GMP reductase 2 (GMPR2)
The protein contains 348 amino acids for an estimated molecular weight of 37874 Da.
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (PubMed:12009299, PubMed:12669231, PubMed:16359702, PubMed:22037469). Plays a role in modulating cellular differentiation (PubMed:12669231). (updated: Sept. 27, 2017)
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.
- 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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| Variant | Description |
|---|---|
| dbSNP:rs34354104 |
The reference OMIM entry for this protein is 610781
Guanosine monophosphate reductase 2; gmpr2
Gmp reductase 2
CLONING
By database searching with the sequence of GMPR1 (GMPR; 139265) as query, Deng et al. (2002) identified and subsequently cloned GMPR2 from a human fetal brain cDNA library. The deduced 348-amino acid protein has a calculated molecular mass of 37.9 kD and shares 90% sequence identity with GMPR1 and 69% identity with E. coli GMPR. Northern blot analysis detected relatively high levels of both GMPR1 and GMPR2 in heart, skeletal muscle, and kidney, and relatively low levels of both in colon, thymus, and peripheral blood leukocyte. Strong signals of GMPR2 were detected in brain, liver, and placenta, whereas weak signals of GMPR1 were observed in these tissues. The apparent Km of GMPR2 for NADPH and GMP are 26.6 and 17.4 microM, respectively. Zhang et al. (2003) cloned GMPR2 from a human dendritic cell cDNA library. Northern blot analysis detected ubiquitous expression of an approximately 2.2-kb transcript, with high expression in testis, ovary, prostate, heart, liver, spleen, skeletal muscle, and kidney. An additional transcript of about 1.3 kb was detected in placenta. Expression was also detected in most cancer cell lines studied.GENE FUNCTION
Zhang et al. (2003) showed that recombinant GMPR2 protein was able to reduce GMP. Transfection experiments demonstrated that overexpression of GMPR2 promoted the monocytic differentiation of HL-60 leukemia cells.EVOLUTION
Deng et al. (2002) presented evidence that the 2 types of GMP reductase are derived from duplication of an ancient gene.GENE STRUCTURE
Deng et al. (2002) determined that the GMPR2 gene contains 10 exons and spans more than 6.6 kb.MAPPING
By genomic sequence analysis, Deng et al. (2002) mapped the GMPR2 gene to chromosome 14p11.2-p11.1. By the same method, Zhang et al. (2003) mapped the gene to chromosome 14q11-q21. ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610781 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed