Aminoacyl-tRNA synthetases consist of a family of enzymes that catalyze the specific aminoacylation of tRNA by their cognate amino acid in the initial step of ribosome-dependent protein biosynthesis. FARSLA, also known as FRSA, CML33, FARSL or PheHA (phenylalanyl-tRNA synthetase, alpha subunit), is a member of the class-II aminoacyl-tRNA synthetase family and is highly expressed in proliferating cells of bone marrow. FARSLA is a cytoplasmic phenylalanine-tRNA synthetase that functions as a heterodimer consisting of a catalytic alpha-subunit and a regulatory beta-subunit. The alpha-subunit is responsible for forming the amino acid binding pocket, mediating the ATP aminoacyl adenylate binding, and interacts with the acceptor stem of the tRNA. FARSLA functions in a cell cycle-dependent and differentiation-dependent manner.