40S ribosomal protein S26 (RPS26)

The protein contains 115 amino acids for an estimated molecular weight of 13015 Da.

 

No function (updated: April 1, 2015)

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. 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.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 100%
Model score: 100
MODL_I-TASSER-3.0

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VariantDescription
DBA10
DBA10

The reference OMIM entry for this protein is 603701

Ribosomal protein s26; rps26

DESCRIPTION

The eukaryotic ribosome is composed of 4 RNA species (see 180450) and approximately 80 different proteins. The ribosomal protein genes appear to be members of multigene families, most of which contain multiple processed pseudogenes and 1 intron-containing functional gene.

CLONING

Vincent et al. (1993) isolated a HeLa cell cDNA encoding ribosomal protein S26 (RPS26). Northern blot analysis demonstrated that the 600- to 700-bp RPS26 transcript is expressed at high and comparable levels in various human adult tissues. The deduced RPS26 protein has 115 amino acids (SWISS-PROT SWISSPROT Q06722).

GENE STRUCTURE

Filipenko et al. (1998) isolated the genomic sequence of the functional RPS26 gene using PCR. The RPS26 gene has 4 exons which span 2,027 bp and result in an mRNA of 438 bp, plus the poly(A) tail. Like other vertebrate ribosomal protein genes, the RPS26 gene has a transcription start site that is located within a polypyrimidine tract, and a short 5-prime untranslated region.

MAPPING

By analysis of somatic cell hybrids, Filipenko et al. (1998) mapped the intron-containing RPS26 gene to chromosome 12. Kenmochi et al. (1998) mapped the RPS26 gene to 12q using somatic cell hybrid and radiation hybrid mapping analyses.

GENE FUNCTION

Using siRNA knockdown in HeLa cells to analyze the role of RPS26 in pre-rRNA processing, Doherty et al. (2010) found that depletion of RPS26 led to decreased levels of 18S rRNA, indicating that RPS26 is necessary for production of the small subunit. RNA blot analysis showed accumulation of 43S, 26S, and 18S-E pre-rRNAs, consistent with defects in cleavage at both ends of the 18S rRNA.

MOLECULAR GENETICS

Doherty et al. (2010) sequenced 35 ribosomal protein genes in a cohort of 117 patients with Diamond-Blackfan anemia (see DBA10, 613309) and identified 9 different mutations in the RPS26 gene in 12 patients (see, e.g., 603701.0001-603701.0005). None of the mutations were found in at least 520 chromosomes from a control population of similar, largely European origin. Six probands had a mutation in the first codon, changing met to leu, val, or arg, suggesting that the translation initiation codon may be a hotspot in RPS26. Doherty et al. (2010) noted that 1 of the mutation-positive patients (603701.0002) had cleft lip and palate, making RPS26 the third DBA gene in which mutation is associated with clefting in DBA. Landowski et al. (2013) performed array CGH for copy number variation in 87 probands with Diamond-Blackfan anemia who were negative for mutation in 10 known DBA-associated ribosomal protein genes and identified a large deletion encompassing all 4 exons of the RPS26 gene (603701.0006) in a transfusion-dependent female patient. ... 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

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 25, 2017: Additional information
No protein expression data in P. Mayeux work for RPS26

March 15, 2016: Protein entry updated
Automatic update: OMIM entry 603701 was added.

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