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P35980

- RL18_MOUSE

UniProt

P35980 - RL18_MOUSE

Protein

60S ribosomal protein L18

Gene

Rpl18

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. 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 L18
    Gene namesi
    Name:Rpl18
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:98003. Rpl18.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 18818760S ribosomal protein L18PRO_0000132770Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301PhosphoserineBy similarity
    Modified residuei158 – 1581PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP35980.
    PaxDbiP35980.
    PRIDEiP35980.

    PTM databases

    PhosphoSiteiP35980.

    Expressioni

    Gene expression databases

    BgeeiP35980.
    CleanExiMM_RPL18.
    GenevestigatoriP35980.

    Interactioni

    Protein-protein interaction databases

    BioGridi202968. 10 interactions.
    IntActiP35980. 4 interactions.
    MINTiMINT-1857698.

    Structurei

    3D structure databases

    ProteinModelPortaliP35980.
    SMRiP35980. Positions 1-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L18e family.Curated

    Phylogenomic databases

    eggNOGiCOG1727.
    HOGENOMiHOG000213425.
    HOVERGENiHBG000875.
    InParanoidiP35980.
    KOiK02883.
    OMAiKVRRTEP.
    OrthoDBiEOG7PS1GP.
    PhylomeDBiP35980.
    TreeFamiTF300202.

    Family and domain databases

    InterProiIPR000039. Ribosomal_L18e.
    IPR021131. Ribosomal_L18e/L15P.
    IPR021132. Ribosomal_L18e_CS.
    [Graphical view]
    PANTHERiPTHR10934. PTHR10934. 1 hit.
    PfamiPF00828. Ribosomal_L18e. 1 hit.
    [Graphical view]
    SUPFAMiSSF52080. SSF52080. 1 hit.
    PROSITEiPS01106. RIBOSOMAL_L18E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P35980-1 [UniParc]FASTAAdd to Basket

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    MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR    50
    LFMSRTNRPP LSLSRMIRKM KLPGRENKTA VVVGTVTDDV RILEVPKLKV 100
    CALRVSSRAR SRILKAGGKI LTFDQLALES PKGRGTVLLS GPRKGREVYR 150
    HFGKAPGTPH SHTKPYVRSK GRKFERARGR RASRGYKN 188
    Length:188
    Mass (Da):21,645
    Last modified:January 23, 2007 - v3
    Checksum:i9489EFE201ABF7A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591P → S in AAA40067. (PubMed:8359697)Curated
    Sequence conflicti109 – 1091A → V in AAA40067. (PubMed:8359697)Curated
    Sequence conflicti115 – 1151K → R in BAB24923. (PubMed:16141072)Curated
    Sequence conflicti116 – 1161A → G in AAA40067. (PubMed:8359697)Curated
    Sequence conflicti147 – 1504EVYR → DVFP in AAA40067. (PubMed:8359697)Curated
    Sequence conflicti155 – 1551A → V in AAA40067. (PubMed:8359697)Curated
    Sequence conflicti160 – 1623HSH → YSQ in AAA40067. (PubMed:8359697)Curated
    Sequence conflicti173 – 1742KF → RL in AAA40067. (PubMed:8359697)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04128 mRNA. Translation: AAA40067.1.
    AK007263 mRNA. Translation: BAB24923.1.
    AK009044 mRNA. Translation: BAB26043.1.
    AK010510 mRNA. Translation: BAB26993.1.
    AK012580 mRNA. Translation: BAB28332.1.
    BC082290 mRNA. Translation: AAH82290.1.
    CCDSiCCDS39958.1.
    PIRiJN0779.
    RefSeqiNP_033103.2. NM_009077.2.
    XP_006540783.1. XM_006540720.1.
    UniGeneiMm.3459.
    Mm.422997.

    Genome annotation databases

    EnsembliENSMUST00000072503; ENSMUSP00000072320; ENSMUSG00000059070.
    ENSMUST00000075178; ENSMUSP00000103365; ENSMUSG00000059070.
    GeneIDi19899.
    KEGGimmu:19899.
    UCSCiuc009gww.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04128 mRNA. Translation: AAA40067.1 .
    AK007263 mRNA. Translation: BAB24923.1 .
    AK009044 mRNA. Translation: BAB26043.1 .
    AK010510 mRNA. Translation: BAB26993.1 .
    AK012580 mRNA. Translation: BAB28332.1 .
    BC082290 mRNA. Translation: AAH82290.1 .
    CCDSi CCDS39958.1.
    PIRi JN0779.
    RefSeqi NP_033103.2. NM_009077.2.
    XP_006540783.1. XM_006540720.1.
    UniGenei Mm.3459.
    Mm.422997.

    3D structure databases

    ProteinModelPortali P35980.
    SMRi P35980. Positions 1-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202968. 10 interactions.
    IntActi P35980. 4 interactions.
    MINTi MINT-1857698.

    PTM databases

    PhosphoSitei P35980.

    Proteomic databases

    MaxQBi P35980.
    PaxDbi P35980.
    PRIDEi P35980.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000072503 ; ENSMUSP00000072320 ; ENSMUSG00000059070 .
    ENSMUST00000075178 ; ENSMUSP00000103365 ; ENSMUSG00000059070 .
    GeneIDi 19899.
    KEGGi mmu:19899.
    UCSCi uc009gww.1. mouse.

    Organism-specific databases

    CTDi 6141.
    MGIi MGI:98003. Rpl18.

    Phylogenomic databases

    eggNOGi COG1727.
    HOGENOMi HOG000213425.
    HOVERGENi HBG000875.
    InParanoidi P35980.
    KOi K02883.
    OMAi KVRRTEP.
    OrthoDBi EOG7PS1GP.
    PhylomeDBi P35980.
    TreeFami TF300202.

    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 297433.
    PROi P35980.
    SOURCEi Search...

    Gene expression databases

    Bgeei P35980.
    CleanExi MM_RPL18.
    Genevestigatori P35980.

    Family and domain databases

    InterProi IPR000039. Ribosomal_L18e.
    IPR021131. Ribosomal_L18e/L15P.
    IPR021132. Ribosomal_L18e_CS.
    [Graphical view ]
    PANTHERi PTHR10934. PTHR10934. 1 hit.
    Pfami PF00828. Ribosomal_L18e. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52080. SSF52080. 1 hit.
    PROSITEi PS01106. RIBOSOMAL_L18E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of mouse cDNAs encoding ribosomal proteins L12 and L18."
      Hou E.W., Li S.S.L.
      Gene 130:287-290(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X CBA.
      Tissue: Lung.
    2. "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: C57BL/6J.
      Tissue: Embryo, Testis and Tongue.
    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].
      Strain: FVB/N-3.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiRL18_MOUSE
    AccessioniPrimary (citable) accession number: P35980
    Secondary accession number(s): Q9CQF1, Q9D987
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: January 23, 2007
    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