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Identification
HMDB Protein ID HMDBP07382
Secondary Accession Numbers
  • 13041
Name Probable glutamate--tRNA ligase, mitochondrial
Synonyms
  1. GluRS
  2. Glutamate--tRNA ligase
  3. Glutamyl-tRNA synthetase
Gene Name EARS2
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By similarity).
Pathways
  • 2-Hydroxyglutric Aciduria (D And L Form)
  • 4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase Deficiency
  • Aminoacyl-tRNA biosynthesis
  • Glutamate Metabolism
  • Homocarnosinosis
  • Hyperinsulinism-Hyperammonemia Syndrome
  • Porphyrin and chlorophyll metabolism
  • Succinic semialdehyde dehydrogenase deficiency
Reactions
Adenosine triphosphate + L-Glutamic acid + tRNA(Glu) → Adenosine monophosphate + Pyrophosphate + L-glutamyl-tRNA(Glu) details
tRNA(Glu) + L-Glutamic acid + Adenosine triphosphate → L-Glutamyl-tRNA(Glu) + Pyrophosphate + Adenosine monophosphate details
GO Classification
Biological Process
glutamyl-tRNA aminoacylation
tRNA aminoacylation for mitochondrial protein translation
Cellular Component
mitochondrial matrix
mitochondrion
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
glutamate-trna ligase activity
ligase activity
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-trna and related compounds
aminoacyl-trna ligase activity
Molecular Function
ATP binding
RNA binding
glutamate-tRNA ligase activity
glutamate-tRNA(Gln) ligase activity
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
glutamyl-trna aminoacylation
biosynthetic process
Cellular Location
  1. Mitochondrion matrix
Gene Properties
Chromosome Location 16
Locus 16p12.2
SNPs EARS2
Gene Sequence
>1572 bp
ATGGCGGCGCTCCTGAGGAGACTGCTGCAGCGCGAGAGGCCTTCGGCGGCCTCTGGCCGC
CCCGTAGGACGGCGCGAGGCCAACCTGGGCACTGATGCCGGGGTTGCGGTGCGAGTGCGG
TTCGCTCCCAGCCCCACAGGCTTCTTGCACCTGGGTGGCCTCCGCACTGCCTTGTACAAC
TACATCTTTGCTAAGAAGTACCAGGGGAGCTTCATCCTGAGGCTAGAGGACACAGATCAG
ACTCGCGTTGTGCCTGGGGCAGCGGAGAATATTGAGGACATGCTGGAGTGGGCAGGCATC
CCGCCTGATGAGAGCCCCCGCCGGGGCGGTCCTGCTGGGCCCTACCAGCAATCTCAGCGG
TTGGAGCTGTATGCCCAGGCCACAGAAGCGCTGCTGAAGACCGGAGCTGCTTACCCCTGT
TTCTGCTCACCCCAGCGGCTGGAGCTCCTGAAGAAGGAGGCCTTGCGGAACCACCAGACG
CCCCGGTATGACAATCGGTGCAGGAACATGAGCCAGGAGCAGGTGGCCCAGAAGCTGGCC
AAGGACCCCAAGCCTGCGATCCGCTTCCGCCTGGAGCAGGTGGTGCCAGCCTTCCAGGAC
CTGGTCTATGGCTGGAATAGGCATGAAGTGGCCAGCGTGGAGGGAGACCCAGTCATCATG
AAGAGCGACGGCTTCCCCACATACCACCTGGCCTGCGTGGTGGACGACCACCACATGGGC
ATCAGCCACGTGCTGCGAGGCTCTGAGTGGCTCGTCTCCACTGCCAAGCACCTGCTCCTC
TACCAGGCCCTGGGCTGGCAGCCACCCCACTTCGCCCACCTGCCCCTGCTCCTCAACAGG
GATGGCAGCAAGCTCTCCAAGAGGCAAGGGGACGTTTTCCTGGAGCACTTTGCTGCTGAT
GGCTTCCTGCCCGATTCCTTGTTGGACATCATCACCAACTGTGGCTCAGGTTTTGCAGAG
AACCAAATGGGCAGGACCCTGCCGGAGCTGATCACACAGTTCAACCTGACACAGGTCACC
TGTCACTCAGCCCTGCTGGACCTGGAGAAGCTCCCAGAATTCAACAGACTGCACCTCCAG
CGGCTGGTGAGCAATGAGAGCCAGAGGCGCCAGCTGGTGGGGAAGCTGCAGGTCCTTGTG
GAGGAGGCCTTTGGTTGCCAGCTGCAAAACAGGGATGTCCTCAACCCAGTCTACGTGGAG
AGGATCCTCCTGCTGAGACAGGGTCACATTTGCCGCCTGCAGGACTTGGTGTCCCCAGTA
TACTCTTACCTGTGGACTCGCCCTGCAGTAGGTCGAGCACAGCTGGACGCCATCTCGGAG
AAGGTGGATGTGATTGCCAAGCGTGTGCTGGGGCTTCTAGAAAGATCTAGTATGAGCTTA
ACTCAGGATATGCTGAATGGAGAACTGAAGAAGCTATCAGAAGGTCTGGAAGGCACCAAG
TACAGTAATGTGATGAAACTCCTTCGGATGGCCCTCAGTGGACAGCAGCAAGGACCTCCT
GTAGCTGAGATGATGTTGGCCTTGGGACCAAAGGAAGTACGGGAACGGATCCAGAAGGTG
GTTTCCAGCTAG
Protein Properties
Number of Residues 523
Molecular Weight 58688.1
Theoretical pI 8.769
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Probable glutamyl-tRNA synthetase, mitochondrial
MAALLRRLLQRERPSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYN
YIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQR
LELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLA
KDPKPAIRFRLEQVVPAFQDLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMG
ISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAAD
GFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQ
RLVSNESQRRQLVGKLQVLVEEAFGCQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPV
YSYLWTRPAVGRAQLDAISEKVDVIAKRVLGLLERSSMSLTQDMLNGELKKLSEGLEGTK
YSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVVSS
GenBank ID Protein 134288884
UniProtKB/Swiss-Prot ID Q5JPH6
UniProtKB/Swiss-Prot Entry Name SYEM_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001083614.1
GeneCard ID EARS2
GenAtlas ID EARS2
HGNC ID HGNC:29419
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  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. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  4. Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed:15779907 ]
  5. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed:11853319 ]