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Protein

60S ribosomal protein L23

Gene

RPL23

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 transcription by RNA polymerase II Source: CAFA
  • negative regulation of ubiquitin-dependent protein catabolic process 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 by RNA polymerase II Source: CAFA
  • protein-DNA complex disassembly Source: CAFA
  • protein stabilization Source: CAFA
  • ribosomal protein import into nucleus Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: UniProtKB
  • translational initiation 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-9010553 Regulation of expression of SLITs and ROBOs
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)

Protein family/group databases

MoonProtiP62829

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
MIMi603662 gene
neXtProtiNX_P62829

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
ProteomicsDBi57430
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, 248 interactors
CORUMiP62829
DIPiDIP-33156N
IntActiP62829, 58 interactors
MINTiP62829
STRINGi9606.ENSP00000377865

Structurei

3D structure databases

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
IPR036853 Ribosomal_L14_sf
IPR000218 Ribosomal_L14P
IPR019972 Ribosomal_L14P_CS
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
Hs.689408

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: July 18, 2018
This is version 146 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

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