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Protein

39S ribosomal protein L18, mitochondrial

Gene

Mrpl18

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Together with thiosulfate sulfurtransferase (TST), acts as a mitochondrial import factor for the cytosolic 5S rRNA. The precursor form shows RNA chaperone activity; is able to fold the 5S rRNA into an import-competent conformation that is recognized by rhodanese (TST). Both the cytoplasmic and mitochondrial forms are able to bind to the helix IV-loop D in the gamma domain of the 5S rRNA (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L18, mitochondrial
Short name:
L18mt
Short name:
MRP-L18
Gene namesi
Name:Mrpl18
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1914931. Mrpl18.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: MGI
  • mitochondrion Source: MGI
  • ribosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 18039S ribosomal protein L18, mitochondrialPRO_0000030557
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiQ9CQL5.
MaxQBiQ9CQL5.
PaxDbiQ9CQL5.
PRIDEiQ9CQL5.

PTM databases

PhosphoSiteiQ9CQL5.

Expressioni

Gene expression databases

BgeeiQ9CQL5.
CleanExiMM_MRPL18.
GenevisibleiQ9CQL5. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000078123.

Structurei

3D structure databases

ProteinModelPortaliQ9CQL5.
SMRiQ9CQL5. Positions 40-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3333. Eukaryota.
ENOG4111MCR. LUCA.
GeneTreeiENSGT00390000006394.
HOGENOMiHOG000043958.
HOVERGENiHBG001529.
InParanoidiQ9CQL5.
KOiK02881.
OMAiCESVGRV.
OrthoDBiEOG7W9RW1.
PhylomeDBiQ9CQL5.
TreeFamiTF313292.

Family and domain databases

InterProiIPR005484. Ribosomal_L18.
[Graphical view]
PfamiPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9CQL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRPRFWKC LSVCRKLECG FAALSTSSVP AVQPDVESKE NEAVAPEFTN
60 70 80 90 100
RNPRNLELLG VARKERGWAT VWPNREFWHR LRVVKTQHHV EAFVEHLNGQ
110 120 130 140 150
VVVSASTREW AIKKHLYSTR NVVACESIGR VLAQRCLEAG INFMVYQPTP
160 170 180
WEASSDSIKR LQNAMTESGV MLREPRRIYE
Length:180
Mass (Da):20,677
Last modified:June 1, 2001 - v1
Checksum:i7B7759EF8A5315DD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291V → A in BAB26735 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003104 mRNA. Translation: BAB22567.1.
AK008680 mRNA. Translation: BAB25828.1.
AK010150 mRNA. Translation: BAB26735.1.
BC011425 mRNA. Translation: AAH11425.1.
CCDSiCCDS28396.1.
RefSeqiNP_080586.1. NM_026310.3.
UniGeneiMm.290166.

Genome annotation databases

EnsembliENSMUST00000079121; ENSMUSP00000078123; ENSMUSG00000057388.
GeneIDi67681.
KEGGimmu:67681.
UCSCiuc008alj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003104 mRNA. Translation: BAB22567.1.
AK008680 mRNA. Translation: BAB25828.1.
AK010150 mRNA. Translation: BAB26735.1.
BC011425 mRNA. Translation: AAH11425.1.
CCDSiCCDS28396.1.
RefSeqiNP_080586.1. NM_026310.3.
UniGeneiMm.290166.

3D structure databases

ProteinModelPortaliQ9CQL5.
SMRiQ9CQL5. Positions 40-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000078123.

PTM databases

PhosphoSiteiQ9CQL5.

Proteomic databases

EPDiQ9CQL5.
MaxQBiQ9CQL5.
PaxDbiQ9CQL5.
PRIDEiQ9CQL5.

Protocols and materials databases

DNASUi67681.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079121; ENSMUSP00000078123; ENSMUSG00000057388.
GeneIDi67681.
KEGGimmu:67681.
UCSCiuc008alj.1. mouse.

Organism-specific databases

CTDi29074.
MGIiMGI:1914931. Mrpl18.

Phylogenomic databases

eggNOGiKOG3333. Eukaryota.
ENOG4111MCR. LUCA.
GeneTreeiENSGT00390000006394.
HOGENOMiHOG000043958.
HOVERGENiHBG001529.
InParanoidiQ9CQL5.
KOiK02881.
OMAiCESVGRV.
OrthoDBiEOG7W9RW1.
PhylomeDBiQ9CQL5.
TreeFamiTF313292.

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Miscellaneous databases

PROiQ9CQL5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQL5.
CleanExiMM_MRPL18.
GenevisibleiQ9CQL5. MM.

Family and domain databases

InterProiIPR005484. Ribosomal_L18.
[Graphical view]
PfamiPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: Heart, Stomach and Tongue.
  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].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiRM18_MOUSE
AccessioniPrimary (citable) accession number: Q9CQL5
Secondary accession number(s): Q9D6N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 110 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.