farsb
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  • Official Full Name
  • phenylalanyl-tRNA synthetase, beta subunit
  • Background
  • 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. 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
  • Synonyms
  • FARSB; phenylalanyl-tRNA synthetase, beta subunit; FARSLB, phenylalanyl tRNA synthetase like, beta subunit; phenylalanine--tRNA ligase beta subunit; FRSB; PheHB; phenylalanine tRNA ligase 1; beta; cytoplasmic; phenylalanine-tRNA ligase beta chain; phenyl; PheRS; FARSLB; HSPC173; phenylalanyl-tRNA synthetase beta chain; OTTHUMP00000164205; phenylalanine--tRNA ligase beta chain; phenylalanyl-tRNA synthetase beta-subunit; phenylalanine tRNA ligase 1, beta, cytoplasmic; phenylalanyl-tRNA synthetase-like, beta subunit; phenylalanine-tRNA synthetase-like, beta subunit
Cat.#:FARSB-3848HTag:GST
Source (Host):Wheat GermSpecies:Human
Product nameRecombinant Human FARSB Protein, GST-tagged
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Cat.#:FARSB-12750HTag:His
Source (Host):E. coliSpecies:Human
Product nameRecombinant Human FARSB, His-tagged
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Cat.#:FARSB-5684MTag:His
Source (Host):Mammalian CellsSpecies:Mouse
Product nameRecombinant Mouse FARSB Protein
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Cat.#:FARSB-1681CTag:His
Source (Host):Mammalian CellsSpecies:Chicken
Product nameRecombinant Chicken FARSB
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Cat.#:FARSB-1844ZTag:His
Source (Host):Mammalian CellsSpecies:Zebrafish
Product nameRecombinant Zebrafish FARSB
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Cat.#:FARSB-6325HCLTag:
Source (Host):Species:Human
Product nameRecombinant Human FARSB 293 Cell Lysate
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Involved Pathway

FARSB involved in several pathways and played different roles in them. We selected most pathways FARSB participated on our site, such as Aminoacyl-tRNA biosynthesis, Cytosolic tRNA aminoacylation, Gene Expression, which may be useful for your reference. Also, other proteins which involved in the same pathway with FARSB were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name
Pathway Related Protein
Aminoacyl-tRNA biosynthesis
RARS2; AARS; SEPSECS; FARS2; IARS; MADD; WARS2; FARSA; PET112L; HARS
Cytosolic tRNA aminoacylation
KARS; EEF1E1; AIMP2; FARSB; AIMP1; DARS; AARS; MADD
Gene Expression
TBX5A; IGF2BP3; ZNF230; ZNF548; TXN; COX7C; HBXIP; ZNF658; NSUN2; DDX20
tRNA Aminoacylation
AIMP1; EARS2; AIMP2; DARS; WARS2; FARSB; KARS; AARS; MADD; EEF1E1

Protein Function

FARSB has several biochemical functions, for example, ATP binding, RNA binding, magnesium ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by FARSB itself. We selected most functions FARSB had, and list some proteins which have the same functions with FARSB. You can find most of the proteins on our site.
Function
Related Protein
Function ATP binding
Related Protein ATP1A1A.5; ACLY; PSMC3; MYO19; ACTR2A; FGFR2; IKBKB; CDC34B; ERBB2; PRKACAA
Function RNA binding
Related Protein PCBP4; HNRNPAB; RNASEH2A; DDX25; RBM18; MIF4GD; RBM44; RNASEL4; RBM14; RPL24
Function magnesium ion binding
Related Protein ATP11A; ENO1B; SIK2; NIM1; PKM; SRPK1; PKLR; PSPH; TSSK4; NLK
Function phenylalanine-tRNA ligase activity
Related Protein FARS2; FARSB; FDXACB1; FARSA

Interacting Protein

FARSB has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with FARSB here. Most of them are supplied by our site. Hope this information will be useful for your research of FARSB.
VCAM1; ACTB; DDA1; FN1; EIF2AK2; HDGF; SLX4

FARSB Related Articles

Carr, JF; Danziger, ME; et al. Engineering the Genome of Thermus thermophilus Using a Counterselectable Marker. JOURNAL OF BACTERIOLOGY 197:1135-1144(2015).
Mermershtain, I; Finarov, I; et al. Idiosyncrasy and identity in the prokaryotic phe-system: Crystal structure of E-coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP. PROTEIN SCIENCE 20:160-167(2011).