Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25300

- BUD5_YEAST

UniProt

P25300 - BUD5_YEAST

Protein

Bud site selection protein 5

Gene

BUD5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (15 Mar 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.3 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. Ras guanyl-nucleotide exchange factor activity Source: SGD

    GO - Biological processi

    1. axial cellular bud site selection Source: SGD
    2. bipolar cellular bud site selection Source: SGD
    3. positive regulation of Ras GTPase activity Source: GOC
    4. small GTPase mediated signal transduction Source: InterPro

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29350-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bud site selection protein 5
    Gene namesi
    Name:BUD5
    Ordered Locus Names:YCR038C
    ORF Names:YCR38C, YCR526
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCR038c.
    SGDiS000000634. BUD5.

    Subcellular locationi

    Bud neck. Cytoplasmcell 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.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cellular bud neck Source: SGD
    3. incipient cellular bud site Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 642642Bud site selection protein 5PRO_0000068859Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP25300.

    Interactioni

    Subunit structurei

    Interacts with AXL2, BEM1, GSP1 and in haploid cells with AXL1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AXL2P389282EBI-3853,EBI-3397
    GSP1P328352EBI-3853,EBI-7926

    Protein-protein interaction databases

    BioGridi31021. 16 interactions.
    DIPiDIP-4991N.
    IntActiP25300. 3 interactions.
    MINTiMINT-474246.
    STRINGi4932.YCR038C.

    Structurei

    3D structure databases

    ProteinModelPortaliP25300.
    SMRiP25300. Positions 411-599.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini224 – 339116N-terminal Ras-GEFPROSITE-ProRule annotationAdd
    BLAST
    Domaini412 – 640229Ras-GEFPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 N-terminal Ras-GEF domain.PROSITE-ProRule annotation
    Contains 1 Ras-GEF domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG3417.
    GeneTreeiENSGT00510000054299.
    OrthoDBiEOG7327XH.

    Family and domain databases

    Gene3Di1.10.840.10. 1 hit.
    InterProiIPR000651. Ras-like_Gua-exchang_fac_N.
    IPR019804. Ras_G-nucl-exch_fac_CS.
    IPR023578. Ras_GEF_dom.
    IPR001895. RasGRF_CDC25.
    [Graphical view]
    PfamiPF00617. RasGEF. 1 hit.
    [Graphical view]
    SMARTiSM00147. RasGEF. 1 hit.
    SM00229. RasGEFN. 1 hit.
    [Graphical view]
    SUPFAMiSSF48366. SSF48366. 1 hit.
    PROSITEiPS00720. RASGEF. 1 hit.
    PS50009. RASGEF_CAT. 1 hit.
    PS50212. RASGEF_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25300-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPKNKYVYI CVEYIYIYFA KIHKQSTLSS DTTKMFVLID NVLAYLLEQD    50
    DLFVTARFAI QGQIVSRRVN KIHISNITDV LLQQFISHTL PYNDNIVPKK 100
    ILDSMRTAVR QLLEATACVS RECPLVKRSQ DIKRARKRLL SDWYRLGADA 150
    NMDAVLLVVN SAWRFLAVWR PFVNSIQHAT QELYQNIAHY LLHGNVNIQR 200
    VTALIQLVMG QDDLLFSMDD VLQEVFRIQL YLNKMLPHNS HKWQKPSPFD 250
    SANLLLNFRD WTTDNALLQE LLLSYPTINK NKHKNHSVPR LIQIWVESYW 300
    QDSETTLKDI LNFWYSHLAE YYEYQELFAD IVQLFINKKR TRQLKIHYIG 350
    LTDKEIEENK PPLDYENLFL QYEIDKTNAN DELCGATDLS DLLFQWKQGE 400
    LLEVEAFALN VSPWSLAKTL TLLESSLYLD IETIEFTRHF KHNDTTIDSV 450
    FTLSNQLSSY VLETTLQQTH TISYWLQVAL SCLYLRNLNS LASIITSLQN 500
    HSIERLSLPI DVKSDHLFQR LKVVVHPNNN YNVYRRTIKH IFHSQLPCVP 550
    FTSLLIRDIT FIRDGNDTFT KDGNNVNMQK FNQITKIVAF AQYLQQKQYE 600
    DIHCSNTTAR SLLGAMIKVH TLYNDNKDRA YQVSIAKVPR LT 642
    Length:642
    Mass (Da):75,046
    Last modified:March 15, 2004 - v2
    Checksum:i55E688DF5AFAB74F
    GO

    Sequence cautioni

    The sequence AAA34462.1 differs from that shown. Reason: Frameshift at positions 60 and 62.
    The sequence CAA45334.1 differs from that shown. Reason: Frameshift at position 38.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101R → P in CAA45334. (PubMed:1789011)Curated
    Sequence conflicti111 – 1111Missing in AAA34462. (PubMed:1905982)Curated
    Sequence conflicti225 – 2251V → D in AAA34460. (PubMed:1905981)Curated
    Sequence conflicti401 – 4011L → P in AAA34462. (PubMed:1905982)Curated
    Sequence conflicti401 – 4011L → P in CAA40230. (PubMed:1964349)Curated
    Sequence conflicti481 – 4811S → A in AAA34462. (PubMed:1905982)Curated
    Sequence conflicti481 – 4811S → A in CAA40230. (PubMed:1964349)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63853 Genomic DNA. Translation: CAA45334.1. Frameshift.
    M68938 Genomic DNA. Translation: AAA34462.1. Frameshift.
    X59720 Genomic DNA. Translation: CAA42305.2.
    M63552 Genomic DNA. Translation: AAA34460.1.
    X56909 Genomic DNA. Translation: CAA40230.1.
    BK006937 Genomic DNA. Translation: DAA07517.1.
    PIRiS19450. BWBYD5.
    RefSeqiNP_009967.2. NM_001178752.1.

    Genome annotation databases

    EnsemblFungiiYCR038C; YCR038C; YCR038C.
    GeneIDi850405.
    KEGGisce:YCR038C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63853 Genomic DNA. Translation: CAA45334.1 . Frameshift.
    M68938 Genomic DNA. Translation: AAA34462.1 . Frameshift.
    X59720 Genomic DNA. Translation: CAA42305.2 .
    M63552 Genomic DNA. Translation: AAA34460.1 .
    X56909 Genomic DNA. Translation: CAA40230.1 .
    BK006937 Genomic DNA. Translation: DAA07517.1 .
    PIRi S19450. BWBYD5.
    RefSeqi NP_009967.2. NM_001178752.1.

    3D structure databases

    ProteinModelPortali P25300.
    SMRi P25300. Positions 411-599.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31021. 16 interactions.
    DIPi DIP-4991N.
    IntActi P25300. 3 interactions.
    MINTi MINT-474246.
    STRINGi 4932.YCR038C.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCR038C ; YCR038C ; YCR038C .
    GeneIDi 850405.
    KEGGi sce:YCR038C.

    Organism-specific databases

    CYGDi YCR038c.
    SGDi S000000634. BUD5.

    Phylogenomic databases

    eggNOGi KOG3417.
    GeneTreei ENSGT00510000054299.
    OrthoDBi EOG7327XH.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29350-MONOMER.

    Miscellaneous databases

    NextBioi 965947.

    Gene expression databases

    Genevestigatori P25300.

    Family and domain databases

    Gene3Di 1.10.840.10. 1 hit.
    InterProi IPR000651. Ras-like_Gua-exchang_fac_N.
    IPR019804. Ras_G-nucl-exch_fac_CS.
    IPR023578. Ras_GEF_dom.
    IPR001895. RasGRF_CDC25.
    [Graphical view ]
    Pfami PF00617. RasGEF. 1 hit.
    [Graphical view ]
    SMARTi SM00147. RasGEF. 1 hit.
    SM00229. RasGEFN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48366. SSF48366. 1 hit.
    PROSITEi PS00720. RASGEF. 1 hit.
    PS50009. RASGEF_CAT. 1 hit.
    PS50212. RASGEF_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The MAT locus revisited within a 9.8 kb fragment of chromosome III containing BUD5 and two new open reading frames."
      Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C., Soustelle C.
      Yeast 7:881-888(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    2. "Functional cloning of BUD5, a CDC25-related gene from S. cerevisiae that can suppress a dominant-negative RAS2 mutant."
      Powers S., Gonzales E., Christensen T., Cubert J., Broek D.
      Cell 65:1225-1231(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The complete DNA sequence of yeast chromosome III."
      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.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Valles G., Volckaerts G.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 110; 401; 481 AND N-TERMINUS.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for bud site selection and interacts with bud formation gene BEM1."
      Chant J., Corrado K., Pringle J.R., Herskowitz I.
      Cell 65:1213-1224(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-642.
      Strain: SP1.
    7. "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."
      Thierry A., Fairhead C., Dujon B.
      Yeast 6:521-534(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-642.
      Strain: ATCC 96604 / S288c / FY1679.
    8. "Genetic evidence for the roles of the bud-site-selection genes BUD5 and BUD2 in control of the Rsr1p (Bud1p) GTPase in yeast."
      Bender A.
      Proc. Natl. Acad. Sci. U.S.A. 90:9926-9929(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "A localized GTPase exchange factor, Bud5, determines the orientation of division axes in yeast."
      Marston A.L., Chen T., Yang M.C., Belhumeur P., Chant J.
      Curr. Biol. 11:803-807(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Overexpression of Bud5p can suppress mutations in the Gsp1p guanine nucleotide exchange factor Prp20p in Saccharomyces cerevisiae."
      Clement M., Lavallee F., Barbes-Morin G., de Repentigny L., Belhumeur P.
      Mol. Genet. Genomics 266:20-27(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GSP1.
    11. "A GDP/GTP exchange factor involved in linking a spatial landmark to cell polarity."
      Kang P.J., Sanson A., Lee B., Park H.-O.
      Science 292:1376-1378(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AXL2.
    12. "Subcellular localization of Axl1, the cell type-specific regulator of polarity."
      Lord M., Inose F., Hiroko T., Hata T., Fujita A., Chant J.
      Curr. Biol. 12:1347-1352(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AXL1.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBUD5_YEAST
    AccessioniPrimary (citable) accession number: P25300
    Secondary accession number(s): D6VR48, Q06729
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: March 15, 2004
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2110 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3