FARSB

Phenylalanyl-tRNA synthetase, beta subunit
Identifiers
Symbols	FARSB ; FARSLB; FRSB; HSPC173; PheHB; PheRS
External IDs	Template:OMIM5 Template:MGI HomoloGene: 4160
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Phenylalanyl-tRNA synthetase, beta subunit, also known as FARSB, is a human gene.

This gene encodes a highly conserved enzyme that belongs to the aminoacyl-tRNA synthetase class IIc subfamily. This enzyme comprises the regulatory beta subunits that form a tetramer with two catalytic alpha subunits. In the presence of ATP, this tetramer is responsible for attaching L-phenylalanine to the terminal adenosine of the appropriate tRNA. A pseudogene located on chromosome 10 has been identified.

Further reading

• Archambault de Vencay J, Thomes JC, Julien R (1978). "Phenylalanyl-tRNA synthetase of the human placenta. Evidence for different enzymatic forms in equilibrium". FEBS Lett. 89 (1): 98–102. PMID 658405.CS1 maint: Multiple names: authors list (link)
• Nazarenko IA, Peterson ET, Zakharova OD; et al. (1992). "Recognition nucleotides for human phenylalanyl-tRNA synthetase". Nucleic Acids Res. 20 (3): 475–8. PMID 1741281.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sen S, Zhou H, Ripmaster T; et al. (1997). "Expression of a gene encoding a tRNA synthetase-like protein is enhanced in tumorigenic human myeloid leukemia cells and is cell cycle stage- and differentiation-dependent". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6164–9. PMID 9177188.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rodova M, Ankilova V, Safro MG (1999). "Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells". Biochem. Biophys. Res. Commun. 255 (3): 765–73. doi:10.1006/bbrc.1999.0141. PMID 10049785.CS1 maint: Multiple names: authors list (link)
• Zhou X, Richon VM, Ngo L; et al. (1999). "Cloning of the cDNA encoding phenylalanyl tRNA synthetase regulatory alpha-subunit-like protein whose expression is down-regulated during differentiation". Gene. 233 (1–2): 13–9. PMID 10375616.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Zhang QH, Ye M, Wu XY; et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. PMID 11042152.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Moor N, Linshiz G, Safro M (2002). "Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymes". Protein Expr. Purif. 24 (2): 260–7. doi:10.1006/prep.2001.1560. PMID 11858721.CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Moor N, Lavrik O, Favre A, Safro M (2003). "Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end". Biochemistry. 42 (36): 10697–708. doi:10.1021/bi034732q. PMID 12962494.CS1 maint: Multiple names: authors list (link)
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yu XY, Finn J, Hill JM; et al. (2004). "A series of spirocyclic analogues as potent inhibitors of bacterial phenylalanyl-tRNA synthetases". Bioorg. Med. Chem. Lett. 14 (5): 1339–42. doi:10.1016/j.bmcl.2003.11.081. PMID 14980694.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Vasil'eva IA, Bogachev VS, Favre A; et al. (2005). "Role of low-molecular-weight substrates in functional binding of the tRNAPhe acceptor end by phenylalanyl-tRNA synthetase". Biochemistry Mosc. 69 (2): 143–53. PMID 15000680.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Andersen JS, Lam YW, Leung AK; et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)