Hmdb loader
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP00625
Secondary Accession Numbers
  • 5897
Name Alanine--tRNA ligase, cytoplasmic
Synonyms
  1. AlaRS
  2. Alanine--tRNA ligase
  3. Renal carcinoma antigen NY-REN-42
  4. Alanyl-tRNA synthetase
Gene Name AARS
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain (By similarity).
Pathways
  • Alanine, aspartate and glutamate metabolism
  • Aminoacyl-tRNA biosynthesis
  • Lactic Acidemia
  • Primary Hyperoxaluria Type I
  • Pyruvate Carboxylase Deficiency
Reactions
Adenosine triphosphate + L-Alanine + tRNA(Ala) → Adenosine monophosphate + Pyrophosphate + L-alanyl-tRNA(Ala) details
Adenosine triphosphate + L-Alanine + tRNA(Ala) → Adenosine monophosphate + Pyrophosphate + L-Alanyl-tRNA details
GO Classification
Biological Process
neuromuscular process controlling balance
response to amino acid stimulus
negative regulation of neuron apoptotic process
protein folding
endoplasmic reticulum unfolded protein response
alanyl-tRNA aminoacylation
cerebellar Purkinje cell layer development
tRNA modification
tRNA processing
skin development
hair follicle development
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
alanine-trna ligase activity
nucleic acid binding
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-trna and related compounds
aminoacyl-trna ligase activity
Molecular Function
metal ion binding
ATP binding
alanine-tRNA ligase activity
aminoacyl-tRNA editing activity
amino acid binding
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
alanyl-trna aminoacylation
biosynthetic process
Cellular Location
  1. Cytoplasm (Potential)
Gene Properties
Chromosome Location 16
Locus 16q22
SNPs AARS
Gene Sequence
>2907 bp
ATGGACTCTACTCTAACAGCAAGTGAAATCCGGCAGCGATTTATAGATTTCTTCAAGAGG
AACGAGCATACGTATGTTCACTCGTCTGCCACCATCCCATTGGATGACCCCACTTTGCTC
TTTGCCAATGCAGGCATGAACCAGTTTAAACCCATTTTCCTGAACACAATTGACCCATCT
CACCCCATGGCAAAGCTGAGCAGAGCTGCCAATACCCAGAAGTGCATCCGGGCTGGGGGC
AAACATAATGACCTGGACGATGTGGGCAAGGATGTCTATCATCACACCTTCTTCGAGATG
CTGGGCTCTTGGTCTTTTGGAGATTACTTTAAGGAATTGGCATGTAAGATGGCTCTGGAA
CTCCTCACCCAAGAGTTTGGCATTCCCATTGAAAGACTTTATGTTACTTACTTTGGCGGG
GATGAAGCAGCTGGCTTAGAAGCAGATCTGGAATGCAAACAGATCTGGCAAAATTTGGGG
CTGGATGACACCAAAATCCTCCCAGGCAACATGAAGGATAACTTCTGGGAGATGGGTGAC
ACGGGCCCCTGTGGTCCTTGCAGTGAGATCCACTACGACCGGATTGGTGGTCGGGACGCC
GCACATCTTGTCAACCAGGACGACCCTAATGTGCTGGAGATCTGGAACCTTGTGTTCATC
CAGTATAACAGGGAAGCTGATGGCATTCTGAAACCTCTTCCCAAGAAAAGCATTGACACA
GGGATGGGCCTGGAACGACTGGTATCTGTGCTGCAGAATAAGATGTCCAACTATGACACT
GACCTTTTTGTCCCTTACTTTGAAGCCATTCAGAAGGGCACAGGTGCCCGACCATACACT
GGGAAAGTTGGTGCTGAGGATGCCGATGGGATTGACATGGCCTACCGGGTGCTGGCTGAC
CACGCTCGGACCATCACTGTGGCACTGGCTGATGGTGGCCGGCCTGACAACACAGGGCGT
GGATATGTGTTGAGACGGATTCTCCGCCGAGCTGTCCGATACGCCCATGAAAAGCTCAAT
GCCAGCAGGGGCTTCTTTGCTACGTTAGTGGATGTTGTCGTCCAGTCCCTGGGAGATGCA
TTTCCTGAGCTGAAGAAGGACCCAGACATGGTGAAGGACATCATTAATGAAGAAGAGGTG
CAGTTTCTCAAGACTCTCAGCAGAGGGCGTCGCATCCTGGACAGGAAAATTCAGAGCCTG
GGAGACAGCAAGACCATTCCCGGAGACACTGCTTGGCTCCTCTATGACACCTATGGGTTT
CCAGTGGATCTGACTGGACTGATTGCTGAAGAGAAGGGCCTGGTGGTAGACATGGATGGC
TTTGAAGAGGAGAGGAAACTGGCCCAGCTGAAATCACAGGGCAAGGGAGCTGGTGGGGAA
GACCTCATTATGCTGGACATTTACGCTATCGAAGAGCTCCGGGCACGGGGTCTGGAGGTC
ACAGATGATTCCCCAAAGTACAATTACCATTTGGACTCCAGTGGTAGCTATGTATTTGAG
AACACAGTGGCTACGGTGATGGCTCTGCGCAGGGAGAAGATGTTCGTGGAAGAGGTGTCC
ACAGGCCAGGAGTGTGGAGTGGTGCTGGACAAGACCTGTTTCTATGCTGAGCAAGGAGGC
CAGATCTATGACGAAGGCTACCTGGTGAAGGTGGATGACAGCAGTGAAGATAAAACAGAG
TTTACAGTGAAGAATGCTCAGGTCCGAGGAGGGTATGTGCTACACATTGGAACCATCTAC
GGTGACCTGAAAGTGGGGGATCAGGTCTGGCTGTTTATTGATGAGCCCCGACGAAGACCC
