60S ribosomal protein L23a (RPL23A)

The protein contains 156 amino acids for an estimated molecular weight of 17695 Da.

 

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds a specific region on the 26S rRNA. May promote p53/TP53 degradation possibly through the stimulation of MDM2-mediated TP53 polyubiquitination (PubMed:26203195). (updated: March 28, 2018)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. 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.
  3. 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.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. 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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 100%
Model score: 100

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VariantDescription
Rare variant found in Diamond-Blackfan anemia patients

The reference OMIM entry for this protein is 602326

Ribosomal protein l23a; rpl23a

See RPL19 (180466) for further discussion of this gene family.

CLONING

Fan et al. (1997) cloned, sequenced, and mapped the gene for human ribosomal protein RPL23A. A 0.6-kb transcript was found in all tissues examined. In adult tissues, the RPL23A transcript was more abundant in pancreas, skeletal muscle, and heart, while much less abundant in kidney, brain, placenta, lung, and liver. The open reading frame encodes a polypeptide of 156 amino acids, which is identical with the rat RPL23A protein. In the 5-prime flanking region of the gene, a canonical TATA sequence and a defined CAAT box were found for the first time in a mammalian ribosomal protein gene.

GENE STRUCTURE

Fan et al. (1997) demonstrated that the 4.0-kb RPL23A gene contains 5 exons and 4 introns.

GENE FUNCTION

Using protein crosslinking, Pool et al. (2002) detected distinct modes in the binding of the signal recognition particle (SRP) to the ribosome. During signal peptide recognition, SRP54 (604857) is positioned at the exit site close to ribosomal proteins L23a and L35. When SRP54 contacts the signal recognition particle receptor (182180), SRP54 is rearranged such that it is no longer close to L23a. This repositioning may allow the translocon to dock with the ribosome, leading to insertion of the signal peptide into the translocation channel. Ito et al. (2014) isolated arthritogenic T-cell receptors (TCRs) from mice engineered to generate T cells mediating autoimmune arthritis, which resembles human rheumatoid arthritis (RA; 180300), and characterized the self antigens that they recognized. One of them was the ubiquitously expressed RPL23A, with which T cells and autoantibodies from RA patients reacted.

MAPPING

By fluorescence in situ hybridization, Fan et al. (1997) mapped the RPL23A gene to chromosome 17q11. ... More on the omim web site

Subscribe to this protein entry history

May 12, 2019: Protein entry updated
Automatic update: model status changed

Nov. 16, 2018: Protein entry updated
Automatic update: model status changed

April 12, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

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 602326 was added.

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed