ALANIINIA koskevaa. Alaniini- tRNA- syntetaasi AARS

 Alaniinia koskevaa

AARS, Kr. 16q22.1  (sytoplasminen entsyymi )

AARS2, Kr. 6p21.1. ( mitokondriaalinen)

• AARS alanyl-tRNA synthetase [ Homo sapiens (human) ]

Gene ID: 16, updated on 4-Jun-2017

Summary

Official Symbol

AARSprovided by HGNC

Official Full Name

alanyl-tRNA synthetaseprovided by HGNC

Primary source

HGNC:HGNC:20

See related

Ensembl:ENSG00000090861 MIM:601065; Vega:OTTHUMG00000177042

Gene type

protein coding

RefSeq status

REVIEWED

Organism

Homo sapiens

Lineage

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo

Also known as

CMT2N; EIEE29

Summary

The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41% identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. [provided by RefSeq, Jul 2008]Related articles in PubMed

1. Genotype/phenotype correlations in AARS-related neuropathy in a cohort of patients from the United Kingdom and Ireland. Bansagi B, et al. J Neurol, 2015 Aug. PMID 26032230, Free PMC Article
2. A novel AARS mutation in a family with dominant myeloneuropathy. Motley WW, et al. Neurology, 2015 May 19. PMID 25904691, Free PMC Article Mitokondriaali
3. Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-recessive early-onset epileptic encephalopathy with persistent myelination defect. Simons C, et al. Am J Hum Genet, 2015 Apr 2. PMID 25817015, Free PMC Article
4. Alanyl-tRNA synthetase mutation in a family with dominant distal hereditary motor neuropathy. Zhao Z, et al. Neurology, 2012 May 22. PMID 22573628, Free PMC Article
5. A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N). McLaughlin HM, et al. Hum Mutat, 2012 Jan. PMID 22009580, Free PMC Article
   

See all (38) citations in PubMed
See citations in PubMed for homologs of this gene provided by HomoloGene
 

GeneRIFs: Gene References Into Functions

1. Number of missense mutations in AARS expand the clinical spectrum and provide pheno-genotypic correlations in AARS-related neuropathies.
2. A novel mutation in alanyl-tRNA synthetase causes a mild myeloneuropathy, a novel phenotype for patients with mutations in one of the tRNA synthetase genes.
3. Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-recessive early-onset epileptic encephalopathy with persistent myelination defect.
4. the pathological consequences of diminished tRNA synthetase editing activity, and thus translational infidelity, are dependent on the cell type and the extent of editing disruption
5. in a family with distal hereditary motor neuropathy (dHMN), all 4 affected family members had a heterozygous missense mutation c.2677G>A (p.D893N) of (AARS), not found in the 4 unaffected members and control subjects; conclude AARS mutation caused dHMN in a Chinese family; AARS mutations result in not only a CMT phenotype but also a dHMN phenotype
6. Methylation-mediated deamination of a CpG dinucleotide gives rise to the recurrent p.Arg329His alanyl-tRNA synthetase mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N).
7. We show here that mutations in AARS2 cause perinatal or infantile cardiomyopathy with near-total combined mitochondrial respiratory chain deficiency in the heart.
8. cytoplasmic Alanyl-tRNA synthetase may have a role in dominant axonal Charcot-Marie-Tooth disease, as shown by its mutation in a major determinant for binding and aminoacylation
   

AARS2, (mitokondriaalinen entsyymi)

• AARS2 alanyl-tRNA synthetase 2, mitochondrial [ Homo sapiens (human) ]

Gene ID: 57505, updated on 4-Jun-2017

Summary

Official Symbol

AARS2provided by HGNC

Official Full Name

alanyl-tRNA synthetase 2, mitochondrialprovided by HGNC

Primary source

HGNC:HGNC:21022

See related

Ensembl:ENSG00000124608 MIM:612035; Vega:OTTHUMG00000014766

Gene type

protein coding

RefSeq status

REVIEWED

Organism

Homo sapiens

Lineage

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo

Also known as

AARSL; LKENP; COXPD8; MTALARS; MT-ALARS

Summary

The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases play critical roles in mRNA translation by charging tRNAs with their cognate amino acids. The encoded protein is a mitochondrial enzyme that specifically aminoacylates alanyl-tRNA. Mutations in this gene are a cause of combined oxidative phosphorylation deficiency 8. [provided by RefSeq, Dec 2011]

Orthologs

mouse all

Related articles in PubMed

1. Analysis of Mutations in AARS2 in a Series of CSF1R-Negative Patients With Adult-Onset Leukoencephalopathy With Axonal Spheroids and Pigmented Glia. Lynch DS, et al. JAMA Neurol, 2016 Dec 1. PMID 27749956
2. Novel AARS2 gene mutation producing leukodystrophy: a case report. Szpisjak L, et al. J Hum Genet, 2017 Feb. PMID 27734837
3. The first Japanese case of leukodystrophy with ovarian failure arising from novel compound heterozygous AARS2 mutations. Hamatani M, et al. J Hum Genet, 2016 Oct. PMID 27251004
4. Novel (ovario) leukodystrophy related to AARS2 mutations. Dallabona C, et al. Neurology, 2014 Jun 10. PMID 24808023, Free PMC Article
5. Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy. Götz A, et al. Am J Hum Genet, 2011 May 13. PMID 21549344, Free PMC Article
   

See all (25) citations in PubMed
See citations in PubMed for homologs of this gene provided by HomoloGene
 

GeneRIFs: Gene References Into Functions

1. Mutations in AARS2 in a Series of CSF1R-Negative Patients With Adult-Onset Leukoencephalopathy With Axonal Spheroids and Pigmented Glia.
2. This paper documented a new, nonsense AARS2 gene mutation (c.578T>G, p.Leu193*) and a known missense mutation (c.595C>T, p.Arg199Cys) associated with leukoencephalopathy in a male patient.
3. we describe a Japanese woman with novel compound heterozygous mutations in AARS2, the first report of leukodystrophy caused by AARS2 mutations in Asia.
4. A new phenotype caused by AARS2 mutations is characterized by leukoencephalopathy and ovarian failure in female patients, indicating that the phenotypic spectrum associated with AARS2 variants is much wider than previously reported.
5. Mutations in AARS2 found in lethal mitochondrial myopathy
6. Observational study of gene-disease association. (HuGE Navigator)
   

Muistiin 5.6. 2017