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P41812

- POP1_YEAST

UniProt

P41812 - POP1_YEAST

Protein

Ribonucleases P/MRP protein subunit POP1

Gene

POP1

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 108 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.2 Publications

    Catalytic activityi

    Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

    GO - Molecular functioni

    1. ribonuclease P activity Source: UniProtKB-EC
    2. RNA binding Source: SGD

    GO - Biological processi

    1. intronic box C/D snoRNA processing Source: SGD
    2. mRNA cleavage Source: SGD
    3. RNA phosphodiester bond hydrolysis Source: GOC
    4. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    5. rRNA processing Source: SGD
    6. tRNA 5'-leader removal Source: InterPro
    7. tRNA processing Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    rRNA processing, tRNA processing

    Enzyme and pathway databases

    BioCyciYEAST:YNL221C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleases P/MRP protein subunit POP1 (EC:3.1.26.5)
    Alternative name(s):
    RNA-processing protein POP1
    RNases P/MRP 100.4 kDa subunit
    Gene namesi
    Name:POP1
    Ordered Locus Names:YNL221C
    ORF Names:N1285
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL221c.
    SGDiS000005165. POP1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleolar ribonuclease P complex Source: SGD
    3. ribonuclease MRP complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 875875Ribonucleases P/MRP protein subunit POP1PRO_0000058514Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei524 – 5241Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP41812.
    PaxDbiP41812.
    PeptideAtlasiP41812.
    PRIDEiP41812.

    Expressioni

    Gene expression databases

    GenevestigatoriP41812.

    Interactioni

    Subunit structurei

    Component of nuclear RNase P and RNase MRP complexes. RNase P consists of an RNA moiety and at least 9 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP complex consists of an RNA moiety and at least 10 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with the RNase P complex.3 Publications

    Protein-protein interaction databases

    BioGridi35615. 29 interactions.
    DIPiDIP-4284N.
    IntActiP41812. 10 interactions.
    MINTiMINT-472608.
    STRINGi4932.YNL221C.

    Structurei

    3D structure databases

    ProteinModelPortaliP41812.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG297409.
    HOGENOMiHOG000247847.
    KOiK01164.
    OMAiPPVMVED.
    OrthoDBiEOG7X3R0Z.

    Family and domain databases

    InterProiIPR012590. POPLD.
    IPR009723. RNase_P/MRP_POP1.
    [Graphical view]
    PfamiPF06978. POP1. 1 hit.
    PF08170. POPLD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P41812-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGSLSRGNG GKKVLNKNQL LKRNRIRNAR SIRAEAVAAS STKTGTPSDL    50
    SESGSKLNVD QFISSRQFEV KQLQLAMHNS KAASSTRIFQ ALPRKLRRRT 100
    ASHNVRRIPK RMRNRALREM RKSDQQDVLK GSSASSRKAH GLNAKQLYKA 150
    RMSIKLLRLA SKSTSMKLSM PPEVTSSNCH VRQKIKTLKR MIKESSTANP 200
    NIKLLNNRMG SYDCTGVNEL APIPKGRVKY TKRQKHFAWL PTHIWNAKRS 250
    HMMKRWGYQM VWAPTQKCFK LTHRLGGDTC SSDGALCMDS SYIGTIIVKD 300
    KSNDSEGDFL KSIIGKLTAE RANLRKYREG QVLFQGLIYS FNEENGEDST 350
    KPLGPCDVFW VQKDTAIIRL HPSIYTQVFN ILLQHKEKLT VQDCRYSLAS 400
    VTLKGAKALE SLASCLRSTE YSKSFEQFKM VSMITDHNAL PQRCTFAFEA 450
    IDPRHLAAPK KLNDSQRKTV NSDDILSLHE NYPQDEINAV FNELCDPESR 500
    TQSYNNQNTL KEISARRYKL LTATPNSINK TTVPFKESDD PSIPLVIIRR 550
    LKTRDWIVVL PWFWLLPLWH LLNRIPRMYH IGLRQFQQIQ YENKQLYFPD 600
    DYPFTQLGYI ENSFYKKEAS KTKWDRKPMG KRINFEKIKD IHNTKLPAYS 650
    GEIGDFFSSD WRFLQILRNG IDYLQRNDKT LELMDSKKTG QFNAQGVRDI 700
    NCVNDVLEFC KDYEAKTKAM SLSIEENIPV ALCKNRKCQF RTPDSISVNS 750
    SSFSLTFFPR CIIAVSCTLL ERGHPKDNAR IYQVPEKDLE HWLQLAKGVY 800
    RPNGRKDHDL KIPLPEVHDL IGFITSGTYH LNCGNGMGIG FIDHHAAIRQ 850
    PTRYVLIRNV GTNTYRLGEW SKISV 875
    Length:875
    Mass (Da):100,395
    Last modified:November 1, 1995 - v1
    Checksum:iE41EA9FFD6262FA9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80358 Genomic DNA. Translation: CAA56589.1.
    Z71497 Genomic DNA. Translation: CAA96124.1.
    BK006947 Genomic DNA. Translation: DAA10335.1.
    PIRiA53901.
    RefSeqiNP_014178.1. NM_001183059.1.

    Genome annotation databases

    EnsemblFungiiYNL221C; YNL221C; YNL221C.
    GeneIDi855500.
    KEGGisce:YNL221C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80358 Genomic DNA. Translation: CAA56589.1 .
    Z71497 Genomic DNA. Translation: CAA96124.1 .
    BK006947 Genomic DNA. Translation: DAA10335.1 .
    PIRi A53901.
    RefSeqi NP_014178.1. NM_001183059.1.

    3D structure databases

    ProteinModelPortali P41812.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35615. 29 interactions.
    DIPi DIP-4284N.
    IntActi P41812. 10 interactions.
    MINTi MINT-472608.
    STRINGi 4932.YNL221C.

    Proteomic databases

    MaxQBi P41812.
    PaxDbi P41812.
    PeptideAtlasi P41812.
    PRIDEi P41812.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL221C ; YNL221C ; YNL221C .
    GeneIDi 855500.
    KEGGi sce:YNL221C.

    Organism-specific databases

    CYGDi YNL221c.
    SGDi S000005165. POP1.

    Phylogenomic databases

    eggNOGi NOG297409.
    HOGENOMi HOG000247847.
    KOi K01164.
    OMAi PPVMVED.
    OrthoDBi EOG7X3R0Z.

    Enzyme and pathway databases

    BioCyci YEAST:YNL221C-MONOMER.

    Miscellaneous databases

    NextBioi 979496.
    PROi P41812.

    Gene expression databases

    Genevestigatori P41812.

    Family and domain databases

    InterProi IPR012590. POPLD.
    IPR009723. RNase_P/MRP_POP1.
    [Graphical view ]
    Pfami PF06978. POP1. 1 hit.
    PF08170. POPLD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins."
      Lygerou Z., Mitchell P., Petfalski E., Seraphin B., Tollervey D.
      Genes Dev. 8:1423-1433(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
      Strain: BSY295.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP."
      Chamberlain J.R., Lee Y., Lane W.S., Engelke D.R.
      Genes Dev. 12:1678-1690(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE RNASE P COMPLEX BY MASS SPECTROMETRY.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component."
      Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.
      J. Biol. Chem. 280:11352-11360(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.
    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-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPOP1_YEAST
    AccessioniPrimary (citable) accession number: P41812
    Secondary accession number(s): D6W0W9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 108 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 846 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3