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Q12754

- RRP12_YEAST

UniProt

Q12754 - RRP12_YEAST

Protein

Ribosomal RNA-processing protein 12

Gene

RRP12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    In association with GSP1, required for nuclear export of both pre-40S and pre-60S ribosomal subunits. Required for the late maturation of the 18S and 5.8S rRNA of the pre-40S ribosomes and for maturation of the 25S and 5.8S rRNA of the pre-60S ribosomes.1 Publication

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
    2. ribosome biogenesis Source: SGD

    Keywords - Biological processi

    Ribosome biogenesis

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33931-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal RNA-processing protein 12
    Gene namesi
    Name:RRP12
    Ordered Locus Names:YPL012W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPL012w.
    SGDiS000005933. RRP12.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB-SubCell
    2. nucleus Source: SGD
    3. ribosome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12281228Ribosomal RNA-processing protein 12PRO_0000270563Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1059 – 10591Phosphoserine1 Publication
    Modified residuei1067 – 10671Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12754.
    PaxDbiQ12754.
    PeptideAtlasiQ12754.
    PRIDEiQ12754.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12754.

    Interactioni

    Subunit structurei

    Interacts with GSP1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EBP2P360491EBI-30678,EBI-6289

    Protein-protein interaction databases

    BioGridi36165. 115 interactions.
    DIPiDIP-6497N.
    IntActiQ12754. 49 interactions.
    MINTiMINT-639557.
    STRINGi4932.YPL012W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12754.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RRP12 family.Curated

    Phylogenomic databases

    eggNOGiNOG149372.
    GeneTreeiENSGT00390000013106.
    HOGENOMiHOG000164239.
    KOiK14794.
    OMAiLQPLLTW.
    OrthoDBiEOG7WDN9V.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR012978. Uncharacterised_NUC173.
    [Graphical view]
    PfamiPF08161. NUC173. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q12754-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQDKVAFLL ELEDKLAKIR SQVNSKLENQ KHIAIILTAV EENIAGQATN     50
    DVSKNIVNYI ISFMSLLDQA VDPSTHEIKD IQLASSSTYL LDLIFHYSPK 100
    VLLRSKFSEI LTKIAPCITA EKANAPLIRA AIGCLESLLI AQDAQAWNNT 150
    YDLNVTPKRG LQGILELSLD VRPKVRKRAL DAVHAVLLNP PVAPTAEHVA 200
    AVFVADFCDK QLAGILNDLS NLSNKQLKAQ KTKEDINASV MRSLRLITSV 250
    VSTGQWPSSQ IEPLCDVLLG VTKSSEQYLV SASFECFESM FKTMAETTIS 300
    SGLAENKYLR VLDTIFALKP SNVDTLLTKS WIAVVIKGMS TYATHQPLKA 350
    LRKIPGVFHI MCTYLASETP EVYQAASQCL ISILSESVKD DLLLYTPSVD 400
    EKVFKNVDEI ISQIAKTFID FLSIRYSHCS REILKILVAA FNKFRYRSNP 450
    HFLKSLKIVD TWRVNEEQFM DLRNEIELVI GASISAMGPE MILAEAPLNL 500
    DNPSSERPGR AWLLPLIRDY TKNANLATFQ NELAPYIKSF QSKFDKVPEE 550
    SIQLRVFQTI VDQIWSTLPR FCELPMDLRE SFTDEFASEL SSLLYSEVEL 600
    RTTICHALKV LAESNVSYAE ESSSHNVLLL QRFPISEAQK NIEYLSTKST 650
    NLLAVLFNVY TQTTPNARSY ILETIDQYLK ITSKEDLEKT FNNVCGLLKN 700
    SMNEESSGNV NKEKKKPQLT ATLLDLIICM ITYLPVSSYS ALFSMFSLTV 750
    NSADALIQKR AYRIITKLSE LKSGSTAVAQ FISDIENVMV DSASSVQTSA 800
    KAARLTAIKT IVELLPLDHL DFIVRTVAEV ILSTKDVNEK SRETAFDTLI 850
    CMGRKMNEPN GIIKLFQIPG YDPTTPDQSS SISEFFKIIS AGLIGESQHM 900
    VSSSITGYAC LVFEFKNELD SGILMDIYDT IELYLTSNSR EIVKSAIGFT 950
    KVCVLGLPEE LMRPKVPELL LKLLRWSHEH TGHFKAKVKH IIERLIRRFG 1000
    YDYIEANFPE EDRRLLTNIR KMRNRNKRKD EEVTTGVSDV AATKGSRFMS 1050
    AFDEAVYGSD EENDNGSDQE ENVAGGKMKN GAKQFIVESG DNPLDLLDSQ 1100
    TLAHISSTRP KKFNKNQNRA RFNDDAFNFD SEGKLVVKGQ PKPSTNVDDP 1150
    LSAVTSGINA YLEAVKSGPV RGQRNKLKFR KNGKDSDEFG DDDDGEKDSR 1200
    LMRGRVNQGN KIGKHNKKGP KFKSRKKL 1228
    Length:1,228
    Mass (Da):137,509
    Last modified:November 1, 1996 - v1
    Checksum:i92333BCD53CB095F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33335 Genomic DNA. Translation: AAB68093.1.
    Z71255 Genomic DNA. Translation: CAA95029.1.
    Z48483 Genomic DNA. Translation: CAA88374.1.
    BK006949 Genomic DNA. Translation: DAA11416.1.
    PIRiS59681.
    RefSeqiNP_015313.1. NM_001183826.1.

