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P05388

- RLA0_HUMAN

UniProt

P05388 - RLA0_HUMAN

Protein

60S acidic ribosomal protein P0

Gene

RPLP0

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    Ribosomal protein P0 is the functional equivalent of E.coli protein L10.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA binding Source: ProtInc
    4. structural constituent of ribosome Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    5. ribosome biogenesis Source: InterPro
    6. RNA metabolic process Source: Reactome
    7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    8. translation Source: UniProtKB
    9. translational elongation Source: Reactome
    10. translational initiation Source: Reactome
    11. translational termination Source: Reactome
    12. viral life cycle Source: Reactome
    13. viral process Source: Reactome
    14. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_1404. Peptide chain elongation.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1986. Eukaryotic Translation Termination.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S acidic ribosomal protein P0
    Alternative name(s):
    60S ribosomal protein L10E
    Gene namesi
    Name:RPLP0
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10371. RPLP0.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    3. cytosol Source: Reactome
    4. cytosolic large ribosomal subunit Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. membrane Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. ribonucleoprotein complex Source: UniProtKB
    9. ribosome Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34772.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31731760S acidic ribosomal protein P0PRO_0000154758Add
    BLAST

    Proteomic databases

    MaxQBiP05388.
    PaxDbiP05388.
    PRIDEiP05388.

    2D gel databases

    REPRODUCTION-2DPAGEP05388.

    PTM databases

    PhosphoSiteiP05388.

    Expressioni

    Gene expression databases

    BgeeiP05388.
    CleanExiHS_RPLP0.
    GenevestigatoriP05388.

    Organism-specific databases

    HPAiHPA003512.

    Interactioni

    Subunit structurei

    P0 forms a pentameric complex by interaction with dimers of P1 and P2. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with Lassa virus Z protein. Interacts with APEX1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAU1O957934EBI-354101,EBI-358174

    Protein-protein interaction databases

    BioGridi112094. 126 interactions.
    IntActiP05388. 36 interactions.
    MINTiMINT-193149.
    STRINGi9606.ENSP00000339027.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J39electron microscopy6.00q5-227[»]
    3J3Belectron microscopy5.00q1-317[»]
    ProteinModelPortaliP05388.
    SMRiP05388. Positions 5-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L10P family.Curated

    Phylogenomic databases

    eggNOGiCOG0244.
    HOVERGENiHBG000711.
    InParanoidiP05388.
    KOiK02941.
    OMAiGILATEM.
    OrthoDBiEOG71K63M.
    PhylomeDBiP05388.
    TreeFamiTF300849.

    Family and domain databases

    InterProiIPR001790. Ribosomal_L10/acidic_P0.
    IPR001813. Ribosomal_L10/L12.
    [Graphical view]
    PfamiPF00428. Ribosomal_60s. 1 hit.
    PF00466. Ribosomal_L10. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05388-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK    50
    AVVLMGKNTM MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD 100
    MLLANKVPAA ARAGAIAPCE VTVPAQNTGL GPEKTSFFQA LGITTKISRG 150
    TIEILSDVQL IKTGDKVGAS EATLLNMLNI SPFSFGLVIQ QVFDNGSIYN 200
    PEVLDITEET LHSRFLEGVR NVASVCLQIG YPTVASVPHS IINGYKRVLA 250
    LSVETDYTFP LAEKVKAFLA DPSAFVAAAP VAAATTAAPA AAAAPAKVEA 300
    KEESEESDED MGFGLFD 317
    Length:317
    Mass (Da):34,274
    Last modified:November 1, 1988 - v1
    Checksum:i255AD25571C51199
    GO
    Isoform 2 (identifier: P05388-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         156-217: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:255
    Mass (Da):27,436
    Checksum:iB10D4073AAA5990A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti246 – 2461K → E in AAH01127. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei156 – 21762Missing in isoform 2. 1 PublicationVSP_055867Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17885 mRNA. Translation: AAA36470.1.
    AC004263 Genomic DNA. Translation: AAC05176.1.
    BC000087 mRNA. Translation: AAH00087.1.
    BC000345 mRNA. Translation: AAH00345.1.
    BC000752 mRNA. Translation: AAH00752.1.
    BC001127 mRNA. Translation: AAH01127.1.
    BC001834 mRNA. Translation: AAH01834.1.
    BC003655 mRNA. Translation: AAH03655.1.
    BC005863 mRNA. Translation: AAH05863.1.
    BC008092 mRNA. Translation: AAH08092.1.
    BC008594 mRNA. Translation: AAH08594.1.
    BC009867 mRNA. Translation: AAH09867.1.
    BC015173 mRNA. Translation: AAH15173.1.
    BC015690 mRNA. Translation: AAH15690.1.
    BC107717 mRNA. Translation: AAI07718.1.
    AB007187 Genomic DNA. Translation: BAA25845.1.
    CCDSiCCDS9193.1.
    PIRiA27125. R5HUP0.
    RefSeqiNP_000993.1. NM_001002.3.
    NP_444505.1. NM_053275.3.
    UniGeneiHs.546285.

