40S ribosomal protein S17 (RPS17)

The protein contains 135 amino acids for an estimated molecular weight of 15550 Da.

 

No function (updated: March 4, 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. 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.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 100%
Model score: 100
MODL_I-TASSER-2.1

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VariantDescription
dbSNP:rs1043734

The reference OMIM entry for this protein is 180472

Ribosomal protein s17; rps17 ribosomal protein s17a-like 1, included; rps17l1, included
Ribosomal protein s17a, included; rps17a, included
Ribosomal protein s17b-like 2, included; rps17l2, included
Ribosomal protein s17b, included; rps17b, incl

For general information about ribosomal proteins, see 180466.

CLONING

Chen et al. (1986) cloned a human ribosomal protein S17 (RPS17) cDNA. The deduced RPS17 protein has 135 amino acids. The authors reported that the RPS17 gene appears to have been stringently conserved during evolution. By screening a human genomic library with an RPS17 cDNA, Chen and Roufa (1988) isolated the functional RPS17 gene and 2 processed RPS17 pseudogenes.

GENE STRUCTURE

Chen and Roufa (1988) determined that the functional RPS17 gene contains 5 exons spanning 4 kb.

MAPPING

By assessing the expression of RPS17 mRNA in rodent/human hybrid cells carrying different human chromosomes, Filipenko et al. (1995) mapped the functional RPS17 gene to chromosome 15. Kenmochi et al. (1998) mapped the functional RPS17 gene to 15q by somatic cell hybrid and radiation hybrid mapping analyses using an STS derived from an RPS17 intron. Nakamichi et al. (1986) mapped the RPS17A, or RPS17L1, gene to 5q33-qter and the RPS17B, or RPS17L2, gene to 17q. Chen and Roufa (1988) stated that the RPS17A and RPS17B genes are not transcriptionally active.

MOLECULAR GENETICS

In a 31-year-old Czech man with Diamond-Blackfan anemia (DBA4; 612527), Cmejla et al. (2007) identified a heterozygous mutation abolishing the translation initiation start codon of the RPS17 gene (180472.0001). The mutation was not found in his apparently healthy brother and parents or in 71 controls. In a male patient with DBA, Gazda et al. (2008) identified heterozygosity for a 2-bp deletion in the RPS17 gene (180472.0002). 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 2 nearly identical large deletions involving exons 3, 4, and 5 of the RPS17 gene (180472.0003) in 2 male patients.

HISTORY

Mammalian ribosomal protein genes are members of multigene families that are composed predominantly of multiple processed pseudogenes and one functional intron-containing gene, which has made the identification and mapping of the functional ribosomal protein genes difficult. Using an intron-containing PCR product for the analysis of rodent/human somatic cell hybrids, Feo et al. (1992) incorrectly mapped the RPS17 gene to chromosome 11pter-p13. ... 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 RPS17

March 15, 2016: Protein entry updated
Automatic update: OMIM entry 180472 was added.

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