exchange factor Prp20p in Saccharomyces cerevisiae.";
Mol. Genet. Genomics 266:20-27(2001).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH AXL2.
DOI=10.1126/science.1060360; PubMed=11313501 [NCBI, ExPASy, EBI, Israel, Japan]
Kang P.J., Sanson A., Lee B., Park H.-O.;
"A GDP/GTP exchange factor involved in linking a spatial landmark to cell polarity.";
Science 292:1376-1378(2001).
[11]
SUBCELLULAR LOCATION, AND INTERACTION WITH AXL1.
DOI=10.1016/S0960-9822(02)01042-4; PubMed=12176366 [NCBI, ExPASy, EBI, Israel, Japan]
Lord M., Inose F., Hiroko T., Hata T., Fujita A., Chant J.;
"Subcellular localization of Axl1, the cell type-specific regulator of polarity.";
Curr. Biol. 12:1347-1352(2002).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
  • FUNCTION: GDP-GTP exchange factor (GEF) for the small GTPase BUD1/RSR1. Regulates the activity of BUD1 together with BUD2 which is a GTPase-activating protein (GAP) of BUD1. Required to produce both the axial and bipolar patterns of bud site selection. Determines the orientation of division axis. Overexpression can suppress mutations in PRP20 which is the GEF for GSP1. May be a cytoplasmic GEF for GSP1. Might also act on the Ras-like protein CDC42. Appears to bind to Ras proteins but not to activate them.
  • SUBUNIT: Interacts with AXL2, BEM1, GSP1 and in haploid cells with AXL1.
  • INTERACTION:
    P40851:AXL1; NbExp=1; IntAct=EBI-3853, EBI-3387;
    P38928:AXL2; NbExp=2; IntAct=EBI-3853, EBI-3397;
    P32835:GSP1; NbExp=2; IntAct=EBI-3853, EBI-7926;
  • SUBCELLULAR LOCATION: Bud neck. Cytoplasm, cell cortex. Note=In haploid cells, forms double rings that encircle the mother-bud neck and split upon cytokinesis, each progeny cell inheriting BUD5 at the axial division remnant. In diploid cells, localizes to the poles of the cell.
  • MISCELLANEOUS: Present with 2110 molecules/cell in log phase SD medium.
  • SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
  • SIMILARITY: Contains 1 Ras-GEF domain.
  • SEQUENCE CAUTION:
    • Sequence=AAA34462.1; Type=Frameshift; Positions=60, 62;
    • Sequence=CAA45334.1; Type=Frameshift; Positions=38;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X63853; CAA45334.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68938; AAA34462.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59720; CAA42305.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63552; AAA34460.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56909; CAA40230.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S19450; BWBYD5.
RefSeq NP_009967.2; -.
3D structure databases
ModBase P25300.
Protein-protein interaction databases
DIP DIP:4991N; -.
IntAct P25300; -.
Organism-specific databases
CYGD YCR038c; -.
SGD S000000634; BUD5.
Yeast-GFP YCR038C.
Gene expression databases
GermOnline YCR038C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005935; Cellular component: cellular bud neck (inferred from direct assay from SGD).
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0000131; Cellular component: incipient cellular bud site (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005088; Molecular function: Ras guanyl-nucleotide exchange factor activity (traceable author statement from SGD).
GO:0007120; Biological process: axial cellular bud site selection (traceable author statement from SGD).
GO:0007121; Biological process: bipolar cellular bud site selection (traceable author statement from SGD).
GO:0007124; Biological process: pseudohyphal growth (traceable author statement from SGD).
GO:0051056; Biological process: regulation of small GTPase mediated signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR008937; Ras_GEF.
IPR000651; RasGef_N.
IPR001895; RasGRF_CDC25.
Graphical view of domain structure.
Gene3D G3DSA:1.10.840.10; RasGRF_CDC25; 1.
PANTHER PTHR23113; Ras_GEF; 1.
Pfam PF00617; RasGEF; 1.
Pfam graphical view of domain structure.
SMART SM00147; RasGEF; 1.
SM00229; RasGEFN; 1.
SMART graphical view of domain structure.
PROSITE PS00720; RASGEF; 1.
PS50009; RASGEF_CAT; 1.
PS50212; RASGEF_NTER; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P25300.
Genome annotation databases
Ensembl YCR038C; Saccharomyces cerevisiae. [Contig view]
GeneID 850405; -.
GenomeReviews X59720_GR; YCR038C.
KEGG sce:YCR038C; -.
NMPDR fig|4932.3.peg.692; -.
Phylogenomic databases
HOGENOM P25300; -.
Other
LinkHub P25300; -.
NextBio 965947; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Guanine-nucleotide releasing factor.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   642  642     Bud site selection protein 5. PRO_0000068859
DOMAIN   224   339  116     N-terminal Ras-GEF. 
DOMAIN   412   640  229     Ras-GEF. 
CONFLICT   110   110        R -> P (in Ref. 1; CAA45334). 
CONFLICT   111   111        Missing (in Ref. 2; AAA34462). 
CONFLICT   225   225        V -> D (in Ref. 5; AAA34460). 
CONFLICT   401   401        L -> P (in Ref. 2 and 6). 
CONFLICT   481   481        S -> A (in Ref. 2 and 6). 
Sequence information
Length: 642 AA [This is the length of the unprocessed precursor] Molecular weight: 75046 Da [This is the MW of the unprocessed precursor] CRC64: 55E688DF5AFAB74F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSPKNKYVYI CVEYIYIYFA KIHKQSTLSS DTTKMFVLID NVLAYLLEQD DLFVTARFAI 

        70         80         90        100        110        120 
QGQIVSRRVN KIHISNITDV LLQQFISHTL PYNDNIVPKK ILDSMRTAVR QLLEATACVS 

       130        140        150        160        170        180 
RECPLVKRSQ DIKRARKRLL SDWYRLGADA NMDAVLLVVN SAWRFLAVWR PFVNSIQHAT 

       190        200        210        220        230        240 
QELYQNIAHY LLHGNVNIQR VTALIQLVMG QDDLLFSMDD VLQEVFRIQL YLNKMLPHNS 

       250        260        270        280        290        300 
HKWQKPSPFD SANLLLNFRD WTTDNALLQE LLLSYPTINK NKHKNHSVPR LIQIWVESYW 

       310        320        330        340        350        360 
QDSETTLKDI LNFWYSHLAE YYEYQELFAD IVQLFINKKR TRQLKIHYIG LTDKEIEENK 

       370        380        390        400        410        420 
PPLDYENLFL QYEIDKTNAN DELCGATDLS DLLFQWKQGE LLEVEAFALN VSPWSLAKTL 

       430        440        450        460        470        480 
TLLESSLYLD IETIEFTRHF KHNDTTIDSV FTLSNQLSSY VLETTLQQTH TISYWLQVAL 

       490        500        510        520        530        540 
SCLYLRNLNS LASIITSLQN HSIERLSLPI DVKSDHLFQR LKVVVHPNNN YNVYRRTIKH 

       550        560        570        580        590        600 
IFHSQLPCVP FTSLLIRDIT FIRDGNDTFT KDGNNVNMQK FNQITKIVAF AQYLQQKQYE 

       610        620        630        640 
DIHCSNTTAR SLLGAMIKVH TLYNDNKDRA YQVSIAKVPR LT 

P25300 in FASTA format

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