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60S ribosomal protein L23

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From Wikipedia, the free encyclopedia

Protein found in humans

RPL23

Available structures

PDB

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

OMIM:603662;MGI:1929455;HomoloGene:68103;GeneCards:RPL23;OMA:RPL23 - orthologs

Gene location (Human)

Chr.	Chromosome 17 (human)^[1]

Band	17q12	Start	38,847,860bp^[1]
Band	17q12	End	38,853,764bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11 D\|11 61.1 cM	Start	97,668,353bp^[2]
Band	11 D\|11 61.1 cM	End	97,673,263bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ganglionic eminence

left ovary

right ovary

ventricular zone

right uterine tube

monocyte

canal of the cervix

body of uterus

right lung

left adrenal cortex

Top expressed in

yolk sac

embryo

embryo

ventricular zone

morula

blastocyst

neural layer of retina

muscle of thigh

dentate gyrus of hippocampal formation granule cell

More reference expression data

BioGPS


More reference expression data

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 extracellular exosome cytosolic large ribosomal subunit extracellular matrix nucleoplasm cytoplasm nucleolus postsynaptic density protein-containing complex
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 protein biosynthesis rRNA processing negative regulation of transcription by RNA polymerase II positive regulation of cell population proliferation positive regulation of gene expression protein-DNA complex disassembly positive regulation of transcription by RNA polymerase II protein stabilization cellular response to actinomycin D positive regulation of signal transduction by p53 class mediator negative regulation of ubiquitin protein ligase activity negative regulation of ubiquitin-dependent protein catabolic process
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


9349


65019

Ensembl


ENSG00000125691


ENSMUSG00000071415

UniProt


P62829


P62830

RefSeq (mRNA)


NM_000978


NM_022891

RefSeq (protein)


NP_000969


NP_075029

Location (UCSC)

Chr 17: 38.85 – 38.85 Mb

Chr 11: 97.67 – 97.67 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Large ribosomal subunit protein uL14 is aprotein that in humans is encoded by theRPL23gene.^[5]^[6]

Ribosomes, theorganelles that catalyzeprotein synthesis, consist of a small40S subunit and a large60S subunit. Together these subunits are composed of 4RNA species and approximately 80 structurally distinct proteins. This gene encodes aribosomal protein that is a component of the 60S subunit. The protein belongs to the universal ribosomal protein uL14 family. It is located in thecytoplasm. This gene has been referred to asRPL17 because the encoded protein shares amino acid identity with ribosomal protein L17 fromSaccharomyces cerevisiae; however, its official symbol is RPL23. As is typical for genes encoding ribosomal proteins, there are multiple processedpseudogenes of this gene dispersed through the genome.^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000125691 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000071415 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.doi:10.1093/nar/19.14.4001.PMC 328500.PMID 1861993.
^^a ^b"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.doi:10.1139/o95-101.PMID 8722009.
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.doi:10.1016/0378-1119(91)90091-O.PMID 1874450.
Yaseen NR, Blobel G (1997)."Cloning and characterization of human karyopherin β3".Proc. Natl. Acad. Sci. U.S.A.94 (9):4451–6.Bibcode:1997PNAS...94.4451Y.doi:10.1073/pnas.94.9.4451.PMC 20743.PMID 9114010.
Kenmochi N, Kawaguchi T, Rozen S, et al. (1998)."A map of 75 human ribosomal protein genes".Genome Res.8 (5):509–23.doi:10.1101/gr.8.5.509.PMID 9582194.
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.doi:10.1101/gr.214202.PMC 155282.PMID 11875025.
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.Bibcode:2002PNAS...9916899M.doi:10.1073/pnas.242603899.PMC 139241.PMID 12477932.
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.doi:10.1038/ncb1086.PMID 14743216.S2CID 11683986.
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.doi:10.1016/j.yexcr.2004.02.009.PMID 15149863.
Dai MS, Lu H (2004)."Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5".J. Biol. Chem.279 (43):44475–82.doi:10.1074/jbc.M403722200.PMID 15308643.
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.doi:10.1128/MCB.24.17.7654-7668.2004.PMC 506971.PMID 15314173.
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.doi:10.1128/MCB.24.17.7669-7680.2004.PMC 506972.PMID 15314174.
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.doi:10.1101/gr.2596504.PMC 528928.PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells".Nat. Biotechnol.23 (1):94–101.doi:10.1038/nbt1046.PMID 15592455.S2CID 7200157.
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.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.

Protein biosynthesis:translation (bacterial,archaeal,eukaryotic)

Proteins

eIF1	eIF1 B SUI1 family eIF1A Y
eIF2	α kinase β γ eIF2A eIF2B 1 2 3 4 5 eIF2D
eIF3	A B C D E F G H I J K L M
eIF4	A 1 2 3 E1 2 3 G 1 2 3 B H
eIF5	EIF5 EIF5A 2 5B
eIF6	EIF6

Elongation factor

Bacterial/Mitochondrial	EF-Tu EF-Ts EF-G EF-4 EF-P TSFM GFM1 GFM2
Archaeal/Eukaryotic	a/eEF-1 A1 2 3 B P1 P2 P3 D E G a/eEF-2

Release factor

Class 1
- eRF1
Class 2/RF3
- GSPT1
- GSPT2

Ribosomal Proteins

Cytoplasmic

60S subunit	RPL3 RPL4 RPL5 RPL6 RPL7 RPL7A RPL8 RPL9 RPL10 RPL10A RPL10-like RPL11 RPL12 RPL13 RPL13A RPL14 RPL15 RPL17 RPL18 RPL18A RPL19 RPL21 RPL22 RPL23 RPL23A RPL24 RPL26 RPL27 RPL27A RPL28 RPL29 RPL30 RPL31 RPL32 RPL34 RPL35 RPL35A RPL36 RPL36A RPL37 RPL37A RPL38 RPL39 RPL40 RPL41 RPLP0 RPLP1 RPLP2 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 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

Archaea
(70S)

Large (50S):

Small (30S):

Bacteria
(70S)

Large (50S):

Small (30S):

Eukaryotes

Cytoplasmic (80S)	Large (60S): 5S 5.8S 28S Small (40S): 18S
Mitochondrial (55S)	Large (28S): MT-RNR2, 16S MT-tRNA^Val Small (39S): MT-RNR1, 12S
Chloroplast (70S)	Large (50S): 5S 4.5S 23S Small (30S): 16S

Ribosomal proteins

(See article table)

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