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Q01560

- NOP3_YEAST

UniProt

Q01560 - NOP3_YEAST

Protein

Nucleolar protein 3

Gene

NPL3

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 153 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Required for pre-rRNA processing and nuclear import as well as mitochondrial protein targeting. Binds to poly(A).

    GO - Molecular functioni

    1. eukaryotic initiation factor 4G binding Source: SGD
    2. identical protein binding Source: IntAct
    3. mRNA binding Source: SGD
    4. nucleotide binding Source: InterPro
    5. poly(A) binding Source: SGD
    6. protein binding Source: IntAct
    7. RNA polymerase II core binding Source: SGD

    GO - Biological processi

    1. mRNA export from nucleus Source: SGD
    2. mRNA splicing, via spliceosome Source: SGD
    3. negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled Source: SGD
    4. negative regulation of translation Source: SGD
    5. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
    6. rRNA processing Source: UniProtKB-KW
    7. translational termination Source: SGD

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29970-MONOMER.
    ReactomeiREACT_191540. mRNA Splicing - Minor Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleolar protein 3
    Alternative name(s):
    Mitochondrial targeting suppressor 1 protein
    Nuclear polyadenylated RNA-binding protein 1
    Gene namesi
    Name:NPL3
    Synonyms:MTR13, MTS1, NAB1, NOP3
    Ordered Locus Names:YDR432W
    ORF Names:D9461.19
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR432w.
    SGDiS000002840. NPL3.

    Subcellular locationi

    Nucleusnucleolus 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleus Source: SGD
    4. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 414414Nucleolar protein 3PRO_0000081676Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei182 – 1821Phosphoserine1 Publication
    Modified residuei224 – 2241Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ01560.
    PaxDbiQ01560.
    PeptideAtlasiQ01560.

    Expressioni

    Gene expression databases

    GenevestigatoriQ01560.

    Interactioni

    Subunit structurei

    Interacts with RRP6.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-12114,EBI-12114
    HMT1P380749EBI-12114,EBI-8394
    RPL25P044562EBI-12114,EBI-15308
    RSP5P399402EBI-12114,EBI-16219

    Protein-protein interaction databases

    BioGridi32489. 1112 interactions.
    DIPiDIP-6464N.
    IntActiQ01560. 34 interactions.
    MINTiMINT-600838.
    STRINGi4932.YDR432W.

    Structurei

    Secondary structure

    1
    414
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi125 – 1295
    Helixi138 – 1458
    Turni146 – 1483
    Beta strandi153 – 1575
    Beta strandi160 – 1645
    Helixi168 – 17811
    Beta strandi189 – 1924
    Beta strandi200 – 2056
    Helixi213 – 22311
    Beta strandi228 – 2314
    Beta strandi236 – 2383
    Beta strandi241 – 2477
    Helixi248 – 25710
    Beta strandi261 – 2633
    Beta strandi266 – 2738

