40S ribosomal protein S3a (RPS3A)

The protein contains 264 amino acids for an estimated molecular weight of 29945 Da.

 

May play a role during erythropoiesis through regulation of transcription factor DDIT3. (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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The reference OMIM entry for this protein is 180478

Ribosomal protein s3a; rps3a

CLONING

Meyuhas and Perry (1980) pioneered the cloning of mammalian ribosomal proteins. Metspalu et al. (1992) cloned the cDNA corresponding to ribosomal protein S3a, one of the approximately 85 different ribosomal proteins constituting the human ribosome. The amino acid sequence of RPS3a was deduced partially from the nucleotide sequence of cDNA and confirmed by direct amino acid sequencing. The RPS3a protein has 263 amino acids.

GENE STRUCTURE

Nolte et al. (1996) found that the coding region of the RPS3A gene spans 5,013 bp and contains 6 exons. They noted that the cDNA sequence reported by Metspalu et al. (1992) lacks the 5-prime untranslated region as well as the 6 bp encoding the first 2 amino acids. Southern blot analysis indicated that there are at least 6 processed RPS3A pseudogenes in the human genome. Rebane et al. (1998) reported that the mouse and human RPS3A genes share an identical exon/intron structure. The predicted proteins differ in only 2 positions. Some small nucleolar RNA (snoRNA) genes are located within the introns of protein-encoding genes. There is a preference for ribosome-related genes as parent genes for the snoRNAs, perhaps to coordinate the production of protein and RNA components of the ribosome. Rebane et al. (1998) reported that introns 3 and 4 of human and mouse RPS3A encode a novel snoRNA designated U73 (603568). Although both variants of U73 are expressed in mouse, only the variant specified by intron 4 is expressed in human cell lines.

GENE FUNCTION

Kho et al. (1996) showed that monoallelic disruption of the rat S3a, or fte1 (v-fos (164810) transformation effector), gene in v-fos-transformed fibroblasts resulted in loss of the transformed phenotype and in a decreased rate of protein synthesis. They concluded that the accumulation of ribosomal subunits and the rate of protein synthesis are important modulators of neoplastic transformation and cell growth.

MAPPING

By analysis of somatic cell hybrids, Nolte et al. (1996) mapped the RPS3A gene to chromosome 4. Kenmochi et al. (1998) mapped the RPS3A gene to 4q by use of somatic cell hybrid and radiation hybrid mapping panels. By fluorescence in situ hybridization, Rebane et al. (1998) refined the map position to 4q31.2-q31.3. ... 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 15, 2016: Protein entry updated
Automatic update: OMIM entry 180478 was added.

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