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P39023

- RL3_HUMAN

UniProt

P39023 - RL3_HUMAN

Protein

60S ribosomal protein L3

Gene

RPL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    The L3 protein is a component of the large subunit of cytoplasmic ribosomes.

    GO - Molecular functioni

    1. poly(A) RNA 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. cellular response to interleukin-4 Source: Ensembl
    3. gene expression Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    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

    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 L3
    Alternative name(s):
    HIV-1 TAR RNA-binding protein B
    Short name:
    TARBP-B
    Gene namesi
    Name:RPL3
    ORF Names:OK/SW-cl.32
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:10332. RPL3.

    Subcellular locationi

    Nucleusnucleolus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34713.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 40340260S ribosomal protein L3PRO_0000077227Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphoserine2 Publications
    Modified residuei136 – 1361N6-acetyllysineBy similarity
    Modified residuei286 – 2861N6-acetyllysineBy similarity
    Modified residuei294 – 2941N6-acetyllysine1 Publication
    Modified residuei304 – 3041Phosphoserine1 Publication
    Modified residuei366 – 3661N6-acetyllysine1 Publication
    Modified residuei373 – 3731N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP39023.
    PaxDbiP39023.
    PRIDEiP39023.

    2D gel databases

    SWISS-2DPAGEP39023.

    PTM databases

    PhosphoSiteiP39023.

    Expressioni

    Gene expression databases

    ArrayExpressiP39023.
    BgeeiP39023.
    CleanExiHS_RPL3.
    GenevestigatoriP39023.

    Organism-specific databases

    HPAiHPA003365.
    HPA055361.

    Interactioni

    Subunit structurei

    Interacts with METTL18.1 Publication

    Protein-protein interaction databases

    BioGridi112042. 102 interactions.
    IntActiP39023. 25 interactions.
    MINTiMINT-1145548.
    STRINGi9606.ENSP00000346001.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00B1-403[»]
    ProteinModelPortaliP39023.
    SMRiP39023. Positions 2-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L3P family.Curated

    Phylogenomic databases

    eggNOGiCOG0087.
    HOGENOMiHOG000107319.
    HOVERGENiHBG001864.
    InParanoidiP39023.
    KOiK02925.
    OMAiFQTFEEK.
    PhylomeDBiP39023.
    TreeFamiTF300555.

    Family and domain databases

    InterProiIPR000597. Ribosomal_L3.
    IPR019926. Ribosomal_L3_CS.
    IPR009000. Transl_B-barrel.
    [Graphical view]
    PfamiPF00297. Ribosomal_L3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P39023-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDPSKP VHLTAFLGYK    50
    AGMTHIVREV DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR 100
    TFKTVFAEHI SDECKRRFYK NWHKSKKKAF TKYCKKWQDE DGKKQLEKDF 150
    SSMKKYCQVI RVIAHTQMRL LPLRQKKAHL MEIQVNGGTV AEKLDWARER 200
    LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL PRKTHRGLRK 250
    VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK 300
    NNASTDYDLS DKSINPLGGF VHYGEVTNDF VMLKGCVVGT KKRVLTLRKS 350
    LLVQTKRRAL EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE 400
    EGA 403
    Length:403
    Mass (Da):46,109
    Last modified:January 23, 2007 - v2
    Checksum:iA607CEE75CF62148
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221S → T in AAA91344. (PubMed:7576925)Curated
    Sequence conflicti260 – 2601A → V in AAA91344. (PubMed:7576925)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111H → R Rare variant found in a Diamond-Blackfan anemia patient; unknown pathological significance. 1 Publication
    VAR_069220
    Natural varianti78 – 781I → T.
    Corresponds to variant rs11548004 [ dbSNP | Ensembl ].
    VAR_052040

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73460 mRNA. Translation: CAA51839.1.
    AB062291 mRNA. Translation: BAB93474.1.
    CR456566 mRNA. Translation: CAG30452.1.
    AK315693 mRNA. Translation: BAG38056.1.
    AL022326 Genomic DNA. Translation: CAA18450.1.
    BC002408 mRNA. Translation: AAH02408.1.
    BC006483 mRNA. Translation: AAH06483.1.
    BC008003 mRNA. Translation: AAH08003.1.
    BC012146 mRNA. Translation: AAH12146.1.
    BC012786 mRNA. Translation: AAH12786.1.
    BC013674 mRNA. Translation: AAH13674.1.
    BC014017 mRNA. Translation: AAH14017.1.
    BC015032 mRNA. Translation: AAH15032.1.
    BC015767 mRNA. Translation: AAH15767.1.
    BC063662 mRNA. Translation: AAH63662.1.
    BC088373 mRNA. Translation: AAH88373.1.
    BC107711 mRNA. Translation: AAI07712.1.
    M90054 mRNA. Translation: AAA60291.1.
    L22453 mRNA. Translation: AAA91344.1.
    AB007166 Genomic DNA. Translation: BAA25828.1.
    CCDSiCCDS13988.1.
    PIRiS34195.
    RefSeqiNP_000958.1. NM_000967.3.
    UniGeneiHs.119598.

    Genome annotation databases

    EnsembliENST00000216146; ENSP00000346001; ENSG00000100316.
    GeneIDi6122.
    KEGGihsa:6122.
    UCSCiuc003axh.3. human.

    Polymorphism databases

    DMDMi730565.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73460 mRNA. Translation: CAA51839.1 .
    AB062291 mRNA. Translation: BAB93474.1 .
    CR456566 mRNA. Translation: CAG30452.1 .
    AK315693 mRNA. Translation: BAG38056.1 .
    AL022326 Genomic DNA. Translation: CAA18450.1 .
    BC002408 mRNA. Translation: AAH02408.1 .
    BC006483 mRNA. Translation: AAH06483.1 .
    BC008003 mRNA. Translation: AAH08003.1 .
    BC012146 mRNA. Translation: AAH12146.1 .
    BC012786 mRNA. Translation: AAH12786.1 .
    BC013674 mRNA. Translation: AAH13674.1 .
    BC014017 mRNA. Translation: AAH14017.1 .
    BC015032 mRNA. Translation: AAH15032.1 .
    BC015767 mRNA. Translation: AAH15767.1 .
    BC063662 mRNA. Translation: AAH63662.1 .
    BC088373 mRNA. Translation: AAH88373.1 .
    BC107711 mRNA. Translation: AAI07712.1 .
    M90054 mRNA. Translation: AAA60291.1 .
    L22453 mRNA. Translation: AAA91344.1 .
    AB007166 Genomic DNA. Translation: BAA25828.1 .
    CCDSi CCDS13988.1.
    PIRi S34195.
    RefSeqi NP_000958.1. NM_000967.3.
    UniGenei Hs.119598.

    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 B 1-403 [» ]
    ProteinModelPortali P39023.
    SMRi P39023. Positions 2-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112042. 102 interactions.
    IntActi P39023. 25 interactions.
    MINTi MINT-1145548.
    STRINGi 9606.ENSP00000346001.

    PTM databases

    PhosphoSitei P39023.

    Polymorphism databases

    DMDMi 730565.

    2D gel databases

    SWISS-2DPAGE P39023.

    Proteomic databases

    MaxQBi P39023.
    PaxDbi P39023.
    PRIDEi P39023.

    Protocols and materials databases

    DNASUi 6122.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216146 ; ENSP00000346001 ; ENSG00000100316 .
    GeneIDi 6122.
    KEGGi hsa:6122.
    UCSCi uc003axh.3. human.

    Organism-specific databases

    CTDi 6122.
    GeneCardsi GC22M039821.
    H-InvDB HIX0172339.
    HGNCi HGNC:10332. RPL3.
    HPAi HPA003365.
    HPA055361.
    MIMi 604163. gene.
    neXtProti NX_P39023.
    PharmGKBi PA34713.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0087.
    HOGENOMi HOG000107319.
    HOVERGENi HBG001864.
    InParanoidi P39023.
    KOi K02925.
    OMAi FQTFEEK.
    PhylomeDBi P39023.
    TreeFami TF300555.

    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 RPL3. human.
    GeneWikii RPL3.
    GenomeRNAii 6122.
    NextBioi 23777.
    PROi P39023.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P39023.
    Bgeei P39023.
    CleanExi HS_RPL3.
    Genevestigatori P39023.

    Family and domain databases

    InterProi IPR000597. Ribosomal_L3.
    IPR019926. Ribosomal_L3_CS.
    IPR009000. Transl_B-barrel.
    [Graphical view ]
    Pfami PF00297. Ribosomal_L3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    PROSITEi PS00474. RIBOSOMAL_L3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete coding sequence of human ribosomal protein L3 mRNA."
      Leffers H.
      Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon adenocarcinoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Brain, Colon, Lung, Muscle, Ovary, PNS, Skin and Uterus.
    7. Still I.H.
      Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-403.
    8. "Molecular cloning and characterization of a TAR-binding nuclear factor from T cells."
      Reddy T.R., Suhasini M., Rappaport J., Looney D.J., Kraus G., Wong-Staal F.
      AIDS Res. Hum. Retroviruses 11:663-669(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-277.
    9. "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 328-398.
    10. "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: PROTEIN SEQUENCE OF 2-13, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47."
      Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.
      Nucleic Acids Res. 34:4593-4608(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-294 AND LYS-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
      Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
      PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH METTL18.
    19. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
    20. "Frameshift mutation in p53 regulator RPL26 is associated with multiple physical abnormalities and a specific pre-ribosomal RNA processing defect in diamond-blackfan anemia."
      Gazda H.T., Preti M., Sheen M.R., O'Donohue M.F., Vlachos A., Davies S.M., Kattamis A., Doherty L., Landowski M., Buros C., Ghazvinian R., Sieff C.A., Newburger P.E., Niewiadomska E., Matysiak M., Glader B., Atsidaftos E., Lipton J.M., Gleizes P.E., Beggs A.H.
      Hum. Mutat. 33:1037-1044(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-11.

    Entry informationi

    Entry nameiRL3_HUMAN
    AccessioniPrimary (citable) accession number: P39023
    Secondary accession number(s): B2RDV9, Q15548, Q5I0G0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 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 22
      Human chromosome 22: 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