60S ribosomal protein L23 (RPL23)
The protein contains 140 amino acids for an estimated molecular weight of 14865 Da.
No function (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Cellular protein metabolic process
Cellular response to actinomycin D
Cytoplasmic translation
Gene expression
Negative regulation of cell cycle arrest
Negative regulation of transcription by RNA polymerase II
Negative regulation of ubiquitin protein ligase activity
Negative regulation of ubiquitin-dependent protein catabolic process
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Positive regulation of cell cycle arrest
Positive regulation of cell population proliferation
Positive regulation of gene expression
Positive regulation of signal transduction by p53 class mediator
Positive regulation of transcription by RNA polymerase II
Protein stabilization
Protein-DNA complex disassembly
Ribosomal protein import into nucleus
RRNA processing
SRP-dependent cotranslational protein targeting to membrane
Translation
Translational elongation
Translational initiation
Translational termination
Viral life cycle
Viral process
Viral transcription
The reference OMIM entry for this protein is 603662
Ribosomal protein l23; rpl23
DESCRIPTION
The mammalian ribosome is composed of 4 RNA species (see 180450) and approximately 80 different proteins, including RPL23 (Kenmochi et al., 1998).CLONING
By differential screening of a human lymphocyte cDNA library with probes derived from actively dividing or quiescent quail neuroretina cells, Herault et al. (1991) isolated cDNAs encoding ribosomal protein L23 (RPL23), which they called rpL17. The deduced 140-amino acid human RPL23 protein is 78% identical to yeast ribosomal protein L17. Berchtold and Berger (1991) isolated a human brain RPL23 cDNA using PCR. Northern blot analysis detected a 600-bp RPL23 transcript in all human tissues examined.GENE FUNCTION
Impeding ribosomal biogenesis generates ribosomal stress that activates p53 (TP53; 191170) to stop cell growth. Dai et al. (2006) stated that the ribosomal proteins L5 (RPL5; 603634), L11 (RPL11; 604175), and L23 interact with MDM2 (164785) and inhibit MDM2-mediated p53 ubiquitination and degradation in response to ribosomal stress. They found that L5 and L23 inhibited ubiquitination of both p53 and MDM2 in human cell lines. In contrast, L11 inhibited proteasome-mediated degradation of ubiquitinated MDM2, but not p53, resulting in stabilization of p53.MAPPING
Kenmochi et al. (1998) mapped the RPL23 gene to 17q using somatic cell hybrid and radiation hybrid mapping analyses. Berchtold and Berger (1991) reported that the human genome contains at least 5 copies of the RPL23 gene, some of which might be pseudogenes. ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 16, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 26, 2017: Protein entry updated
Automatic update: model status changed
March 15, 2016: Protein entry updated
Automatic update: OMIM entry 603662 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed