Ribokinase (RBKS)
The protein contains 322 amino acids for an estimated molecular weight of 34143 Da.
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. (updated: March 1, 2001)
Protein identification was indicated in the following studies:
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
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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The reference OMIM entry for this protein is 611132
Ribokinase; rbks
DESCRIPTION
All metabolic sugars are phosphorylated to trap them inside the cell and to prepare them for further chemical reactions. Ribokinase (EC 2.7.1.15) phosphorylates ribose, an essential sugar in nucleotide biosynthesis (Bork et al., 1993).GENE FUNCTION
Although D-ribose is not generally effective as a sole carbon source for cultured animal cells, ribose-utilizing strains have been isolated. Ribose-utilizing variants of the rat Novikoff hepatoma cell line show changes in ribokinase activity. Jargiello (1982) found that parental and some variant Novikoff cells had 3 peaks of ribokinase activity, during S, G2, and M phase. In contrast, variants with high basal levels of ribokinase had only 1 peak of enzyme activity, during S phase. Ribokinase activity was either soluble or membrane-associated, and the subcellular localization differed between cell strains.MAPPING
Hartz (2007) mapped the RBKS gene to chromosome 2p23.2 based on an alignment of the RBKS sequence (GenBank GENBANK AJ404857) with the genomic sequence (build 36.1). ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 611132 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).