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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

  • poly(A) RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L23
Alternative name(s):
60S ribosomal protein L17
Gene namesi
Name:RPL23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10316. RPL23.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: Ensembl
  • ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34690.

Polymorphism and mutation databases

BioMutaiRPL23.
DMDMi51338639.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14014060S ribosomal protein L23PRO_0000128612Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine1 Publication
Modified residuei38 – 381Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP62829.
PaxDbiP62829.
PRIDEiP62829.

2D gel databases

SWISS-2DPAGEP62829.

PTM databases

PhosphoSiteiP62829.

Expressioni

Gene expression databases

BgeeiP62829.
CleanExiHS_RPL23.
ExpressionAtlasiP62829. baseline and differential.
GenevisibleiP62829. HS.

Organism-specific databases

HPAiHPA003373.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
BCCIPQ9P2874EBI-353303,EBI-711154
MDM2Q009873EBI-353303,EBI-389668

Protein-protein interaction databases

BioGridi114752. 158 interactions.
IntActiP62829. 32 interactions.
MINTiMINT-5001181.
STRINGi9606.ENSP00000377865.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CV1-140[»]
5AJ0electron microscopy3.50AV1-140[»]
ProteinModelPortaliP62829.
SMRiP62829. Positions 9-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.Curated

Phylogenomic databases

eggNOGiCOG0093.
GeneTreeiENSGT00390000004690.
HOGENOMiHOG000183703.
HOVERGENiHBG000282.
InParanoidiP62829.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG7ZD1X5.
PhylomeDBiP62829.
TreeFamiTF300913.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771H → R in AAH62716 (PubMed:15489334).Curated

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.1. human.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CV1-140[»]
5AJ0electron microscopy3.50AV1-140[»]
ProteinModelPortaliP62829.
SMRiP62829. Positions 9-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114752. 158 interactions.
IntActiP62829. 32 interactions.
MINTiMINT-5001181.
STRINGi9606.ENSP00000377865.

PTM databases

PhosphoSiteiP62829.

Polymorphism and mutation databases

BioMutaiRPL23.
DMDMi51338639.

2D gel databases

SWISS-2DPAGEP62829.

Proteomic databases

MaxQBiP62829.
PaxDbiP62829.
PRIDEiP62829.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394332; ENSP00000377865; ENSG00000125691.
ENST00000479035; ENSP00000420311; ENSG00000125691.
GeneIDi9349.
KEGGihsa:9349.
UCSCiuc002hqx.1. human.

Organism-specific databases

CTDi9349.
GeneCardsiGC17M037005.
HGNCiHGNC:10316. RPL23.
HPAiHPA003373.
MIMi603662. gene.
neXtProtiNX_P62829.
PharmGKBiPA34690.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0093.
GeneTreeiENSGT00390000004690.
HOGENOMiHOG000183703.
HOVERGENiHBG000282.
InParanoidiP62829.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG7ZD1X5.
PhylomeDBiP62829.
TreeFamiTF300913.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPL23. human.
GeneWikiiRPL23.
GenomeRNAii9349.
NextBioi35009.
PROiP62829.
SOURCEiSearch...

Gene expression databases

BgeeiP62829.
CleanExiHS_RPL23.
ExpressionAtlasiP62829. baseline and differential.
GenevisibleiP62829. HS.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
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. "cDNA and predicted amino acid sequences of the human ribosomal protein genes rpS12 and rpL17."
    Herault Y., Michel D., Chatelain G., Brun G.
    Nucleic Acids Res. 19:4001-4001(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation and analysis of a human cDNA highly homologous to the yeast gene encoding L17A ribosomal protein."
    Berchtold M.W., Berger M.C.
    Gene 102:283-288(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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: Brain, Kidney and Uterus.
  5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL23_HUMAN
AccessioniPrimary (citable) accession number: P62829
Secondary accession number(s): P23131
, P24048, Q29246, Q3SWV7, Q6P5S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 22, 2015
This is version 113 of the entry and version 1 of the sequence. [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

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.