60S ribosomal protein L23

RPL23

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3J7R, 4V5Z, 4V6X, 4UJD, 3J7P, 4D67, 3J92, 4D5Y, 5AJ0, 3J7Q, 4UG0, 4UJE, 3J7O, 4UJC

Identifiers

Aliases

RPL23, L23, rpL17, ribosomal protein L23

External IDs

MGI: 1929455 HomoloGene: 68103 GeneCards: RPL23

Gene ontology
Molecular function	• structural constituent of ribosome • large ribosomal subunit rRNA binding • protein binding • RNA binding • transcription coactivator binding • ubiquitin protein ligase binding • ubiquitin ligase inhibitor activity
Cellular component	• cytosol • ribosome • membrane • focal adhesion • intracellular ribonucleoprotein complex • extracellular exosome • cytosolic large ribosomal subunit • extracellular matrix • nucleoplasm • cytoplasm • protein complex • nucleolus
Biological process	• ribosomal protein import into nucleus • viral transcription • SRP-dependent cotranslational protein targeting to membrane • translational initiation • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • translation • rRNA processing • negative regulation of transcription from RNA polymerase II promoter • positive regulation of cell proliferation • positive regulation of gene expression • protein-DNA complex disassembly • positive regulation of transcription from RNA polymerase II promoter • protein stabilization • negative regulation of cell cycle arrest • positive regulation of cell cycle arrest • cellular response to actinomycin D • positive regulation of signal transduction by p53 class mediator • negative regulation of ubiquitin protein ligase activity • negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


9349


65019

Ensembl


ENSG00000125691


ENSMUSG00000071415

UniProt


P62829


P62830

RefSeq (mRNA)


NM_000978


NM_022891

RefSeq (protein)


NP_000969


XP_003689266 XP_003688806

Location (UCSC)

Chr 17: 38.85 – 38.85 Mb

Chr 11: 97.78 – 97.78 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

60S ribosomal protein L23 is a protein that in humans is encoded by the RPL23 gene.^[3]^[4]

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L14P family of ribosomal proteins. It is located in the cytoplasm. This gene has been referred to as RPL17 because the encoded protein shares amino acid identity with ribosomal protein L17 from Saccharomyces cerevisiae; however, its official symbol is RPL23. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Herault Y, Michel D, Chatelain G, Brun G (Aug 1991). "cDNA and predicted amino acid sequences of the human ribosomal protein genes rpS12 and rpL17". Nucleic Acids Res. 19 (14): 4001. PMC 328500 . PMID 1861993. doi:10.1093/nar/19.14.4001.
1 2 "Entrez Gene: RPL23 ribosomal protein L23".

Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. PMID 8722009. doi:10.1139/o95-101.
Berchtold MW, Berger MC (1991). "Isolation and analysis of a human cDNA highly homologous to the yeast gene encoding L17A ribosomal protein". Gene. 102 (2): 283–8. PMID 1874450. doi:10.1016/0378-1119(91)90091-O.
Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin β3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): 4451–6. PMC 20743 . PMID 9114010. doi:10.1073/pnas.94.9.4451.
Kenmochi N, Kawaguchi T, Rozen S, et al. (1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. PMID 9582194. doi:10.1101/gr.8.5.509.
Yoshihama M, Uechi T, Asakawa S, et al. (2002). "The Human Ribosomal Protein Genes: Sequencing and Comparative Analysis of 73 Genes". Genome Res. 12 (3): 379–90. PMC 155282 . PMID 11875025. doi:10.1101/gr.214202.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. PMID 14743216. doi:10.1038/ncb1086.
Shi Y, Zhai H, Wang X, et al. (2004). "Ribosomal proteins S13 and L23 promote multidrug resistance in gastric cancer cells by suppressing drug-induced apoptosis". Exp. Cell Res. 296 (2): 337–46. PMID 15149863. doi:10.1016/j.yexcr.2004.02.009.
Dai MS, Lu H (2004). "Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5". J. Biol. Chem. 279 (43): 44475–82. PMID 15308643. doi:10.1074/jbc.M403722200.
Dai MS, Zeng SX, Jin Y, et al. (2004). "Ribosomal Protein L23 Activates p53 by Inhibiting MDM2 Function in Response to Ribosomal Perturbation but Not to Translation Inhibition". Mol. Cell. Biol. 24 (17): 7654–68. PMC 506971 . PMID 15314173. doi:10.1128/MCB.24.17.7654-7668.2004.
Jin A, Itahana K, O'Keefe K, Zhang Y (2004). "Inhibition of HDM2 and Activation of p53 by Ribosomal Protein L23". Mol. Cell. Biol. 24 (17): 7669–80. PMC 506972 . PMID 15314174. doi:10.1128/MCB.24.17.7669-7680.2004.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. PMID 15592455. doi:10.1038/nbt1046.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. PMID 16189514. doi:10.1038/nature04209.

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Proteins

Initiation factor

Prokaryotic

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	eIF1 EIF1AX AY 1B
eIF2	EIF2S1 EIF2S2 EIF2S3 EIF2B1 EIF2B2 EIF2B3 EIF2B4 EIF2B5 EIF-2 kinase eIF2A eIF2D
eIF3	EIF3A B C D E F G H I J K L M
eIF4	EIF4A2 A3 B E1 E2 E3 G1 G2 G3 H
eIF5	EIF5 EIF5A A2 5B
eIF6	EIF6

Elongation factor

Prokaryotic	EF-Tu EF-Ts EF-G
Archaeal	aEF-1 aEF-2
Eukaryotic	EEF-1 EEF1A1 EEF1A2 EEF1A3 EEF1B1 EEF1B2 EEF1B3 EEF1B4 EEF1D EEF1E1 EEF1G EEF2

Release factor

Ribosomal Proteins

Cytoplasmic

60S subunit	RPL3 RPL4 RPL5 RPL6 RPL7 RPL7A RPL8 RPL9 RPL10 RPL10A RPL10-like RPL11 RPL12 RPL13 RPL13A RPL14 RPL15 RPL16 RPL17 RPL18 RPL18A RPL19 RPL20 RPL21 RPL22 RPL23 RPL23A RPL24 RPL25 RPL26 RPL27 RPL27A RPL28 RPL29 RPL30 RPL31 RPL32 RPL33 RPL34 RPL35 RPL35A RPL36 RPL36A RPL37 RPL37A RPL38 RPL39 RPL40 RPL41 RPLP0 RPLP1 RPLP2 RPLP3 RRP15-like RSL24D1
40S subunit	RPSA RPS2 RPS3 RPS3A RPS4 (RPS4X, RPS4Y1, RPS4Y2) RPS5 RPS6 RPS7 RPS8 RPS9 RPS10 RPS11 RPS12 RPS13 RPS14 RPS15 RPS15A RPS16 RPS17 RPS18 RPS19 RPS20 RPS21 RPS22 RPS23 RPS24 RPS25 RPS26 RPS27 RPS27A RPS28 RPS29 RPS30 RACK1

Mitochondrial

39S subunit	MRPL1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42
28S subunit	MRPS1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35

Other concepts

Ribosomal RNA / ribosome subunits

Prokaryotes (70S)

Large:
50S
5S
23S

Small:
30S
16S

Eukaryotes (80S)

Cytoplasmic	Large: 60S 5S 5.8S 28S Small: 40S 18S
Mitochondrial	MT-RNR1, 12S MT-RNR2, 16S

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60S ribosomal protein L23

References

Further reading