60S ribosomal protein L3 (RPL3)
The protein contains 403 amino acids for an estimated molecular weight of 46109 Da.
The L3 protein is a component of the large subunit of cytoplasmic ribosomes. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
- 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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| Variant | Description |
|---|---|
| Rare variant found in a Diamond-Blackfan anemia patient |
Biological Process
Cellular response to interleukin-4
Cytoplasmic translation
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Ribosomal large subunit assembly
RRNA processing
SRP-dependent cotranslational protein targeting to membrane
Translation
Translational initiation
Viral transcription
The reference OMIM entry for this protein is 604163
Ribosomal protein l3; rpl3
DESCRIPTION
RPL3 is an essential and indispensable component for formation of the ribosomal peptidyltransferase center. It has a role in aminoacyl-tRNA binding, peptidyltransferase activity, drug resistance, translational frame maintenance, and virus replication. RPL3 also acts as a binding site for a ribosome inhibitory protein (Meskauskas and Dinman, 2007).CLONING
Adams et al. (1992) isolated the 3-prime region of an RPL3 cDNA as a human brain EST. The complete coding sequence of the human RPL3 gene has been deposited in GenBank (GENBANK X73460). The deduced RPL3 protein has 403 amino acids. Cuccurese et al. (2005) identified an RPL3 splice variant in a human lung carcinoma cell line that was induced by pharmacologic blockade of the nonsense-mediated mRNA decay pathway. This splice variant retains the 3-prime-most 180 nucleotides of intron 3, resulting in an in-frame premature termination codon. Northern blot analysis showed that the variant transcript is 1.5 kb, while the major RPL3 transcript is 1.3 kb. Intron 3 is highly conserved in human, mouse, and bovine RPL3.GENE FUNCTION
Cuccurese et al. (2005) blocked nonsense-mediated mRNA decay using cycloheximide and wortmannin and observed pronounced accumulation of the 1.5-kb RPL3 splice variant, but no change in the level of the major RPL3 transcript. The level of the 1.5-kb transcript progressively decreased following drug withdrawal. RPL3 protein overexpression resulted in accumulation of the alternative transcript in a dose-dependent manner. Cuccurese et al. (2005) concluded that the RPL3 protein regulates alternative splicing of the RPL3 gene. Meskauskas and Dinman (2007) stated that RPL3 has 2 long tentacle-like structures that extend deep into the mostly rRNA core of the ribosome. The central extension, called the 'W finger,' reaches all the way to the A-site side of the peptidyltransferase center. Meskauskas and Dinman (2007) used targeted mutagenesis and structural, biochemical, and genetic approaches to examine the W finger of S. cerevisiae Rpl3. The findings suggested a model in which RPL3 plays a role in synchronizing aminoacyl-tRNA accommodation and translocation by functioning as a sensor of tRNA occupancy at the A site of the peptidyltransferase center.GENE STRUCTURE
Duga et al. (2000) determined that the RPL3 gene contains 10 exons and spans about 6.7 kb. Introns 1, 3, 5, and 7 of the RPL3 gene encode the C/D box small nucleolar RNAs (snoRNAs) U43 (SNORD43; 611068), U86 (611069), U83A (SNORD83A; 611070), and U83B (SNORD83B; 611071), respectively. Intron 4 harbors a 283-bp Alu-SP-like repeat.MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi et al. (1998) mapped the human RPL3 gene to 22q.MOLECULAR GENETICS
Duga et al. (2000) identified a polymorphic 19-bp deletion within intron 6 of the RPL3 gene that showed an allelic frequency of about 3% in a Northern Italian population. ... More on the omim web site
July 4, 2019: Protein entry updated
Automatic update: OMIM entry 604163 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).