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Protein
Submitted name:

Uncharacterized protein

Gene

RPL8

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_204671. SRP-dependent cotranslational protein targeting to membrane.
REACT_236501. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_236618. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_244619. Peptide chain elongation.
REACT_249312. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_256443. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_263476. Eukaryotic Translation Termination.
REACT_269652. Formation of a pool of free 40S subunits.

Names & Taxonomyi

Protein namesi
Submitted name:
Uncharacterized proteinImported
Gene namesi
Name:RPL8Imported
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)Imported
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 13

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: Ensembl
  2. focal adhesion Source: Ensembl
  3. membrane Source: Ensembl
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiE2RIA8.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKRelectron microscopy8.70a1-257[»]
ProteinModelPortaliE2RIA8.
SMRiE2RIA8. Positions 2-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00390000009907.
InParanoidiE2RIA8.
KOiK02938.
OMAiAHNPDTK.
OrthoDBiEOG7ZKSBZ.
TreeFamiTF300748.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_A. Ribosomal_L2_A.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR023672. Ribosomal_L2_arc.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E2RIA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH
60 70 80 90 100
DPGRGAPLAK VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN
110 120 130 140 150
VLPVGTMPEG TIVCCLEEKP GDRGKLARAS GNYATVISHN PETKKTRVKL
160 170 180 190 200
PSGSKKVISS ANRAVVGVVA GGGRIDKPIL KAGRAYHKYK AKRNCWPRVR
210 220 230 240 250
GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA RRTGRLRGTK

TVQEKEN
Length:257
Mass (Da):28,025
Last modified:November 30, 2010 - v1
Checksum:iCE1610449749318B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03008983 Genomic DNA. No translation available.
RefSeqiXP_858496.1. XM_853403.3.

Genome annotation databases

EnsembliENSCAFT00000002627; ENSCAFP00000002440; ENSCAFG00000001677.
GeneIDi475130.
KEGGicfa:475130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03008983 Genomic DNA. No translation available.
RefSeqiXP_858496.1. XM_853403.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKRelectron microscopy8.70a1-257[»]
ProteinModelPortaliE2RIA8.
SMRiE2RIA8. Positions 2-245.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiE2RIA8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000002627; ENSCAFP00000002440; ENSCAFG00000001677.
GeneIDi475130.
KEGGicfa:475130.

Organism-specific databases

CTDi6132.

Phylogenomic databases

GeneTreeiENSGT00390000009907.
InParanoidiE2RIA8.
KOiK02938.
OMAiAHNPDTK.
OrthoDBiEOG7ZKSBZ.
TreeFamiTF300748.

Enzyme and pathway databases

ReactomeiREACT_204671. SRP-dependent cotranslational protein targeting to membrane.
REACT_236501. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_236618. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_244619. Peptide chain elongation.
REACT_249312. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_256443. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_263476. Eukaryotic Translation Termination.
REACT_269652. Formation of a pool of free 40S subunits.

Miscellaneous databases

NextBioi20851021.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_A. Ribosomal_L2_A.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR023672. Ribosomal_L2_arc.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 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. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).
  3. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: BoxerImported.

Entry informationi

Entry nameiE2RIA8_CANFA
AccessioniPrimary (citable) accession number: E2RIA8
Entry historyi
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: March 4, 2015
This is version 40 of the entry and version 1 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

3D-structureCombined sources, 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.