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Identification
HMDB Protein ID HMDBP00274
Secondary Accession Numbers
  • 5506
Name Phenylalanine--tRNA ligase alpha subunit
Synonyms
  1. CML33
  2. PheRS
  3. Phenylalanine--tRNA ligase alpha chain
  4. Phenylalanyl-tRNA synthetase alpha subunit
Gene Name FARSA
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Not Available
Pathways
  • Aminoacyl-tRNA biosynthesis
  • Phenylalanine and Tyrosine Metabolism
  • Phenylketonuria
  • Tyrosinemia Type 2 (or Richner-Hanhart syndrome)
  • Tyrosinemia Type 3 (TYRO3)
Reactions
Adenosine triphosphate + L-Phenylalanine + tRNA(Phe) → Adenosine monophosphate + Pyrophosphate + L-phenylalanyl-tRNA(Phe) details
Adenosine triphosphate + L-Phenylalanine + tRNA(Phe) → Adenosine monophosphate + Pyrophosphate + L-Phenylalanyl-tRNA(Phe) details
GO Classification
Biological Process
phenylalanyl-tRNA aminoacylation
tRNA aminoacylation for protein translation
Cellular Component
cytosol
Component
cell part
intracellular part
cytoplasm
Function
binding
nucleotide binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
ligase activity
nucleic acid binding
rna binding
trna binding
phenylalanine-trna ligase activity
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-trna and related compounds
aminoacyl-trna ligase activity
Molecular Function
ATP binding
phenylalanine-tRNA ligase activity
tRNA binding
Process
rna metabolic process
ncrna metabolic process
trna metabolic process
trna aminoacylation
trna aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
biosynthetic process
phenylalanyl-trna aminoacylation
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 19
Locus 19p13.2
SNPs FARSA
Gene Sequence
>1527 bp
ATGGCGGATGGTCAGGTGGCGGAACTGCTGCTCCGGCGGCTGGAGGCGTCTGATGGCGGC
CTGGACAGCGCCGAGTTGGCGGCTGAGCTGGGCATGGAGCACCAGGCGGTGGTGGGCGCC
GTGAAGAGCCTTCAGGCGCTGGGCGAGGTCATCGAGGCTGAACTTCGGTCCACCAAGCAC
TGGGAGCTTACTGCGGAGGGCGAGGAGATTGCCCGGGAGGGCAGCCATGAGGCCCGTGTG
TTTCGAAGCATTCCCCCAGAGGGCCTGGCCCAGAGCGAGCTTATGCGACTGCCCAGTGGC
AAAGTGGGCTTCAGCAAGGCCATGTCCAACAAGTGGATTCGGGTGGACAAGAGTGCGGCT
GACGGGCCCCGGGTGTTCCGAGTGGTGGACAGCATGGAGGATGAGGTGCAGCGGCGGCTC
CAGCTGGTCCGGGGGGGACAGGCTGAGAAGCTGGGGGAGAAGGAGAGGAGCGAGCTGAGG
AAGAGGAAGCTGTTGGCTGAAGTGACTCTGAAGACCTACTGGGTGAGCAAAGGCAGTGCC
TTTAGTACCAGCATCTCCAAGCAAGAGACAGAGCTGAGCCCAGAGATGATCTCCAGTGGC
TCTTGGCGGGACCGGCCCTTCAAGCCCTACAACTTCTTGGCCCACGGTGTCCTCCCCGAC
AGCGGCCACCTTCACCCGCTGCTCAAGGTCCGCTCCCAGTTCCGACAGATCTTCCTGGAG
ATGGGGTTCACCGAGATGCCGACTGATAACTTCATTGAGAGCTCCTTCTGGAACTTTGAC
GCCCTCTTCCAGCCCCAGCAGCACCCAGCCCGTGACCAGCACGACACCTTCTTCCTTCGA
GATCCAGCGGAGGCCCTGCAGCTCCCAATGGACTATGTCCAGCGGGTCAAGCGGACCCAC
TCTCAGGGCGGCTACGGCTCACAGGGGTACAAGTATAACTGGAAGCTGGACGAGGCCCGG
AAAAACCTACTGCGAACCCACACCACATCAGCCAGCGCCCGTGCGCTCTACCGCCTTGCC
CAGAAGAAGCCCTTCACTCCGGTCAAGTACTTCTCCATCGACCGCGTATTCCGGAATGAG
ACCCTGGACGCCACGCACCTGGCTGAGTTCCACCAGATCGAGGGCGTGGTGGCGGATCAT
GGTCTCACCTTGGGCCACCTCATGGGCGTTCTGCGGGAGTTCTTCACCAAGCTGGGTATC
ACGCAACTCCGCTTCAAGCCAGCCTACAACCCATACACAGAGCCCAGCATGGAGGTGTTC
AGCTACCACCAAGGCCTGAAGAAGTGGGTGGAGGTCGGAAACTCGGGGGTCTTCCGTCCA
GAGATGCTGCTGCCCATGGGGCTTCCCGAGAACGTGTCGGTCATTGCCTGGGGCCTCTCC
CTGGAGCGCCCAACGATGATCAAATATGGCATCAACAATATCCGGGAGCTGGTGGGCCAC
AAGGTGAACCTGCAGATGGTGTATGACAGTCCCCTGTGCCGCCTGGATGCCGAGCCGAGG
CCCCCTCCCACACAGGAGGCTGCGTGA
Protein Properties
Number of Residues 508
Molecular Weight 57563.225
Theoretical pI 7.793
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Phenylalanyl-tRNA synthetase alpha chain
MADGQVAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAELRSTKH
WELTAEGEEIAREGSHEARVFRSIPPEGLAQSELMRLPSGKVGFSKAMSNKWIRVDKSAA
DGPRVFRVVDSMEDEVQRRLQLVRGGQAEKLGEKERSELRKRKLLAEVTLKTYWVSKGSA
FSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLE
MGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEALQLPMDYVQRVKRTH
SQGGYGSQGYKYNWKLDEARKNLLRTHTTSASARALYRLAQKKPFTPVKYFSIDRVFRNE
TLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKLGITQLRFKPAYNPYTEPSMEVF
SYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGH
KVNLQMVYDSPLCRLDAEPRPPPTQEAA
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9Y285
UniProtKB/Swiss-Prot Entry Name SYFA_HUMAN
PDB IDs
GenBank Gene ID U07424
GeneCard ID FARSA
GenAtlas ID FARSA
HGNC ID HGNC:3592
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
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  7. Sen S, Zhou H, Ripmaster T, Hittelman WN, Schimmel P, White RA: 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. 1997 Jun 10;94(12):6164-9. [PubMed:9177188 ]
  8. Rodova M, Ankilova V, Safro MG: 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. 1999 Feb 24;255(3):765-73. [PubMed:10049785 ]