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P05386

- RLA1_HUMAN

UniProt

P05386 - RLA1_HUMAN

Protein

60S acidic ribosomal protein P1

Gene

RPLP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Plays an important role in the elongation step of protein synthesis.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. RNA binding Source: ProtInc
    3. 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. RNA metabolic process Source: Reactome
    6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    7. translation Source: UniProtKB
    8. translational elongation Source: Reactome
    9. translational initiation Source: Reactome
    10. translational termination Source: Reactome
    11. viral life cycle Source: Reactome
    12. viral process Source: Reactome
    13. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    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 P1
    Gene namesi
    Name:RPLP1
    Synonyms:RRP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:10372. RPLP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. cytosolic large ribosomal subunit Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34775.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 11411360S acidic ribosomal protein P1PRO_0000157686Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei101 – 1011Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05386.
    PaxDbiP05386.
    PRIDEiP05386.

    PTM databases

    PhosphoSiteiP05386.

    Expressioni

    Gene expression databases

    BgeeiP05386.
    CleanExiHS_RPLP1.
    HS_RRP1.
    GenevestigatoriP05386.

    Organism-specific databases

    HPAiHPA003368.

    Interactioni

    Subunit structurei

    Heterodimer with RPLP2 at the lateral ribosomal stalk of the large ribosomal subunit.1 Publication

    Protein-protein interaction databases

    BioGridi112095. 96 interactions.
    IntActiP05386. 50 interactions.
    MINTiMINT-193188.
    STRINGi9606.ENSP00000346037.

    Structurei

    Secondary structure

    1
    114
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1916
    Helixi25 – 3511
    Helixi42 – 509
    Turni51 – 533
    Helixi56 – 605
    Turni61 – 644

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LBFNMR-A1-69[»]
    3J3Belectron microscopy5.00s/t1-114[»]
    4BEHNMR-A1-114[»]
    ProteinModelPortaliP05386.
    SMRiP05386. Positions 1-114.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L12P family.Curated

    Phylogenomic databases

    eggNOGiCOG2058.
    HOGENOMiHOG000229898.
    HOVERGENiHBG002291.
    InParanoidiP05386.
    KOiK02942.
    OMAiTSELACI.
    OrthoDBiEOG7M0NVC.
    PhylomeDBiP05386.
    TreeFamiTF312932.

    Family and domain databases

    HAMAPiMF_01478. Ribosomal_L12_arch.
    InterProiIPR001813. Ribosomal_L10/L12.
    IPR027534. Ribosomal_L12.
    [Graphical view]
    PfamiPF00428. Ribosomal_60s. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05386-1) [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

    MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVNVE PFWPGLFAKA    50
    LANVNIGSLI CNVGAGGPAP AAGAAPAGGP APSTAAAPAE EKKVEAKKEE 100
    SEESDDDMGF GLFD 114
    Length:114
    Mass (Da):11,514
    Last modified:November 1, 1988 - v1
    Checksum:i4C282AB8DCA079C8
    GO
    Isoform 2 (identifier: P05386-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         25-49: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:89
    Mass (Da):8,804
    Checksum:iB84B9045B930348B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei25 – 4925Missing in isoform 2. 1 PublicationVSP_045244Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17886 mRNA. Translation: AAA36471.1.
    AB061836 Genomic DNA. Translation: BAB79474.1.
    AC027237 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77845.1.
    BC003369 mRNA. Translation: AAH03369.1.
    BC007590 mRNA. Translation: AAH07590.1.
    CD388103 mRNA. No translation available.
    CCDSiCCDS10233.1. [P05386-1]
    CCDS10234.1. [P05386-2]
    PIRiB27125. R6HUP1.
    RefSeqiNP_000994.1. NM_001003.2. [P05386-1]
    NP_998890.1. NM_213725.1. [P05386-2]
    UniGeneiHs.356502.

    Genome annotation databases

    EnsembliENST00000260379; ENSP00000346037; ENSG00000137818. [P05386-1]
    ENST00000357790; ENSP00000350437; ENSG00000137818. [P05386-2]
    GeneIDi6176.
    KEGGihsa:6176.
    UCSCiuc002asd.1. human. [P05386-1]
    uc002ase.1. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17886 mRNA. Translation: AAA36471.1 .
    AB061836 Genomic DNA. Translation: BAB79474.1 .
    AC027237 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77845.1 .
    BC003369 mRNA. Translation: AAH03369.1 .
    BC007590 mRNA. Translation: AAH07590.1 .
    CD388103 mRNA. No translation available.
    CCDSi CCDS10233.1. [P05386-1 ]
    CCDS10234.1. [P05386-2 ]
    PIRi B27125. R6HUP1.
    RefSeqi NP_000994.1. NM_001003.2. [P05386-1 ]
    NP_998890.1. NM_213725.1. [P05386-2 ]
    UniGenei Hs.356502.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LBF NMR - A 1-69 [» ]
    3J3B electron microscopy 5.00 s/t 1-114 [» ]
    4BEH NMR - A 1-114 [» ]
    ProteinModelPortali P05386.
    SMRi P05386. Positions 1-114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112095. 96 interactions.
    IntActi P05386. 50 interactions.
    MINTi MINT-193188.
    STRINGi 9606.ENSP00000346037.

    PTM databases

    PhosphoSitei P05386.

    Proteomic databases

    MaxQBi P05386.
    PaxDbi P05386.
    PRIDEi P05386.

    Protocols and materials databases

    DNASUi 6176.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260379 ; ENSP00000346037 ; ENSG00000137818 . [P05386-1 ]
    ENST00000357790 ; ENSP00000350437 ; ENSG00000137818 . [P05386-2 ]
    GeneIDi 6176.
    KEGGi hsa:6176.
    UCSCi uc002asd.1. human. [P05386-1 ]
    uc002ase.1. human.

    Organism-specific databases

    CTDi 6176.
    GeneCardsi GC15P069745.
    HGNCi HGNC:10372. RPLP1.
    HPAi HPA003368.
    MIMi 180520. gene.
    neXtProti NX_P05386.
    PharmGKBi PA34775.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2058.
    HOGENOMi HOG000229898.
    HOVERGENi HBG002291.
    InParanoidi P05386.
    KOi K02942.
    OMAi TSELACI.
    OrthoDBi EOG7M0NVC.
    PhylomeDBi P05386.
    TreeFami TF312932.

    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 RpLP1. human.
    GeneWikii RPLP1.
    GenomeRNAii 6176.
    NextBioi 23995.
    PROi P05386.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05386.
    CleanExi HS_RPLP1.
    HS_RRP1.
    Genevestigatori P05386.

    Family and domain databases

    HAMAPi MF_01478. Ribosomal_L12_arch.
    InterProi IPR001813. Ribosomal_L10/L12.
    IPR027534. Ribosomal_L12.
    [Graphical view ]
    Pfami PF00428. Ribosomal_60s. 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 human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
      Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
      Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Eye, Placenta and Trophoblast.
    6. "Identification and characterization of phosphorylated proteins in the human pituitary."
      Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.
      Proteomics 4:587-598(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-101.
      Tissue: Pituitary.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex."
      Lee K.M., Yu C.W., Chiu T.Y., Sze K.H., Shaw P.C., Wong K.B.
      Nucleic Acids Res. 40:3172-3182(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-69, SUBUNIT.
    12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

    Entry informationi

    Entry nameiRLA1_HUMAN
    AccessioniPrimary (citable) accession number: P05386
    Secondary accession number(s): A6NIB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    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 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, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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