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Protein

60S ribosomal protein L23

Gene

RPL23

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • large ribosomal subunit rRNA binding Source: GO_Central
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: GO_Central
  • transcription coactivator binding Source: CAFA
  • ubiquitin ligase inhibitor activity Source: CAFA
  • ubiquitin protein ligase binding Source: CAFA

GO - Biological processi

  • cellular response to actinomycin D Source: CAFA
  • negative regulation of cell cycle arrest Source: CAFA
  • negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: CAFA
  • negative regulation of transcription from RNA polymerase II promoter Source: CAFA
  • negative regulation of ubiquitin protein ligase activity Source: CAFA
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • positive regulation of cell cycle arrest Source: CAFA
  • positive regulation of cell proliferation Source: CAFA
  • positive regulation of gene expression Source: CAFA
  • positive regulation of signal transduction by p53 class mediator Source: CAFA
  • positive regulation of transcription from RNA polymerase II promoter Source: CAFA
  • protein-DNA complex disassembly Source: CAFA
  • protein stabilization Source: CAFA
  • ribosomal protein import into nucleus Source: UniProtKB
  • rRNA processing Source: Reactome
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: UniProtKB
  • translational initiation Source: Reactome
  • viral transcription Source: Reactome

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L23
Alternative name(s):
60S ribosomal protein L17
Large ribosomal subunit protein uL141 Publication
Gene namesi
Name:RPL23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000125691.12.
HGNCiHGNC:10316. RPL23.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Organism-specific databases

DisGeNETi9349.
OpenTargetsiENSG00000125691.
PharmGKBiPA34690.

Chemistry databases

DrugBankiDB02494. Alpha-Hydroxy-Beta-Phenyl-Propionic Acid.
DB07374. Anisomycin.
DB08437. Puromycin.

Polymorphism and mutation databases

BioMutaiRPL23.
DMDMi51338639.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001286121 – 14060S ribosomal protein L23Add BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphoserineCombined sources1
Modified residuei38PhosphotyrosineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP62829.
MaxQBiP62829.
PaxDbiP62829.
PeptideAtlasiP62829.
PRIDEiP62829.
TopDownProteomicsiP62829.

2D gel databases

SWISS-2DPAGEiP62829.

PTM databases

iPTMnetiP62829.
PhosphoSitePlusiP62829.
SwissPalmiP62829.

Expressioni

Gene expression databases

BgeeiENSG00000125691.
CleanExiHS_RPL23.
ExpressionAtlasiP62829. baseline and differential.
GenevisibleiP62829. HS.

Organism-specific databases

HPAiHPA003373.

Interactioni

Binary interactionsi

Show more details

GO - Molecular functioni

  • transcription coactivator binding Source: CAFA
  • ubiquitin protein ligase binding Source: CAFA

Protein-protein interaction databases

BioGridi114752. 243 interactors.
CORUMiP62829.
DIPiDIP-33156N.
IntActiP62829. 47 interactors.
MINTiMINT-5001181.
STRINGi9606.ENSP00000377865.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-LV1-140[»]
4V6Xelectron microscopy5.00CV1-140[»]
5AJ0electron microscopy3.50AV1-140[»]
5LKSelectron microscopy3.60LV1-140[»]
5T2Celectron microscopy3.60P1-140[»]
ProteinModelPortaliP62829.
SMRiP62829.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0901. Eukaryota.
COG0093. LUCA.
GeneTreeiENSGT00390000004690.
HOGENOMiHOG000183703.
HOVERGENiHBG000282.
InParanoidiP62829.
KOiK02894.
OMAiIKGPVAR.
OrthoDBiEOG091G0QGZ.
PhylomeDBiP62829.
TreeFamiTF300913.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14. 1 hit.
InterProiView protein in InterPro
IPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
IPR036853. Ribosomal_L14P_sf.
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiView protein in Pfam
PF00238. Ribosomal_L14. 1 hit.
SMARTiView protein in SMART
SM01374. Ribosomal_L14. 1 hit.
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiView protein in PROSITE
PS00049. RIBOSOMAL_L14. 1 hit.

Sequencei

Sequence statusi: Complete.

P62829-1 [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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti77H → R in AAH62716 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52839 mRNA. Translation: CAA37023.1.
X55954 mRNA. Translation: CAA39417.1.
AB061827 Genomic DNA. Translation: BAB79465.1.
BC010114 mRNA. Translation: AAH10114.1.
BC062716 mRNA. Translation: AAH62716.1.
BC104651 mRNA. Translation: AAI04652.1.
BC106061 mRNA. Translation: AAI06062.1.
CCDSiCCDS11330.1.
PIRiS18815. R5HU23.
RefSeqiNP_000969.1. NM_000978.3.
UniGeneiHs.406300.

Genome annotation databases

EnsembliENST00000394332; ENSP00000377865; ENSG00000125691.
ENST00000479035; ENSP00000420311; ENSG00000125691.
GeneIDi9349.
KEGGihsa:9349.
UCSCiuc002hqx.2. human.

Similar proteinsi

Entry informationi

Entry nameiRL23_HUMAN
AccessioniPrimary (citable) accession number: P62829
Secondary accession number(s): P23131
, P24048, Q29246, Q3SWV7, Q6P5S1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: October 25, 2017
This is version 138 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families