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P62913

- RL11_HUMAN

UniProt

P62913 - RL11_HUMAN

Protein

60S ribosomal protein L11

Gene

RPL11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Binds to 5S ribosomal RNA By similarity. Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML By similarity.By similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA binding Source: ProtInc
    4. rRNA binding Source: UniProtKB-KW
    5. 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. protein localization to nucleus Source: UniProtKB
    6. protein targeting Source: UniProtKB
    7. ribosomal large subunit biogenesis Source: UniProtKB
    8. RNA metabolic process Source: Reactome
    9. rRNA processing Source: UniProtKB
    10. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    11. translation Source: UniProtKB
    12. translational elongation Source: Reactome
    13. translational initiation Source: Reactome
    14. translational termination Source: Reactome
    15. viral life cycle Source: Reactome
    16. viral process Source: Reactome
    17. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    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 ribosomal protein L11
    Alternative name(s):
    CLL-associated antigen KW-12
    Gene namesi
    Name:RPL11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10301. RPL11.

    Subcellular locationi

    Nucleusnucleolus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic large ribosomal subunit Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. nucleolus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Diamond-Blackfan anemia 7 (DBA7) [MIM:612562]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201L → H in DBA7. 1 Publication
    VAR_055448
    Natural varianti161 – 1611Missing in DBA7. 1 Publication
    VAR_055449

    Keywords - Diseasei

    Diamond-Blackfan anemia, Disease mutation

    Organism-specific databases

    MIMi612562. phenotype.
    Orphaneti124. Blackfan-Diamond anemia.
    PharmGKBiPA34664.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 17817760S ribosomal protein L11PRO_0000125082Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei44 – 441Phosphothreonine1 Publication
    Modified residuei52 – 521N6-acetyllysine1 Publication
    Modified residuei85 – 851N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62913.
    PaxDbiP62913.
    PRIDEiP62913.

    2D gel databases

    SWISS-2DPAGEP62913.

    PTM databases

    PhosphoSiteiP62913.

    Miscellaneous databases

    PMAP-CutDBP62913.

    Expressioni

    Gene expression databases

    ArrayExpressiP62913.
    BgeeiP62913.
    CleanExiHS_RPL11.
    GenevestigatoriP62913.

    Organism-specific databases

    HPAiHPA002734.

    Interactioni

    Subunit structurei

    Interacts with PML and MDM2.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MDM2Q0098711EBI-354380,EBI-389668
    MYCP011063EBI-354380,EBI-447544
    NEDD8Q158434EBI-354380,EBI-716247

    Protein-protein interaction databases

    BioGridi112055. 138 interactions.
    IntActiP62913. 32 interactions.
    MINTiMINT-1140097.
    STRINGi9606.ENSP00000363676.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00J1-178[»]
    ProteinModelPortaliP62913.
    SMRiP62913. Positions 9-176.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L5P family.Curated

    Phylogenomic databases

    eggNOGiCOG0094.
    HOGENOMiHOG000231312.
    HOVERGENiHBG055214.
    InParanoidiP62913.
    KOiK02868.
    OMAiEDTMAWF.
    OrthoDBiEOG7ZPNMB.
    PhylomeDBiP62913.
    TreeFamiTF300017.

    Family and domain databases

    Gene3Di3.30.1440.10. 1 hit.
    InterProiIPR002132. Ribosomal_L5.
    IPR020929. Ribosomal_L5_CS.
    IPR022803. Ribosomal_L5_domain.
    [Graphical view]
    PANTHERiPTHR11994. PTHR11994. 1 hit.
    PfamiPF00281. Ribosomal_L5. 1 hit.
    PF00673. Ribosomal_L5_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
    SUPFAMiSSF55282. SSF55282. 1 hit.
    PROSITEiPS00358. RIBOSOMAL_L5. 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: P62913-1) [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

    MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF    50
    SKARYTVRSF GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS 100
    DTGNFGFGIQ EHIDLGIKYD PSIGIYGLDF YVVLGRPGFS IADKKRRTGC 150
    IGAKHRISKE EAMRWFQQKY DGIILPGK 178
    Length:178
    Mass (Da):20,252
    Last modified:January 23, 2007 - v2
    Checksum:i26EC965C9239774E
    GO
    Isoform 2 (identifier: P62913-2) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3-3: Missing.

    Show »
    Length:177
    Mass (Da):20,124
    Checksum:i534FC28B1D3CF195
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311D → G in CAA55816. (PubMed:7748210)Curated
    Sequence conflicti73 – 731T → A in CAA55816. (PubMed:7748210)Curated
    Sequence conflicti92 – 921Y → L in CAA55816. (PubMed:7748210)Curated
    Sequence conflicti118 – 1181K → E in CAA55816. (PubMed:7748210)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201L → H in DBA7. 1 Publication
    VAR_055448
    Natural varianti161 – 1611Missing in DBA7. 1 Publication
    VAR_055449

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei3 – 31Missing in isoform 2. 1 PublicationVSP_008320

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79234 mRNA. Translation: CAA55816.1.
    L05092 mRNA. Translation: AAC15856.1.
    AF101385 Genomic DNA. Translation: AAD20460.3.
    BC018970 mRNA. Translation: AAH18970.1.
    AF432212 mRNA. Translation: AAL99919.1.
    AB007171 Genomic DNA. Translation: BAA25831.1.
    CCDSiCCDS238.1.
    PIRiS45049.
    RefSeqiNP_000966.2. NM_000975.3. [P62913-1]
    NP_001186731.1. NM_001199802.1. [P62913-2]
    UniGeneiHs.719951.

