Phosphoribosylformylglycinamidine synthase (PFAS)
The protein contains 1338 amino acids for an estimated molecular weight of 144734 Da.
Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity). (updated: March 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.
- 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.
- 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.
- 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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| Variant | Description |
|---|---|
| dbSNP:rs9891699 | |
| dbSNP:rs4791641 | |
| dbSNP:rs35217368 | |
| dbSNP:rs11078738 |
Biological Process
'de novo' IMP biosynthetic process
Anterior head development
Glutamine metabolic process
Nucleobase-containing small molecule metabolic process
Purine nucleobase biosynthetic process
Purine nucleobase metabolic process
Purine nucleotide biosynthetic process
Purine ribonucleoside monophosphate biosynthetic process
Response to drug
Ribonucleoside monophosphate biosynthetic process
Small molecule metabolic process
Molecular Function
ATP binding
Metal ion binding
Phosphoribosylformylglycinamidine synthase activity
The reference OMIM entry for this protein is 602133
Phosphoribosylformylglycinamidine synthase; pfas
Phosphoribosylformylglycinamide amidotransferase; fgarat
DESCRIPTION
Five-prime-phosphoribosyl N-formylglycinamide (FGAR) amidotransferase (EC 6.3.5.3) catalyzes the fourth reaction in the de novo synthesis of purines, that is, the conversion of FGAR to 5-prime-phosphoribosyl N-formylglycinamidine (FGAM) (summary by Barnes et al., 1994).CLONING
Barnes et al. (1994) purified and characterized phosphoribosylformylglycinamide amidotransferase (FGARAT) the fourth enzyme in the de novo purine pathway.GENE FUNCTION
The human GARS-AIRS-GART locus (138440), located on chromosome 21, encodes 3 of the 10 enzymatic steps necessary for the conversion of phosphoribosyl pyrophosphate to inosine monophosphate by the de novo purine pathway. The 3 enzyme activities are encoded in a linear, nonoverlapping fashion on the GARS-AIRS-GART mRNA, starting at the 5-prime end of the cDNA. These enzymatic activities catalyze the second, fifth, and third step of the de novo purine pathway, respectively. FGARAT catalyzes the fourth step in the pathway (summary by Brodsky et al., 1997). Brodsky et al. (1997) reported that, unlike the developmentally regulated expression of the GARS-AIRS-GART locus, expression of the FGARAT gene appears to be constitutive.MAPPING
By analysis of somatic cell hybrids, Barnes et al. (1994) mapped the PFAS gene to chromosome 17p. ... 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
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 602133 was added.