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P25555

- GBP2_YEAST

UniProt

P25555 - GBP2_YEAST

Protein

Single-strand telomeric DNA-binding protein GBP2

Gene

GBP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    Binds single-stranded telomeric sequences of the type (TG[1-3])n in vitro. Also binds to RNA. Influences the localization of RAP1 in the nuclei. Involved in modulating telomere length.

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. RNA binding Source: SGD
    3. telomeric DNA binding Source: SGD

    GO - Biological processi

    1. nuclear mRNA surveillance Source: SGD
    2. poly(A)+ mRNA export from nucleus Source: SGD
    3. telomere maintenance Source: SGD

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29280-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Single-strand telomeric DNA-binding protein GBP2
    Short name:
    G-strand-binding protein 2
    Alternative name(s):
    RAP1 localization factor 6
    Gene namesi
    Name:GBP2
    Synonyms:RLF6
    Ordered Locus Names:YCL011C
    ORF Names:YCL11C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCL011c.
    SGDiS000000517. GBP2.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome, telomeric region Source: UniProtKB-SubCell
    2. cytoplasmic stress granule Source: SGD
    3. cytosol Source: SGD
    4. nucleus Source: SGD

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Single-strand telomeric DNA-binding protein GBP2PRO_0000081596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP25555.
    PaxDbiP25555.
    PeptideAtlasiP25555.

    Expressioni

    Gene expression databases

    GenevestigatoriP25555.

    Interactioni

    Protein-protein interaction databases

    BioGridi30970. 121 interactions.
    DIPiDIP-2735N.
    IntActiP25555. 46 interactions.
    MINTiMINT-481140.
    STRINGi4932.YCL011C.

    Structurei

    3D structure databases

    ProteinModelPortaliP25555.
    SMRiP25555. Positions 122-296.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini122 – 19877RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini219 – 29678RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 42678RRM 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    GeneTreeiENSGT00410000025635.
    HOGENOMiHOG000111155.
    OMAiISMEAIN.
    OrthoDBiEOG76TB3G.

    Family and domain databases

    Gene3Di3.30.70.330. 3 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 3 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25555-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERELGMYGN DRSRSRSPVR RRLSDDRDRY DDYNDSSSNN GNGSRRQRRD    50
    RGSRFNDRYD QSYGGSRYHD DRNWPPRRGG RGRGGSRSFR GGRGGGRGRT 100
    LGPIVERDLE RQFDATKRNF ENSIFVRNLT FDCTPEDLKE LFGTVGEVVE 150
    ADIITSKGHH RGMGTVEFTK NESVQDAISK FDGALFMDRK LMVRQDNPPP 200
    EAAKEFSKKA TREEIDNGFE VFIINLPYSM NWQSLKDMFK ECGHVLRADV 250
    ELDFNGFSRG FGSVIYPTED EMIRAIDTFN GMEVEGRVLE VREGRFNKRK 300
    NNDRYNQRRE DLEDTRGTEP GLAQDAAVHI DETAAKFTEG VNPGGDRNCF 350
    IYCSNLPFST ARSDLFDLFG PIGKINNAEL KPQENGQPTG VAVVEYENLV 400
    DADFCIQKLN NYNYGGCSLQ ISYARRD 427
    Length:427
    Mass (Da):48,729
    Last modified:May 1, 1992 - v1
    Checksum:i5341D7A0E07F208C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAA42348.1.
    AY692807 Genomic DNA. Translation: AAT92826.1.
    BK006937 Genomic DNA. Translation: DAA07470.1.
    PIRiS19338.
    RefSeqiNP_009916.1. NM_001178660.1.

    Genome annotation databases

    EnsemblFungiiYCL011C; YCL011C; YCL011C.
    GeneIDi850346.
    KEGGisce:YCL011C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAA42348.1 .
    AY692807 Genomic DNA. Translation: AAT92826.1 .
    BK006937 Genomic DNA. Translation: DAA07470.1 .
    PIRi S19338.
    RefSeqi NP_009916.1. NM_001178660.1.

    3D structure databases

    ProteinModelPortali P25555.
    SMRi P25555. Positions 122-296.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 30970. 121 interactions.
    DIPi DIP-2735N.
    IntActi P25555. 46 interactions.
    MINTi MINT-481140.
    STRINGi 4932.YCL011C.

    Proteomic databases

    MaxQBi P25555.
    PaxDbi P25555.
    PeptideAtlasi P25555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCL011C ; YCL011C ; YCL011C .
    GeneIDi 850346.
    KEGGi sce:YCL011C.

    Organism-specific databases

    CYGDi YCL011c.
    SGDi S000000517. GBP2.

    Phylogenomic databases

    eggNOGi COG0724.
    GeneTreei ENSGT00410000025635.
    HOGENOMi HOG000111155.
    OMAi ISMEAIN.
    OrthoDBi EOG76TB3G.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29280-MONOMER.

    Miscellaneous databases

    NextBioi 965800.

    Gene expression databases

    Genevestigatori P25555.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 3 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Isolation and characterization of two Saccharomyces cerevisiae genes that encode proteins that bind to (TG1-3)n single strand telomeric DNA in vitro."
      Lin J.-J., Zakian V.A.
      Nucleic Acids Res. 22:4906-4913(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "A class of single-stranded telomeric DNA-binding proteins required for Rap1p localization in yeast nuclei."
      Konkel L.C., Enomoto S., Chamberlain E., McCune-Zierath P., Iyadurai S.J.P., Berman J.
      Proc. Natl. Acad. Sci. U.S.A. 92:5558-5562(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "Exposure of single-stranded telomeric DNA causes G2/M cell cycle arrest in Saccharomyces cerevisiae."
      Pang T.-L., Wang C.-Y., Hsu C.-L., Chen M.-Y., Lin J.-J.
      J. Biol. Chem. 278:9318-9321(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "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 THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGBP2_YEAST
    AccessioniPrimary (citable) accession number: P25555
    Secondary accession number(s): D6VR01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 129 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 2540 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