    Genome annotation databases

    EnsembliENST00000374550; ENSP00000363676; ENSG00000142676. [P62913-1]
    GeneIDi6135.
    KEGGihsa:6135.
    UCSCiuc001bhk.3. human.
    uc001bhl.3. human. [P62913-2]

    Polymorphism databases

    DMDMi51702795.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Diamond-Blackfan Anemia mutation database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79234 mRNA. Translation: CAA55816.1 .
    L05092 mRNA. Translation: AAC15856.1 .
    AF101385 Genomic DNA. Translation: AAD20460.3 .
    BC018970 mRNA. Translation: AAH18970.1 .
    AF432212 mRNA. Translation: AAL99919.1 .
    AB007171 Genomic DNA. Translation: BAA25831.1 .
    CCDSi CCDS238.1.
    PIRi S45049.
    RefSeqi NP_000966.2. NM_000975.3. [P62913-1 ]
    NP_001186731.1. NM_001199802.1. [P62913-2 ]
    UniGenei Hs.719951.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3B electron microscopy 5.00 J 1-178 [» ]
    ProteinModelPortali P62913.
    SMRi P62913. Positions 9-176.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112055. 138 interactions.
    IntActi P62913. 32 interactions.
    MINTi MINT-1140097.
    STRINGi 9606.ENSP00000363676.

    PTM databases

    PhosphoSitei P62913.

    Polymorphism databases

    DMDMi 51702795.

    2D gel databases

    SWISS-2DPAGE P62913.

    Proteomic databases

    MaxQBi P62913.
    PaxDbi P62913.
    PRIDEi P62913.

    Protocols and materials databases

    DNASUi 6135.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374550 ; ENSP00000363676 ; ENSG00000142676 . [P62913-1 ]
    GeneIDi 6135.
    KEGGi hsa:6135.
    UCSCi uc001bhk.3. human.
    uc001bhl.3. human. [P62913-2 ]

    Organism-specific databases

    CTDi 6135.
    GeneCardsi GC01P024018.
    GeneReviewsi RPL11.
    HGNCi HGNC:10301. RPL11.
    HPAi HPA002734.
    MIMi 604175. gene.
    612562. phenotype.
    neXtProti NX_P62913.
    Orphaneti 124. Blackfan-Diamond anemia.
    PharmGKBi PA34664.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0094.
    HOGENOMi HOG000231312.
    HOVERGENi HBG055214.
    InParanoidi P62913.
    KOi K02868.
    OMAi EDTMAWF.
    OrthoDBi EOG7ZPNMB.
    PhylomeDBi P62913.
    TreeFami TF300017.

    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 RPL11. human.
    GeneWikii RPL11.
    GenomeRNAii 6135.
    NextBioi 23831.
    PMAP-CutDB P62913.
    PROi P62913.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62913.
    Bgeei P62913.
    CleanExi HS_RPL11.
    Genevestigatori P62913.

    Family and domain databases

    Gene3Di 3.30.1440.10. 1 hit.
    InterProi IPR002132. Ribosomal_L5.
    IPR020929. Ribosomal_L5_CS.
    IPR022803. Ribosomal_L5_domain.
    [Graphical view ]
    PANTHERi PTHR11994. PTHR11994. 1 hit.
    Pfami PF00281. Ribosomal_L5. 1 hit.
    PF00673. Ribosomal_L5_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002161. Ribosomal_L5. 1 hit.
    SUPFAMi SSF55282. SSF55282. 1 hit.
    PROSITEi PS00358. RIBOSOMAL_L5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and determination of the primary structure of DNA complementary to the mRNA of human ribosomal protein L11."
      Mishin V.P., Filipenko M.L., Muravlev A.I., Karpova G.G., Mertvetsov N.P.
      Bioorg. Khim. 21:158-160(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Expressed sequence tags from a human cell line."
      Bhat K.S.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Structural and functional analysis of the human ribosomal protein L11 gene."
      Voronina E.N., Kolokol'tsova T.D., Nechaeva E.A., Filipenko M.L.
      Mol. Biol. (Mosk.) 37:425-435(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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] (ISOFORM 2).
      Tissue: Tonsil.
    5. Quadroni M., Bienvenut W.V.
      Submitted (NOV-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 89-95; 119-145 AND 157-164, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    6. "Identification of novel tumor antigens in CLL by SEREX: assessment of their potential as targets for immunotherapeutic approaches."
      Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-178 (ISOFORM 1).
    7. "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 17-52.
    8. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
      Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
      J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    9. Cited for: FUNCTION, VARIANT DBA7 GLU-161 DEL.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
    16. "Identification of mutations in the ribosomal protein L5 (RPL5) and ribosomal protein L11 (RPL11) genes in Czech patients with Diamond-Blackfan anemia."
      Cmejla R., Cmejlova J., Handrkova H., Petrak J., Petrtylova K., Mihal V., Stary J., Cerna Z., Jabali Y., Pospisilova D.
      Hum. Mutat. 30:321-327(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DBA7 HIS-20.

    Entry informationi

    Entry nameiRL11_HUMAN
    AccessioniPrimary (citable) accession number: P62913
    Secondary accession number(s): P25121
    , P39026, Q8TDH2, Q9Y674
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Ribosomal proteins
      Ribosomal proteins families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3