Ribose-phosphate pyrophosphokinase 2 (PRPS2)
The protein contains 318 amino acids for an estimated molecular weight of 34769 Da.
Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. (updated: Feb. 4, 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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
5-phosphoribose 1-diphosphate biosynthetic process
AMP biosynthetic process
Animal organ regeneration
Nucleobase-containing compound metabolic process
Nucleoside metabolic process
Nucleotide biosynthetic process
Purine nucleotide biosynthetic process
Ribonucleoside monophosphate biosynthetic process
Cellular Component
Cytoplasm
Extracellular exosome
Protein complex
Ribose phosphate diphosphokinase complex
The reference OMIM entry for this protein is 311860
Phosphoribosylpyrophosphate synthetase ii; prps2
CLONING
Five-phosphoribosyl 1-pyrophosphate (PPRibP), an essential substrate and a critical regulator in the purine, pyrimidine, and pyridine nucleotide production pathways, is synthesized from MgATP and ribose 5-phosphate by the enzyme PPRibP synthetase (EC 2.7.6.1). By cDNA cloning, Taira et al. (1987) found 2 distinct PPRibP synthetase subunits, PRS I (PRPS1; 311850) and PRS II. By screening a testis library with a rat PRS II cDNA, Iizasa et al. (1989) isolated cDNAs encoding human PRS II. The predicted 318-amino acid protein shares 99% identity with rat PRS II. Northern blot analysis revealed that PRS II is expressed as a 2.7-kb mRNA in testis. By Northern blot analysis using rat Prps2 as probe, Taira et al. (1989) detected a 2.7-kb transcript in human testis and in 2 human cell lines.GENE FUNCTION
Wang et al. (1992) demonstrated that the PRPS2 gene is inactivated with lyonization but that it lies between 2 genes that escape inactivation, STS (300747) distally and ZFX (314980) proximally. The PRPS1 gene also undergoes X inactivation. Wang et al. (1992) commented that it was not known which of the 2 PRPS loci is altered in patients with inherited PRPS superactivity. The ZFX gene, which escapes X-inactivation, is bracketed proximally by the POLA gene (312040) which, like PRPS2, undergoes inactivation. The A1S9T (314370) locus in the proximal short arm and the RPS4X gene (312760) in the proximal long arm are other loci that escape inactivation and are interspersed among genes that do undergo X-inactivation. Furthermore, the XIST gene (314670), located at Xq13, is transcribed only from the inactive X chromosome.MAPPING
By using a rat cDNA probe for PRPS1 and a human cDNA probe for PRPS2, Taira et al. (1989) showed in DNA from somatic cell hybrids and in spot-blot hybridization of flow-sorted chromosomes that whereas PRPS1 is on Xq21-qter, PRPS2 is on Xpter-q21. Furthermore, 2 PRPS1-related genes were identified on chromosomes 7 and 9. By a combination of in situ hybridization and study of human/rodent somatic cell hybrids, Becker et al. (1990) assigned the PRPS2 locus to Xp22.3-p22.2. Despite the striking homology in the cDNA sequence and deduced amino acid sequence, PRPS1 and PRPS2 are encoded by genes on opposite arms of the X chromosome. ... 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 311860 was added.