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P27659

- RL3_MOUSE

UniProt

P27659 - RL3_MOUSE

Protein

60S ribosomal protein L3

Gene

Rpl3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. cellular response to interleukin-4 Source: MGI
    2. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
    REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60S ribosomal protein L3
    Alternative name(s):
    J1 protein
    Gene namesi
    Name:Rpl3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1351605. Rpl3.

    Subcellular locationi

    Nucleusnucleolus By similarity. Cytoplasm

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: Ensembl
    2. nucleolus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 40340260S ribosomal protein L3PRO_0000077229Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP27659.
    PaxDbiP27659.
    PRIDEiP27659.

    PTM databases

    PhosphoSiteiP27659.

    Expressioni

    Gene expression databases

    BgeeiP27659.
    CleanExiMM_RPL3.
    GenevestigatoriP27659.

    Interactioni

    Subunit structurei

    Interacts with METTL18.By similarity

    Protein-protein interaction databases

    BioGridi205174. 10 interactions.
    IntActiP27659. 5 interactions.
    MINTiMINT-4120935.

    Structurei

    3D structure databases

    ProteinModelPortaliP27659.
    SMRiP27659. Positions 2-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L3P family.Curated

    Phylogenomic databases

    eggNOGiCOG0087.
    GeneTreeiENSGT00390000017606.
    HOGENOMiHOG000107319.
    HOVERGENiHBG001864.
    InParanoidiQ91VJ6.
    KOiK02925.
    OMAiFQTFEEK.
    OrthoDBiEOG7HF1JK.
    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.

    P27659-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDASKP VHLTAFLGYK    50
    AGMTHIVREV DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR 100
    TFKTVFAEHI SDECKRRFYK NWHKSKKKAF TKYCKKWQDD TGKKQLEKDF 150
    NSMKKYCQVI RIIAHTQMRL LPLRQKKAHL MEIQVNGGTV AEKLDWARER 200
    LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL PRKTHRGLRK 250
    VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK 300
    NNASTDYDLS DKSINPLGGF VHYGEVTNDF IMLKGCVVGT KKRVLTLRKS 350
    LLVQTKRRAL EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE 400
    EGA 403
    Length:403
    Mass (Da):46,110
    Last modified:July 27, 2011 - v3
    Checksum:i87AA82D9B2A8481E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti265 – 2651S → T in CAA68370. (PubMed:2628163)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00225 mRNA. Translation: CAA68370.1.
    U89417 mRNA. Translation: AAC36524.1.
    AK088993 mRNA. Translation: BAC40691.1.
    AK144518 mRNA. Translation: BAE25922.1.
    AK144816 mRNA. Translation: BAE26078.1.
    AK146502 mRNA. Translation: BAE27217.1.
    AK149494 mRNA. Translation: BAE28917.1.
    AK151596 mRNA. Translation: BAE30536.1.
    AK166433 mRNA. Translation: BAE38773.1.
    AK166825 mRNA. Translation: BAE39049.1.
    AK167787 mRNA. Translation: BAE39818.1.
    AK167947 mRNA. Translation: BAE39950.1.
    AK168040 mRNA. Translation: BAE40022.1.
    AK168059 mRNA. Translation: BAE40037.1.
    AK168126 mRNA. Translation: BAE40095.1.
    AK168128 mRNA. Translation: BAE40097.1.
    AK168224 mRNA. Translation: BAE40178.1.
    AK168744 mRNA. Translation: BAE40585.1.
    AK169060 mRNA. Translation: BAE40848.1.
    AK169235 mRNA. Translation: BAE41003.1.
    AK169321 mRNA. Translation: BAE41075.1.
    AK170819 mRNA. Translation: BAE42051.1.
    CH466550 Genomic DNA. Translation: EDL04616.1.
    BC009655 mRNA. Translation: AAH09655.1.
    BC083134 mRNA. Translation: AAH83134.1.
    BC094059 mRNA. Translation: AAH94059.1.
    BC158039 mRNA. Translation: AAI58040.1.
    CCDSiCCDS37144.1.
    RefSeqiNP_038790.2. NM_013762.2.
    UniGeneiMm.290771.
    Mm.321484.
    Mm.396243.
    Mm.474802.

