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Protein

Ribosomal protein L18

Gene

RPL18

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_280121. Eukaryotic Translation Termination.
REACT_280392. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_298388. SRP-dependent cotranslational protein targeting to membrane.
REACT_306007. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_329635. Formation of a pool of free 40S subunits.
REACT_330632. Peptide chain elongation.
REACT_346841. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_353757. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein L18
Gene namesi
Name:RPL18
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Chromosome 1

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 – 188187Ribosomal protein L18PRO_0000405589Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiD0VWQ3.

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000005899.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V5Zelectron microscopy8.70o1-188[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiD0VWQ3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18e family.Curated

Phylogenomic databases

eggNOGiCOG1727.
GeneTreeiENSGT00390000012976.
HOVERGENiHBG000875.
InParanoidiD0VWQ3.
KOiK02883.
OMAiIRIQDIP.
OrthoDBiEOG7PS1GP.
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.

D0VWQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR
60 70 80 90 100
LFMSRTNRPP LSLSRMIRKM KLPGRENKTA VVVGTITDDV RVQEVPKLKV
110 120 130 140 150
CALRVSSRAR SRILKAGGKI LTFDQLALDS PKGCGTVLLS GPRKGREVYR
160 170 180
HFGKAPGTPH SHTKPYVRSK GRKFERARGR RASRGYKN
Length:188
Mass (Da):21,592
Last modified:February 22, 2012 - v2
Checksum:iB3FB31DFEA45A32C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301K → M in ABD77168 (PubMed:16751257).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ403035 mRNA. Translation: ABD77168.1.
RefSeqiNP_001238887.1. NM_001251958.1.
UniGeneiCfa.39179.

Genome annotation databases

EnsembliENSCAFT00000006369; ENSCAFP00000005899; ENSCAFG00000003967.
GeneIDi476422.
KEGGicfa:476422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ403035 mRNA. Translation: ABD77168.1.
RefSeqiNP_001238887.1. NM_001251958.1.
UniGeneiCfa.39179.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V5Zelectron microscopy8.70o1-188[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000005899.

Proteomic databases

PaxDbiD0VWQ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000006369; ENSCAFP00000005899; ENSCAFG00000003967.
GeneIDi476422.
KEGGicfa:476422.

Organism-specific databases

CTDi6141.

Phylogenomic databases

eggNOGiCOG1727.
GeneTreeiENSGT00390000012976.
HOVERGENiHBG000875.
InParanoidiD0VWQ3.
KOiK02883.
OMAiIRIQDIP.
OrthoDBiEOG7PS1GP.
TreeFamiTF300202.

Enzyme and pathway databases

ReactomeiREACT_280121. Eukaryotic Translation Termination.
REACT_280392. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_298388. SRP-dependent cotranslational protein targeting to membrane.
REACT_306007. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_329635. Formation of a pool of free 40S subunits.
REACT_330632. Peptide chain elongation.
REACT_346841. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_353757. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

EvolutionaryTraceiD0VWQ3.

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. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
    , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Boxer.
  2. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
    Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
    Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-187.
    Tissue: Liver.
  3. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).

Entry informationi

Entry nameiRL18_CANFA
AccessioniPrimary (citable) accession number: D0VWQ3
Secondary accession number(s): Q0QEV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: February 22, 2012
Last modified: July 22, 2015
This is version 39 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.