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Q99N96

- RM01_MOUSE

UniProt

Q99N96 - RM01_MOUSE

Protein

39S ribosomal protein L1, mitochondrial

Gene

Mrpl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. RNA binding Source: InterPro
    2. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    39S ribosomal protein L1, mitochondrial
    Short name:
    L1mt
    Short name:
    MRP-L1
    Gene namesi
    Name:Mrpl1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:2137202. Mrpl1.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. large ribosomal subunit Source: InterPro
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5050MitochondrionSequence AnalysisAdd
    BLAST
    Chaini51 – 33628639S ribosomal protein L1, mitochondrialPRO_0000252441Add
    BLAST

    Proteomic databases

    MaxQBiQ99N96.
    PaxDbiQ99N96.
    PRIDEiQ99N96.

    PTM databases

    PhosphoSiteiQ99N96.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99N96.
    BgeeiQ99N96.
    CleanExiMM_MRPL1.
    GenevestigatoriQ99N96.

    Interactioni

    Protein-protein interaction databases

    BioGridi220433. 1 interaction.
    IntActiQ99N96. 1 interaction.
    MINTiMINT-4124547.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99N96.
    SMRiQ99N96. Positions 93-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi44 – 507Poly-Ala

    Sequence similaritiesi

    Belongs to the ribosomal protein L1P family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0081.
    GeneTreeiENSGT00390000003587.
    HOGENOMiHOG000293225.
    HOVERGENiHBG061212.
    InParanoidiQ99N96.
    KOiK02863.
    OMAiLVPLKNK.
    OrthoDBiEOG73BVDN.
    PhylomeDBiQ99N96.

    Family and domain databases

    Gene3Di3.30.190.20. 2 hits.
    3.40.50.790. 1 hit.
    InterProiIPR023674. Ribosomal_L1-like.
    IPR016094. Ribosomal_L1_2-a/b-sand.
    IPR016095. Ribosomal_L1_3-a/b-sand.
    IPR024663. Ribosomal_L1_chr.
    IPR005879. Ribosomal_L1_mit.
    [Graphical view]
    PfamiPF13003. MRL1. 1 hit.
    [Graphical view]
    SUPFAMiSSF56808. SSF56808. 1 hit.
    TIGRFAMsiTIGR01170. rplA_mito. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q99N96-1 [UniParc]FASTAAdd to Basket

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    MAAAVRCLRR VLIHHQRHCL CKMASQASLY PCSVNSLLHN RHFAAAAAAA    50
    TKPARKIKKG AKEKTSDEKP VDDIEKIKSY TYMESDPEDD VYLKRLYPRR 100
    IYEVEKAIHL LKKFQVLDFT NPKQGVYLDL TLDMALGKKK TVEPFASVIA 150
    LPHLFSSEVN KVAVFTANAS EIKIAEENGA AFAGGTDLVK KIMDDEVVVD 200
    FYVAVPEIMG ELNPLRKKLK KRFPKATRNS IGRDIPKMLE LFKTAHEIMV 250
    DEERQNFLST KIATLDMPSD QIAANLQAVI NEVCKHRPLN LGPFVVRAFL 300
    RSSTSEGLLL KTDSLLPKEA KTTEAETEET QTAEAA 336
    Length:336
    Mass (Da):37,597
    Last modified:June 16, 2009 - v2
    Checksum:i328783081296B824
    GO