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JVONMR-A116-201[»]
    2JVRNMR-A193-282[»]
    2OSQNMR-A121-194[»]
    2OSRNMR-A194-280[»]
    ProteinModelPortaliQ01560.
    SMRiQ01560. Positions 121-280.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01560.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini125 – 19571RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini200 – 27576RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi280 – 398119Arg/Gly-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RRM GAR family.Curated
    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    GeneTreeiENSGT00700000104103.
    KOiK14651.
    OMAiPEGCSWQ.
    OrthoDBiEOG7QVMDQ.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q01560-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEAQETHVE QLPESVVDAP VEEQHQEPPQ APDAPQEPQV PQESAPQESA    50
    PQEPPAPQEQ NDVPPPSNAP IYEGEESHSV QDYQEAHQHH QPPEPQPYYP 100
    PPPPGEHMHG RPPMHHRQEG ELSNTRLFVR PFPLDVQESE LNEIFGPFGP 150
    MKEVKILNGF AFVEFEEAES AAKAIEEVHG KSFANQPLEV VYSKLPAKRY 200
    RITMKNLPEG CSWQDLKDLA RENSLETTFS SVNTRDFDGT GALEFPSEEI 250
    LVEALERLNN IEFRGSVITV ERDDNPPPIR RSNRGGFRGR GGFRGGFRGG 300
    FRGGFSRGGF GGPRGGFGGP RGGYGGYSRG GYGGYSRGGY GGSRGGYDSP 350
    RGGYDSPRGG YSRGGYGGPR NDYGPPRGSY GGSRGGYDGP RGDYGPPRDA 400
    YRTRDAPRER SPTR 414
    Length:414
    Mass (Da):45,407
    Last modified:July 1, 1993 - v1
    Checksum:i024439E4B6578787
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66019 Genomic DNA. Translation: CAA46817.1.
    M86731 Genomic DNA. Translation: AAA34818.1.
    X70951 Genomic DNA. Translation: CAA50291.1.
    U33007 Genomic DNA. Translation: AAB64865.1.
    BK006938 Genomic DNA. Translation: DAA12270.1.
    PIRiJN0866.
    RefSeqiNP_010720.3. NM_001180740.3.

    Genome annotation databases

    EnsemblFungiiYDR432W; YDR432W; YDR432W.
    GeneIDi852042.
    KEGGisce:YDR432W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66019 Genomic DNA. Translation: CAA46817.1 .
    M86731 Genomic DNA. Translation: AAA34818.1 .
    X70951 Genomic DNA. Translation: CAA50291.1 .
    U33007 Genomic DNA. Translation: AAB64865.1 .
    BK006938 Genomic DNA. Translation: DAA12270.1 .
    PIRi JN0866.
    RefSeqi NP_010720.3. NM_001180740.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JVO NMR - A 116-201 [» ]
    2JVR NMR - A 193-282 [» ]
    2OSQ NMR - A 121-194 [» ]
    2OSR NMR - A 194-280 [» ]
    ProteinModelPortali Q01560.
    SMRi Q01560. Positions 121-280.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32489. 1112 interactions.
    DIPi DIP-6464N.
    IntActi Q01560. 34 interactions.
    MINTi MINT-600838.
    STRINGi 4932.YDR432W.

    Proteomic databases

    MaxQBi Q01560.
    PaxDbi Q01560.
    PeptideAtlasi Q01560.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR432W ; YDR432W ; YDR432W .
    GeneIDi 852042.
    KEGGi sce:YDR432W.

    Organism-specific databases

    CYGDi YDR432w.
    SGDi S000002840. NPL3.

    Phylogenomic databases

    eggNOGi COG0724.
    GeneTreei ENSGT00700000104103.
    KOi K14651.
    OMAi PEGCSWQ.
    OrthoDBi EOG7QVMDQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29970-MONOMER.
    Reactomei REACT_191540. mRNA Splicing - Minor Pathway.

    Miscellaneous databases

    EvolutionaryTracei Q01560.
    NextBioi 970290.
    PROi Q01560.

    Gene expression databases

    Genevestigatori Q01560.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NOP3 is an essential yeast protein which is required for pre-rRNA processing."
      Russell I.D., Tollervey D.
      J. Cell Biol. 119:737-747(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast."
      Bossie M.A., Dehoratious C., Barcelo G., Silver P.
      Mol. Biol. Cell 3:875-893(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding protein involved in mitochondrial protein targeting."
      Ellis E.M., Reid G.A.
      Gene 132:175-183(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae."
      Wilson S.M., Datar K.V., Paddy M.R., Swedlow J.R., Swanson M.S.
      J. Cell Biol. 127:1173-1184(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, BINDING TO POLYADENYLATED RNA.
    7. "A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p."
      Burkard K.T.D., Butler J.S.
      Mol. Cell. Biol. 20:604-616(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RRP6.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "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-182 AND SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNOP3_YEAST
    AccessioniPrimary (citable) accession number: Q01560
    Secondary accession number(s): D6VT60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 153 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 78700 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3