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Protein

60S ribosomal protein L18

Gene

Rpl18

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

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L18
Gene namesi
Name:Rpl18
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98003. Rpl18.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.
ExpressionAtlasiP35980. baseline and differential.
GenevisibleiP35980. MM.

Interactioni

Protein-protein interaction databases

BioGridi202968. 10 interactions.
IntActiP35980. 4 interactions.
MINTiMINT-1857698.
STRINGi10090.ENSMUSP00000072320.

Structurei

3D structure databases

ProteinModelPortaliP35980.
SMRiP35980. Positions 54-121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18e family.Curated

Phylogenomic databases

eggNOGiCOG1727.
HOGENOMiHOG000213425.
HOVERGENiHBG000875.
InParanoidiP35980.
KOiK02883.
OMAiKEDNIAV.
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

« Hide

        10         20         30         40         50
MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR
60 70 80 90 100
LFMSRTNRPP LSLSRMIRKM KLPGRENKTA VVVGTVTDDV RILEVPKLKV
110 120 130 140 150
CALRVSSRAR SRILKAGGKI LTFDQLALES PKGRGTVLLS GPRKGREVYR
160 170 180
HFGKAPGTPH SHTKPYVRSK GRKFERARGR RASRGYKN
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:
EMBLi
GenBanki
DDBJi
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.
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:
EMBLi
GenBanki
DDBJi
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.
UniGeneiMm.3459.
Mm.422997.

3D structure databases

ProteinModelPortaliP35980.
SMRiP35980. Positions 54-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202968. 10 interactions.
IntActiP35980. 4 interactions.
MINTiMINT-1857698.
STRINGi10090.ENSMUSP00000072320.

PTM databases

PhosphoSiteiP35980.

Proteomic databases

MaxQBiP35980.
PaxDbiP35980.
PRIDEiP35980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6141.
MGIiMGI:98003. Rpl18.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

NextBioi297433.
PROiP35980.
SOURCEiSearch...

Gene expression databases

BgeeiP35980.
CleanExiMM_RPL18.
ExpressionAtlasiP35980. baseline and differential.
GenevisibleiP35980. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 118 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

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 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.