    Sequence cautioni

    The sequence BAB26866.1 differs from that shown. Reason: Frameshift at position 7.
    The sequence AAH61042.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB26866.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB40837.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561K → E in BAB26866. (PubMed:15489334)Curated
    Sequence conflicti94 – 941K → R in BAB26866. (PubMed:15489334)Curated
    Sequence conflicti118 – 1181D → G in BAB26866. (PubMed:15489334)Curated
    Sequence conflicti131 – 1311T → R in BAB26866. (PubMed:15489334)Curated
    Sequence conflicti140 – 1401K → R in BAB26866. (PubMed:15489334)Curated
    Sequence conflicti180 – 1801A → V in BAB26866. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010343 mRNA. Translation: BAB26866.1. Sequence problems.
    AK142249 mRNA. Translation: BAE24994.1.
    BC028774 mRNA. Translation: AAH28774.1.
    BC061042 mRNA. Translation: AAH61042.1. Different initiation.
    AB049632 mRNA. Translation: BAB40837.1. Different initiation.
    CCDSiCCDS19449.1.
    RefSeqiNP_444388.2. NM_053158.3.
    XP_006535355.1. XM_006535292.1.
    UniGeneiMm.295499.

    Genome annotation databases

    EnsembliENSMUST00000036437; ENSMUSP00000037046; ENSMUSG00000029486.
    ENSMUST00000117766; ENSMUSP00000112977; ENSMUSG00000029486.
    GeneIDi94061.
    KEGGimmu:94061.
    UCSCiuc008yfi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010343 mRNA. Translation: BAB26866.1 . Sequence problems.
    AK142249 mRNA. Translation: BAE24994.1 .
    BC028774 mRNA. Translation: AAH28774.1 .
    BC061042 mRNA. Translation: AAH61042.1 . Different initiation.
    AB049632 mRNA. Translation: BAB40837.1 . Different initiation.
    CCDSi CCDS19449.1.
    RefSeqi NP_444388.2. NM_053158.3.
    XP_006535355.1. XM_006535292.1.
    UniGenei Mm.295499.

    3D structure databases

    ProteinModelPortali Q99N96.
    SMRi Q99N96. Positions 93-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 220433. 1 interaction.
    IntActi Q99N96. 1 interaction.
    MINTi MINT-4124547.

    PTM databases

    PhosphoSitei Q99N96.

    Proteomic databases

    MaxQBi Q99N96.
    PaxDbi Q99N96.
    PRIDEi Q99N96.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000036437 ; ENSMUSP00000037046 ; ENSMUSG00000029486 .
    ENSMUST00000117766 ; ENSMUSP00000112977 ; ENSMUSG00000029486 .
    GeneIDi 94061.
    KEGGi mmu:94061.
    UCSCi uc008yfi.1. mouse.

    Organism-specific databases

    CTDi 65008.
    MGIi MGI:2137202. Mrpl1.

    Phylogenomic databases

    eggNOGi COG0081.
    GeneTreei ENSGT00390000003587.
    HOGENOMi HOG000293225.
    HOVERGENi HBG061212.
    InParanoidi Q99N96.
    KOi K02863.
    OMAi LVPLKNK.
    OrthoDBi EOG73BVDN.
    PhylomeDBi Q99N96.

    Miscellaneous databases

    NextBioi 352027.
    PROi Q99N96.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99N96.
    Bgeei Q99N96.
    CleanExi MM_MRPL1.
    Genevestigatori Q99N96.

    Family and domain databases

    Gene3Di 3.30.190.20. 2 hits.
    3.40.50.790. 1 hit.
    InterProi IPR023674. Ribosomal_L1-like.
    IPR016094. Ribosomal_L1_2-a/b-sand.
    IPR016095. Ribosomal_L1_3-a/b-sand.
    IPR024663. Ribosomal_L1_chr.
    IPR005879. Ribosomal_L1_mit.
    [Graphical view ]
    Pfami PF13003. MRL1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56808. SSF56808. 1 hit.
    TIGRFAMsi TIGR01170. rplA_mito. 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: Embryonic stem cell and Heart.
    2. "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: C57BL/6J.
      Tissue: Mammary gland and Testis.
    3. "Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria."
      Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., Watanabe K.
      J. Biol. Chem. 276:21724-21736(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-336.
    4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.

    Entry informationi

    Entry nameiRM01_MOUSE
    AccessioniPrimary (citable) accession number: Q99N96
    Secondary accession number(s): Q3UQP5, Q8K351, Q9CWW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 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