    Genome annotation databases

    EnsemblFungiiYPL012W; YPL012W; YPL012W.
    GeneIDi856095.
    KEGGisce:YPL012W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33335 Genomic DNA. Translation: AAB68093.1 .
    Z71255 Genomic DNA. Translation: CAA95029.1 .
    Z48483 Genomic DNA. Translation: CAA88374.1 .
    BK006949 Genomic DNA. Translation: DAA11416.1 .
    PIRi S59681.
    RefSeqi NP_015313.1. NM_001183826.1.

    3D structure databases

    ProteinModelPortali Q12754.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36165. 115 interactions.
    DIPi DIP-6497N.
    IntActi Q12754. 49 interactions.
    MINTi MINT-639557.
    STRINGi 4932.YPL012W.

    Proteomic databases

    MaxQBi Q12754.
    PaxDbi Q12754.
    PeptideAtlasi Q12754.
    PRIDEi Q12754.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL012W ; YPL012W ; YPL012W .
    GeneIDi 856095.
    KEGGi sce:YPL012W.

    Organism-specific databases

    CYGDi YPL012w.
    SGDi S000005933. RRP12.

    Phylogenomic databases

    eggNOGi NOG149372.
    GeneTreei ENSGT00390000013106.
    HOGENOMi HOG000164239.
    KOi K14794.
    OMAi LQPLLTW.
    OrthoDBi EOG7WDN9V.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33931-MONOMER.

    Miscellaneous databases

    NextBioi 981131.
    PROi Q12754.

    Gene expression databases

    Genevestigatori Q12754.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR012978. Uncharacterised_NUC173.
    [Graphical view ]
    Pfami PF08161. NUC173. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [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. "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes."
      Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.
      EMBO J. 22:1370-1380(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "A pre-ribosome-associated HEAT-repeat protein is required for export of both ribosomal subunits."
      Oeffinger M., Dlakic M., Tollervey D.
      Genes Dev. 18:196-209(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GSP1, SUBCELLULAR LOCATION.
    7. "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-1067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    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 SER-1067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-1059 AND SER-1067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRRP12_YEAST
    AccessioniPrimary (citable) accession number: Q12754
    Secondary accession number(s): D6W400, Q7LH12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 104 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 8170 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 XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3