Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Uncharacterized protein

Gene

RPL11

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal proteinUniRule annotation

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
Submitted name:
Uncharacterized proteinImported
Gene namesi
Name:RPL11Imported
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)Imported
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiE2R9G7.

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000030830.

Structurei

3D structure databases

ProteinModelPortaliE2R9G7.
SMRiE2R9G7. Positions 10-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000013411.
InParanoidiE2R9G7.
KOiK02868.
OMAiEDTMAWF.
OrthoDBiEOG7ZPNMB.
TreeFamiTF300017.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E2R9G7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF
60 70 80 90 100
SKARYTVRSF GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS
110 120 130 140 150
DTGNFGFGIQ EHIDLGIKYD PSIGIYGLDF YVVLGRPGFS IADKKRRTGC
160 170
IGAKHRISKE EAMRWFQQKY DGIILPGK
Length:178
Mass (Da):20,252
Last modified:October 31, 2012 - v2
Checksum:i26EC965C9239774E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03001751 Genomic DNA. No translation available.
RefSeqiNP_001240835.1. NM_001253906.1.
UniGeneiCfa.39464.

Genome annotation databases

EnsembliENSCAFT00000035556; ENSCAFP00000030830; ENSCAFG00000013232.
GeneIDi100684296.
KEGGicfa:100684296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03001751 Genomic DNA. No translation available.
RefSeqiNP_001240835.1. NM_001253906.1.
UniGeneiCfa.39464.

3D structure databases

ProteinModelPortaliE2R9G7.
SMRiE2R9G7. Positions 10-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000030830.

Proteomic databases

PRIDEiE2R9G7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000035556; ENSCAFP00000030830; ENSCAFG00000013232.
GeneIDi100684296.
KEGGicfa:100684296.

Organism-specific databases

CTDi6135.

Phylogenomic databases

GeneTreeiENSGT00390000013411.
InParanoidiE2R9G7.
KOiK02868.
OMAiEDTMAWF.
OrthoDBiEOG7ZPNMB.
TreeFamiTF300017.

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.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Broad Sequencing Platform
    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: BoxerImported.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: BoxerImported.

Entry informationi

Entry nameiE2R9G7_CANFA
AccessioniPrimary (citable) accession number: E2R9G7
Entry historyi
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: October 31, 2012
Last modified: July 22, 2015
This is version 37 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.