    Genome annotation databases

    EnsembliENST00000228306; ENSP00000339027; ENSG00000089157. [P05388-1]
    ENST00000313104; ENSP00000366471; ENSG00000089157. [P05388-2]
    ENST00000392514; ENSP00000376299; ENSG00000089157. [P05388-1]
    ENST00000551150; ENSP00000449328; ENSG00000089157. [P05388-1]
    GeneIDi6175.
    KEGGihsa:6175.
    UCSCiuc001txp.3. human.

    Polymorphism databases

    DMDMi133041.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17885 mRNA. Translation: AAA36470.1 .
    AC004263 Genomic DNA. Translation: AAC05176.1 .
    BC000087 mRNA. Translation: AAH00087.1 .
    BC000345 mRNA. Translation: AAH00345.1 .
    BC000752 mRNA. Translation: AAH00752.1 .
    BC001127 mRNA. Translation: AAH01127.1 .
    BC001834 mRNA. Translation: AAH01834.1 .
    BC003655 mRNA. Translation: AAH03655.1 .
    BC005863 mRNA. Translation: AAH05863.1 .
    BC008092 mRNA. Translation: AAH08092.1 .
    BC008594 mRNA. Translation: AAH08594.1 .
    BC009867 mRNA. Translation: AAH09867.1 .
    BC015173 mRNA. Translation: AAH15173.1 .
    BC015690 mRNA. Translation: AAH15690.1 .
    BC107717 mRNA. Translation: AAI07718.1 .
    AB007187 Genomic DNA. Translation: BAA25845.1 .
    CCDSi CCDS9193.1.
    PIRi A27125. R5HUP0.
    RefSeqi NP_000993.1. NM_001002.3.
    NP_444505.1. NM_053275.3.
    UniGenei Hs.546285.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J39 electron microscopy 6.00 q 5-227 [» ]
    3J3B electron microscopy 5.00 q 1-317 [» ]
    ProteinModelPortali P05388.
    SMRi P05388. Positions 5-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112094. 126 interactions.
    IntActi P05388. 36 interactions.
    MINTi MINT-193149.
    STRINGi 9606.ENSP00000339027.

    PTM databases

    PhosphoSitei P05388.

    Polymorphism databases

    DMDMi 133041.

    2D gel databases

    REPRODUCTION-2DPAGE P05388.

    Proteomic databases

    MaxQBi P05388.
    PaxDbi P05388.
    PRIDEi P05388.

    Protocols and materials databases

    DNASUi 6175.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228306 ; ENSP00000339027 ; ENSG00000089157 . [P05388-1 ]
    ENST00000313104 ; ENSP00000366471 ; ENSG00000089157 . [P05388-2 ]
    ENST00000392514 ; ENSP00000376299 ; ENSG00000089157 . [P05388-1 ]
    ENST00000551150 ; ENSP00000449328 ; ENSG00000089157 . [P05388-1 ]
    GeneIDi 6175.
    KEGGi hsa:6175.
    UCSCi uc001txp.3. human.

    Organism-specific databases

    CTDi 6175.
    GeneCardsi GC12M120634.
    HGNCi HGNC:10371. RPLP0.
    HPAi HPA003512.
    MIMi 180510. gene.
    neXtProti NX_P05388.
    PharmGKBi PA34772.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0244.
    HOVERGENi HBG000711.
    InParanoidi P05388.
    KOi K02941.
    OMAi GILATEM.
    OrthoDBi EOG71K63M.
    PhylomeDBi P05388.
    TreeFami TF300849.

    Enzyme and pathway databases

    Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_1404. Peptide chain elongation.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1986. Eukaryotic Translation Termination.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_9491. Viral mRNA Translation.

    Miscellaneous databases

    ChiTaRSi RPLP0. human.
    GeneWikii RPLP0.
    GenomeRNAii 6175.
    NextBioi 23989.
    PROi P05388.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05388.
    CleanExi HS_RPLP0.
    Genevestigatori P05388.

    Family and domain databases

    InterProi IPR001790. Ribosomal_L10/acidic_P0.
    IPR001813. Ribosomal_L10/L12.
    [Graphical view ]
    Pfami PF00428. Ribosomal_60s. 1 hit.
    PF00466. Ribosomal_L10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly."
      Rich B.E., Steitz J.A.
      Mol. Cell. Biol. 7:4065-4074(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain, Cervix, Colon, Lung, Lymph, Muscle and Pancreas.
    4. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 17-38; 84-92; 135-146; 150-162; 248-264 AND 267-297, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    5. "A map of 75 human ribosomal protein genes."
      Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
      Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 218-310.
    6. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    7. "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
      Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.
      Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRLA0_HUMAN
    AccessioniPrimary (citable) accession number: P05388
    Secondary accession number(s): Q3B7A4, Q9BVK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 164 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Ribosomal proteins
      Ribosomal proteins families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3