60S acidic ribosomal protein P2 (RPLP2)
The protein contains 115 amino acids for an estimated molecular weight of 11665 Da.
Plays an important role in the elongation step of protein synthesis. (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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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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Biological Process
Cellular protein metabolic process
Cytoplasmic translation
Cytoplasmic translational elongation
Gene expression
Nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
RRNA processing
SRP-dependent cotranslational protein targeting to membrane
Translation
Translational elongation
Translational initiation
Translational termination
Viral life cycle
Viral process
Viral transcription
Cellular Component
Cytosol
Cytosolic large ribosomal subunit
Extracellular exosome
Focal adhesion
Membrane
Synapse
The reference OMIM entry for this protein is 180530
Ribosomal phosphoprotein, large, p2; rplp2
Ribosomal phosphoprotein, acidic, p2
DESCRIPTION
Acidic ribosomal proteins, called A-proteins or P-proteins, are generally present in multiple copies on the ribosome and have isoelectric points in the range of pH 3 to 5, in contrast to most ribosomal proteins, which are single copy and basic. A-proteins have hydrophobic amino acid compositions, notably about 20% alanine.CLONING
Rich and Steitz (1987) described the isolation and analysis of 3 cDNA molecules that encode the human P-proteins, P2, P1 (180520), and P0 (180510). The human P1 and P2 cDNA nucleotide sequences and deduced amino acid sequences of the proteins are very similar to the sequences that have been determined for the corresponding rat, shrimp, and yeast proteins and cDNAs. P0 sequences had not previously been described. To demonstrate that the coding sequences are full length, Rich and Steitz (1987) transcribed the P0, P1, and P2 cDNAs in vitro. The P0, P1, and P2 proteins produced were serologically and electrophoretically identical to P-proteins extracted from HeLa cells. The deduced P2 protein contains 115 amino acids. Northern blot analysis revealed expression of a 0.60-kb transcript in HeLa cells. ... More on the omim web site
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
March 15, 2016: Protein entry updated
Automatic update: OMIM entry 180530 was added.