    Genome annotation databases

    EnsembliENSMUST00000081650; ENSMUSP00000080354; ENSMUSG00000060036.
    GeneIDi27367.
    KEGGimmu:27367.
    UCSCiuc007wvb.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00225 mRNA. Translation: CAA68370.1 .
    U89417 mRNA. Translation: AAC36524.1 .
    AK088993 mRNA. Translation: BAC40691.1 .
    AK144518 mRNA. Translation: BAE25922.1 .
    AK144816 mRNA. Translation: BAE26078.1 .
    AK146502 mRNA. Translation: BAE27217.1 .
    AK149494 mRNA. Translation: BAE28917.1 .
    AK151596 mRNA. Translation: BAE30536.1 .
    AK166433 mRNA. Translation: BAE38773.1 .
    AK166825 mRNA. Translation: BAE39049.1 .
    AK167787 mRNA. Translation: BAE39818.1 .
    AK167947 mRNA. Translation: BAE39950.1 .
    AK168040 mRNA. Translation: BAE40022.1 .
    AK168059 mRNA. Translation: BAE40037.1 .
    AK168126 mRNA. Translation: BAE40095.1 .
    AK168128 mRNA. Translation: BAE40097.1 .
    AK168224 mRNA. Translation: BAE40178.1 .
    AK168744 mRNA. Translation: BAE40585.1 .
    AK169060 mRNA. Translation: BAE40848.1 .
    AK169235 mRNA. Translation: BAE41003.1 .
    AK169321 mRNA. Translation: BAE41075.1 .
    AK170819 mRNA. Translation: BAE42051.1 .
    CH466550 Genomic DNA. Translation: EDL04616.1 .
    BC009655 mRNA. Translation: AAH09655.1 .
    BC083134 mRNA. Translation: AAH83134.1 .
    BC094059 mRNA. Translation: AAH94059.1 .
    BC158039 mRNA. Translation: AAI58040.1 .
    CCDSi CCDS37144.1.
    RefSeqi NP_038790.2. NM_013762.2.
    UniGenei Mm.290771.
    Mm.321484.
    Mm.396243.
    Mm.474802.

    3D structure databases

    ProteinModelPortali P27659.
    SMRi P27659. Positions 2-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205174. 10 interactions.
    IntActi P27659. 5 interactions.
    MINTi MINT-4120935.

    PTM databases

    PhosphoSitei P27659.

    Proteomic databases

    MaxQBi P27659.
    PaxDbi P27659.
    PRIDEi P27659.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081650 ; ENSMUSP00000080354 ; ENSMUSG00000060036 .
    GeneIDi 27367.
    KEGGi mmu:27367.
    UCSCi uc007wvb.2. mouse.

    Organism-specific databases

    CTDi 6122.
    MGIi MGI:1351605. Rpl3.

    Phylogenomic databases

    eggNOGi COG0087.
    GeneTreei ENSGT00390000017606.
    HOGENOMi HOG000107319.
    HOVERGENi HBG001864.
    InParanoidi Q91VJ6.
    KOi K02925.
    OMAi FQTFEEK.
    OrthoDBi EOG7HF1JK.
    TreeFami TF300555.

    Enzyme and pathway databases

    Reactomei REACT_196445. SRP-dependent cotranslational protein targeting to membrane.
    REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Miscellaneous databases

    NextBioi 305258.
    PROi P27659.
    SOURCEi Search...

    Gene expression databases

    Bgeei P27659.
    CleanExi MM_RPL3.
    Genevestigatori P27659.

    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. "Retrovirus activation in embryonal carcinoma cells by cellular promoters."
      Peckham I., Sobel S., Comer J., Jaenisch R., Barklis E.
      Genes Dev. 3:2062-2071(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cellular transcripts encoded at a locus which permits retrovirus expression in mouse embryonic cells."
      Petersen R., Sobel S., Wang C.T., Jaenisch R., Barklis E.
      Gene 101:177-183(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c, C57BL/6J, DBA/2 and NOD.
      Tissue: Bone marrow, Brain cortex, Heart, Kidney, Liver, Lung, Mammary gland and Thymus.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      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].
      Tissue: Limb and Mammary tumor.
    6. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
      Chu C.C., Paul W.E.
      Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 183-299.
      Strain: BALB/c.
      Tissue: Spleen.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136; LYS-286 AND LYS-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiRL3_MOUSE
    AccessioniPrimary (citable) accession number: P27659
    Secondary accession number(s): O89071, Q91VJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3