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Protein

60S ribosomal protein L23

Gene

Rpl23

Organism
Rattus norvegicus (Rat)
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

ReactomeiR-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-RNO-6791226. Major pathway of rRNA processing in the nucleolus.
R-RNO-72689. Formation of a pool of free 40S subunits.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-RNO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-RNO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L23
Gene namesi
Name:Rpl23
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi62067. Rpl23.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: RGD
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: Ensembl
  • membrane Source: Ensembl
  • nucleolus Source: Ensembl
  • ribosome Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14014060S ribosomal protein L23PRO_0000128616Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei38 – 381PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP62832.
PRIDEiP62832.

PTM databases

iPTMnetiP62832.
PhosphoSiteiP62832.

Expressioni

Gene expression databases

GenevisibleiP62832. RN.

Interactioni

Protein-protein interaction databases

BioGridi247952. 4 interactions.
IntActiP62832. 3 interactions.
MINTiMINT-1855140.
STRINGi10116.ENSRNOP00000005471.

Structurei

3D structure databases

ProteinModelPortaliP62832.
SMRiP62832. Positions 9-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.Curated

Phylogenomic databases

eggNOGiKOG0901. Eukaryota.
COG0093. LUCA.
GeneTreeiENSGT00390000004690.
HOGENOMiHOG000183703.
HOVERGENiHBG000282.
InParanoidiP62832.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG7ZD1X5.
PhylomeDBiP62832.
TreeFamiTF300913.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SMARTiSM01374. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62832-1 [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:August 16, 2004 - v1
Checksum:i807E14139B2EB0B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58200 mRNA. Translation: CAA41177.1.
BC058500 mRNA. Translation: AAH58500.1.
PIRiJH0418. R5RT23.
RefSeqiNP_001007600.1. NM_001007599.2.
UniGeneiRn.103172.

Genome annotation databases

EnsembliENSRNOT00000005471; ENSRNOP00000005471; ENSRNOG00000004107.
GeneIDi29282.
KEGGirno:29282.
UCSCiRGD:62067. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58200 mRNA. Translation: CAA41177.1.
BC058500 mRNA. Translation: AAH58500.1.
PIRiJH0418. R5RT23.
RefSeqiNP_001007600.1. NM_001007599.2.
UniGeneiRn.103172.

3D structure databases

ProteinModelPortaliP62832.
SMRiP62832. Positions 9-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247952. 4 interactions.
IntActiP62832. 3 interactions.
MINTiMINT-1855140.
STRINGi10116.ENSRNOP00000005471.

PTM databases

iPTMnetiP62832.
PhosphoSiteiP62832.

Proteomic databases

PaxDbiP62832.
PRIDEiP62832.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005471; ENSRNOP00000005471; ENSRNOG00000004107.
GeneIDi29282.
KEGGirno:29282.
UCSCiRGD:62067. rat.

Organism-specific databases

CTDi9349.
RGDi62067. Rpl23.

Phylogenomic databases

eggNOGiKOG0901. Eukaryota.
COG0093. LUCA.
GeneTreeiENSGT00390000004690.
HOGENOMiHOG000183703.
HOVERGENiHBG000282.
InParanoidiP62832.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG7ZD1X5.
PhylomeDBiP62832.
TreeFamiTF300913.

Enzyme and pathway databases

ReactomeiR-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-RNO-6791226. Major pathway of rRNA processing in the nucleolus.
R-RNO-72689. Formation of a pool of free 40S subunits.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-RNO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-RNO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP62832.

Gene expression databases

GenevisibleiP62832. RN.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SMARTiSM01374. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of rat ribosomal protein L23."
    Chan Y.-L., Paz V., Wool I.G.
    Biochem. Biophys. Res. Commun. 178:1153-1159(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "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].
    Tissue: Pituitary.

Entry informationi

Entry nameiRL23_RAT
AccessioniPrimary (citable) accession number: P62832
Secondary accession number(s): P23131, P24048, Q29246
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 6, 2016
This is version 96 of the entry and version 1 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.