ATCATGAGCAACCACACAGCTACGCACATTCTGAACTTCGCCCTGCGCTCAGTGCTTGGG
GAAGCTGACCAGAAAGGCTCATTGGTTGCTCCTGACCGCCTCAGATTTGACTTTACTGCC
AAGGGAGCCATGTCCACCCAACAGATCAAGAAGGCTGAAGAGATTGCTAATGAGATGATT
GAGGCAGCCAAGGCCGTCTATACCCAGGATTGCCCCCTGGCAGCAGCGAAAGCCATCCAG
GGCCTACGGGCTGTGTTTGATGAGACCTATCCTGACCCTGTGCGAGTCGTCTCCATTGGG
GTCCCGGTGTCCGAGTTGCTGGATGACCCCTCTGGGCCTGCTGGCTCCCTGACTTCTGTT
GAGTTCTGTGGGGGAACGCACCTGCGGAACTCGAGTCATGCAGGAGCTTTTGTGATCGTG
ACGGAAGAAGCCATTGCCAAGGGTATCCGGAGGATTGTGGCTGTCACAGGTGCCGAGGCC
CAGAAGGCCCTCAGGAAAGCAGAGAGCTTGAAGAAATGTCTCTCTGTCATGGAAGCCAAA
GTGAAGGCTCAGACTGCTCCAAACAAGGATGTGCAGAGGGAGATCGCTGACCTTGGAGAG
GCCCTGGCCACTGCAGTCATCCCCCAGTGGCAGAAGGATGAATTGCGGGAGACTCTCAAA
TCCCTAAAGAAGGTCATGGATGACTTGGACCGAGCCAGCAAAGCCGATGTCCAGAAACGA
GTGTTAGAGAAGACGAAGCAGTTCATCGACAGCAACCCCAACCAGCCTCTTGTCATCCTG
GAGATGGAGAGCGGCGCCTCAGCCAAGGCCCTGAATGAAGCCTTGAAGCTCTTCAAGATG
CACTCCCCTCAGACTTCTGCCATGCTCTTCACGGTGGACAATGAGGCTGGCAAGATCACG
TGCCTGTGTCAAGTTCCCCAGAATGCAGCCAATCGGGGCTTAAAAGCCAGCGAGTGGGTG
CAGCAGGTGTCAGGCTTGATGGACGGTAAAGGTGGTGGCAAGGATGTGTCTGCACAGGCC
ACAGGCAAGAACGTTGGCTGCCTGCAGGAGGCGCTGCAGCTGGCCACTTCCTTCGCCCAG
CTGCGCCTCGGGGATGTAAAGAACTGA
Protein Properties
Number of Residues 968
Molecular Weight 106809.525
Theoretical pI 5.53
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Alanyl-tRNA synthetase, cytoplasmic
MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPS
HPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALE
LLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGD
TGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNREADGILKPLPKKSIDT
GMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLAD
HARTITVALADGGRPDNTGRGYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDA
FPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGF
PVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEV
TDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGG
QIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRP
IMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMI
EAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSV
EFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAK
VKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKR
VLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKIT
CLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQ
LRLGDVKN
GenBank ID Protein 109148542
UniProtKB/Swiss-Prot ID P49588
UniProtKB/Swiss-Prot Entry Name SYAC_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001605.2
GeneCard ID AARS
GenAtlas ID AARS
HGNC ID HGNC:20
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  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. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  5. 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 ]
  6. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed:10508479 ]
  7. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed:15616553 ]
  8. Shiba K, Ripmaster T, Suzuki N, Nichols R, Plotz P, Noda T, Schimmel P: Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition. Biochemistry. 1995 Aug 22;34(33):10340-9. [PubMed:7654687 ]
  9. Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P: The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science. 2009 Aug 7;325(5941):744-7. doi: 10.1126/science.1174343. [PubMed:19661429 ]
  10. Latour P, Thauvin-Robinet C, Baudelet-Mery C, Soichot P, Cusin V, Faivre L, Locatelli MC, Mayencon M, Sarcey A, Broussolle E, Camu W, David A, Rousson R: A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. Am J Hum Genet. 2010 Jan;86(1):77-82. doi: 10.1016/j.ajhg.2009.12.005. Epub 2009 Dec 31. [PubMed:20045102 ]