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Q9CR57

- RL14_MOUSE

UniProt

Q9CR57 - RL14_MOUSE

Protein

60S ribosomal protein L14

Gene

Rpl14

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (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. ribosomal large subunit biogenesis Source: Ensembl
    2. rRNA processing Source: Ensembl
    3. 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 L14
    Gene namesi
    Name:Rpl14
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1914365. Rpl14.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 21721660S ribosomal protein L14PRO_0000132032Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysineBy similarity
    Modified residuei85 – 851N6-acetyllysine; alternate1 Publication
    Modified residuei85 – 851N6-succinyllysine; alternate1 Publication
    Modified residuei139 – 1391PhosphoserineBy similarity
    Modified residuei206 – 2061N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9CR57.
    PaxDbiQ9CR57.
    PRIDEiQ9CR57.

    PTM databases

    PhosphoSiteiQ9CR57.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CR57.
    BgeeiQ9CR57.
    CleanExiMM_RPL14.
    GenevestigatoriQ9CR57.

    Interactioni

    Protein-protein interaction databases

    BioGridi211949. 11 interactions.
    IntActiQ9CR57. 5 interactions.
    MINTiMINT-4132595.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CR57.
    SMRiQ9CR57. Positions 1-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati173 – 17751-1; approximate
    Repeati178 – 18251-2
    Repeati183 – 18751-3
    Repeati188 – 19251-4
    Repeati195 – 19732-1
    Repeati198 – 20032-2

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni173 – 192204 X 5 AA tandem repeats of Q-K-A-[APS]-XAdd
    BLAST
    Regioni195 – 20062 X 3 AA tandem repeats of K-G-Q

    Sequence similaritiesi

    Belongs to the ribosomal protein L14e family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG2163.
    GeneTreeiENSGT00390000007888.
    HOGENOMiHOG000201693.
    HOVERGENiHBG005187.
    InParanoidiQ9CR57.
    KOiK02875.
    OMAiYVRAAWE.
    OrthoDBiEOG7MD4S6.
    TreeFamiTF314356.

    Family and domain databases

    Gene3Di2.30.30.30. 1 hit.
    InterProiIPR014722. Rib_L2_dom2.
    IPR002784. Ribosomal_L14.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view]
    PfamiPF01929. Ribosomal_L14e. 1 hit.
    [Graphical view]
    SUPFAMiSSF50104. SSF50104. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9CR57-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVFRRYVEVG RVAYISFGPH AGKLVAIVDV IDQNRALVDG PCTRVRRQAM    50
    PFKCMQLTDF ILKFPHSARQ KYVRKAWEKA DINTKWAATR WAKKIDARER 100
    KAKMTDFDRF KVMKAKKMRN RIIKTEVKKL QRAAILKASP KKAAVAKAAI 150
    AAAAAAAAAK AKVPAKKATG PGKKAAGQKA PAQKAAGQKA APPAKGQKGQ 200
    KTPAQKAPAP KAAGKKA 217
    Length:217
    Mass (Da):23,564
    Last modified:January 23, 2007 - v3
    Checksum:i1DB57CAA155D05A9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261A → T in BAB25272. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK007807 mRNA. Translation: BAB25272.1.
    AK012277 mRNA. Translation: BAB28136.1.
    AK013912 mRNA. Translation: BAB29051.1.
    CCDSiCCDS40809.1.
    RefSeqiNP_080250.1. NM_025974.2.
    UniGeneiMm.289810.

    Genome annotation databases

    EnsembliENSMUST00000165532; ENSMUSP00000131489; ENSMUSG00000025794.
    GeneIDi67115.
    KEGGimmu:67115.
    UCSCiuc009scr.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK007807 mRNA. Translation: BAB25272.1 .
    AK012277 mRNA. Translation: BAB28136.1 .
    AK013912 mRNA. Translation: BAB29051.1 .
    CCDSi CCDS40809.1.
    RefSeqi NP_080250.1. NM_025974.2.
    UniGenei Mm.289810.

    3D structure databases

    ProteinModelPortali Q9CR57.
    SMRi Q9CR57. Positions 1-139.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211949. 11 interactions.
    IntActi Q9CR57. 5 interactions.
    MINTi MINT-4132595.

    PTM databases

    PhosphoSitei Q9CR57.

    Proteomic databases

    MaxQBi Q9CR57.
    PaxDbi Q9CR57.
    PRIDEi Q9CR57.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000165532 ; ENSMUSP00000131489 ; ENSMUSG00000025794 .
    GeneIDi 67115.
    KEGGi mmu:67115.
    UCSCi uc009scr.1. mouse.

    Organism-specific databases

    CTDi 9045.
    MGIi MGI:1914365. Rpl14.

    Phylogenomic databases

    eggNOGi COG2163.
    GeneTreei ENSGT00390000007888.
    HOGENOMi HOG000201693.
    HOVERGENi HBG005187.
    InParanoidi Q9CR57.
    KOi K02875.
    OMAi YVRAAWE.
    OrthoDBi EOG7MD4S6.
    TreeFami TF314356.

    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 323609.
    PROi Q9CR57.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CR57.
    Bgeei Q9CR57.
    CleanExi MM_RPL14.
    Genevestigatori Q9CR57.

    Family and domain databases

    Gene3Di 2.30.30.30. 1 hit.
    InterProi IPR014722. Rib_L2_dom2.
    IPR002784. Ribosomal_L14.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view ]
    Pfami PF01929. Ribosomal_L14e. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50104. SSF50104. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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: Head and Pancreas.
    2. "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-85, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-85 AND LYS-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiRL14_MOUSE
    AccessioniPrimary (citable) accession number: Q9CR57
    Secondary accession number(s): Q9D8Q1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 85 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