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P25299

- RNA15_YEAST

UniProt

P25299 - RNA15_YEAST

Protein

mRNA 3'-end-processing protein RNA15

Gene

RNA15

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 120 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements.2 Publications

    GO - Molecular functioni

    1. mRNA binding Source: SGD
    2. nucleotide binding Source: InterPro
    3. protein binding Source: IntAct
    4. protein heterodimerization activity Source: SGD

    GO - Biological processi

    1. mRNA cleavage Source: SGD
    2. mRNA polyadenylation Source: SGD

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30555-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    mRNA 3'-end-processing protein RNA15
    Gene namesi
    Name:RNA15
    Ordered Locus Names:YGL044C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL044c.
    SGDiS000003012. RNA15.

    Subcellular locationi

    GO - Cellular componenti

    1. mRNA cleavage factor complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 296296mRNA 3'-end-processing protein RNA15PRO_0000081807Add
    BLAST

    Proteomic databases

    MaxQBiP25299.
    PaxDbiP25299.
    PeptideAtlasiP25299.

    Expressioni

    Gene expression databases

    GenevestigatoriP25299.

    Interactioni

    Subunit structurei

    Component of the CFIA complex, which is composed of RNA14, RNA15, PCF11 and CLP1. Interacts directly with RNA14. Interacts with polyadenylate-binding protein PAB1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PCF11P390819EBI-15640,EBI-12980
    RNA14P252988EBI-15640,EBI-15632
    SUB1P540002EBI-15640,EBI-18492

    Protein-protein interaction databases

    BioGridi33204. 115 interactions.
    DIPiDIP-1489N.
    IntActiP25299. 11 interactions.
    MINTiMINT-389896.
    STRINGi4932.YGL044C.

    Structurei

    Secondary structure

    1
    296
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 247
    Helixi31 – 399
    Beta strandi44 – 485
    Turni53 – 553
    Beta strandi60 – 689
    Helixi69 – 7911
    Beta strandi85 – 873
    Beta strandi90 – 934
    Helixi99 – 1013
    Helixi139 – 1435
    Turni156 – 1583
    Helixi161 – 17010
    Helixi174 – 19017
    Helixi192 – 20110
    Helixi203 – 21614
    Beta strandi217 – 2193
    Helixi221 – 2244
    Turni225 – 2273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KM8NMR-B14-97[»]
    2L9BNMR-A127-232[»]
    2X1AX-ray2.05A16-111[»]
    2X1BX-ray1.80A16-111[»]
    2X1FX-ray1.60A16-103[»]
    ProteinModelPortaliP25299.
    SMRiP25299. Positions 16-101, 138-228.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25299.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 9679RRMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi104 – 1096Poly-Gln
    Compositional biasi111 – 12818Asn-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG246793.
    GeneTreeiENSGT00750000117707.
    HOGENOMiHOG000247912.
    KOiK14407.
    OMAiQILDLCS.
    OrthoDBiEOG706125.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR026896. CSTF_C.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF14304. CSTF_C. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25299-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNRQSGVNAG VQNNPPSRVV YLGSIPYDQT EEQILDLCSN VGPVINLKMM    50
    FDPQTGRSKG YAFIEFRDLE SSASAVRNLN GYQLGSRFLK CGYSSNSDIS 100
    GVSQQQQQQY NNINGNNNNN GNNNNNSNGP DFQNSGNANF LSQKFPELPS 150
    GIDVNINMTT PAMMISSELA KKPKEVQLKF LQKFQEWTRA HPEDAVSLLE 200
    LCPQLSFVTA ELLLTNGICK VDDLIPLASR PQEEASATNN NSVNEVVDPA 250
    VLNKQKELLK QVLQLNDSQI SILPDDERMA IWDLKQKALR GEFGAF 296
    Length:296
    Mass (Da):32,791
    Last modified:May 1, 1992 - v1
    Checksum:i10053B8648A71ECB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73462 Genomic DNA. Translation: AAA34984.1.
    Z72566 Genomic DNA. Translation: CAA96746.1.
    BK006941 Genomic DNA. Translation: DAA08056.1.
    PIRiB40257.
    RefSeqiNP_011471.1. NM_001180909.1.

    Genome annotation databases

    EnsemblFungiiYGL044C; YGL044C; YGL044C.
    GeneIDi852838.
    KEGGisce:YGL044C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73462 Genomic DNA. Translation: AAA34984.1 .
    Z72566 Genomic DNA. Translation: CAA96746.1 .
    BK006941 Genomic DNA. Translation: DAA08056.1 .
    PIRi B40257.
    RefSeqi NP_011471.1. NM_001180909.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KM8 NMR - B 14-97 [» ]
    2L9B NMR - A 127-232 [» ]
    2X1A X-ray 2.05 A 16-111 [» ]
    2X1B X-ray 1.80 A 16-111 [» ]
    2X1F X-ray 1.60 A 16-103 [» ]
    ProteinModelPortali P25299.
    SMRi P25299. Positions 16-101, 138-228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33204. 115 interactions.
    DIPi DIP-1489N.
    IntActi P25299. 11 interactions.
    MINTi MINT-389896.
    STRINGi 4932.YGL044C.

    Proteomic databases

    MaxQBi P25299.
    PaxDbi P25299.
    PeptideAtlasi P25299.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL044C ; YGL044C ; YGL044C .
    GeneIDi 852838.
    KEGGi sce:YGL044C.

    Organism-specific databases

    CYGDi YGL044c.
    SGDi S000003012. RNA15.

    Phylogenomic databases

    eggNOGi NOG246793.
    GeneTreei ENSGT00750000117707.
    HOGENOMi HOG000247912.
    KOi K14407.
    OMAi QILDLCS.
    OrthoDBi EOG706125.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30555-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P25299.
    NextBioi 972414.

    Gene expression databases

    Genevestigatori P25299.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR026896. CSTF_C.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF14304. CSTF_C. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein."
      Minvielle-Sebastia L., Winsor B., Bonneaud N., Lacroute F.
      Mol. Cell. Biol. 11:3075-3087(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 28383 / FL100 / VTT C-80102.
    2. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
      Feuermann M., de Montigny J., Potier S., Souciet J.-L.
      Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor."
      Minvielle-Sebastia L., Preker P.J., Keller W.
      Science 266:1702-1705(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro."
      Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F.
      Mol. Cell. Biol. 17:3694-3701(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAB1.
    7. "Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I."
      Gross S., Moore C.
      Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE CFIA COMPLEX.
    8. "Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3'-end formation."
      Gross S., Moore C.L.
      Mol. Cell. Biol. 21:8045-8055(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    9. "Purification of the Saccharomyces cerevisiae cleavage/polyadenylation factor I. Separation into two components that are required for both cleavage and polyadenylation of mRNA 3' ends."
      Kessler M.M., Zhao J., Moore C.L.
      J. Biol. Chem. 271:27167-27175(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPOSITION OF THE CFIA COMPLEX.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRNA15_YEAST
    AccessioniPrimary (citable) accession number: P25299
    Secondary accession number(s): D6VU95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 120 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 6350 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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3