Phenylalanine--tRNA ligase beta subunit (FARSB)
The protein contains 589 amino acids for an estimated molecular weight of 66116 Da.
No function (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.
- 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.
The reference OMIM entry for this protein is 609690
Phenylalanine-trna synthetase, beta subunit; farsb
Phenylalanine-trna synthetase, cytoplasmic, beta subunit; frsb
Phenylalanine-trna synthetase-like, beta subunit; farslb
Phersb
DESCRIPTION
Aminoacyl-tRNA synthetases are enzymes that charge tRNAs with specific amino acids. Cytoplasmic phenylalanine-tRNA synthetase is a heterodimer consisting of a catalytic alpha subunit, FARSA (602918), and a regulatory beta subunit, FARSB (Rodova et al., 1999).CLONING
By database analysis, RT-PCR using embryonic kidney cell RNA, and screening a fetal kidney cDNA library, Rodova et al. (1999) cloned FARSB. The 589-amino acid protein has a predicted molecular mass of 66 kD. Sequence alignment of FARSB orthologs from multiple species showed conservation of DNA-binding domains and suggested the heterodimer of FARSB and FARSA form a 4-helix bundle interface similar to that seen in Thermus thermophilus. Human FARSB is approximately 200 amino acids shorter than its prokaryotic homologs and does not contain the RNP domain that binds to anticodons. Northern blot analysis detected a 2.4-kb FARSB transcript in heart, brain, placenta, skeletal muscle, kidney, and pancreas. FARSB expression was stronger in malignant cell lines compared to normal tissue lines. Using differential display and Northern blot analysis, Zhou et al. (1999) identified murine Farsb as a gene downregulated during suberoylanilide hydroxamic acid-induced differentiation of erythroleukemia cells. Human FARSB shares 93% amino acid identity with its mouse homolog. Lo et al. (2014) reported the discovery of a large number of natural catalytic nulls for each human aminoacyl tRNA synthetase. Splicing events retain noncatalytic domains while ablating the catalytic domain to create catalytic nulls with diverse functions. Each synthetase is converted into several new signaling proteins with biologic activities 'orthogonal' to that of the catalytic parent. The recombinant aminoacyl tRNA synthetase variants had specific biologic activities across a spectrum of cell-based assays: about 46% across all species affect transcriptional regulation, 22% cell differentiation, 10% immunomodulation, 10% cytoprotection, and 4% each for proliferation, adipogenesis/cholesterol transport, and inflammatory response. Lo et al. (2014) identified in-frame splice variants of cytoplasmic aminoacyl tRNA synthetases. They identified 4 catalytic domain-retained splice variants for PheRSb.GENE FUNCTION
Rodova et al. (1999) showed that COS-7 cells transfected with FARSB and FARSA increased phenylalanine charging of tRNA, whereas transfection of FARSB alone caused a decrease in activity of the endogenous heterodimeric enzyme.MAPPING
Using database analysis, Zhou et al. (1999) mapped the FARSB gene to chromosome 2 near the PAX3 gene (606597). ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609690 was added.