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Protein
Submitted name:

60S ribosomal protein L23

Gene

RPL23

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. structural constituent of ribosome Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal proteinUniRule 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:
60S ribosomal protein L23Imported
Gene namesi
Name:RPL23Imported
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)Imported
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 9

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiF2Z4P3.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKRelectron microscopy8.70k1-140[»]
ProteinModelPortaliF2Z4P3.
SMRiF2Z4P3. Positions 10-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000004690.
OMAiKTMPAVV.
OrthoDBiEOG7ZD1X5.
TreeFamiTF300913.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
InterProiIPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F2Z4P3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKRGRGGSS GAKFRISLGL PVGAVINCAD NTGAKNLYII SVKGIKGRLN
60 70 80 90 100
RLPAAGVGDM VMATVKKGKP ELRKKVHPAV VIRQRKSYRR KDGVFLYFED
110 120 130 140
NAGVIVNNKG EMKGSAITGP VAKECADLWP RIASNAGSIA
Length:140
Mass (Da):14,865
Last modified:May 31, 2011 - v1
Checksum:i807E14139B2EB0B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03006484 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSCAFT00000026221; ENSCAFP00000024349; ENSCAFG00000028955.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03006484 Genomic DNA. No translation available.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKRelectron microscopy8.70k1-140[»]
ProteinModelPortaliF2Z4P3.
SMRiF2Z4P3. Positions 10-140.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiF2Z4P3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000026221; ENSCAFP00000024349; ENSCAFG00000028955.

Phylogenomic databases

GeneTreeiENSGT00390000004690.
OMAiKTMPAVV.
OrthoDBiEOG7ZD1X5.
TreeFamiTF300913.

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.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
InterProiIPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 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 nameiF2Z4P3_CANFA
AccessioniPrimary (citable) accession number: F2Z4P3
Entry historyi
Integrated into UniProtKB/TrEMBL: May 31, 2011
Last sequence update: May 31, 2011
Last modified: January 7, 2015
This is version 30 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.