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Search results 1 to 89 out of 89 for Aars

0.023s

Categories

Hits by Pathway

Hits by Category

Type Details Score
Strain
MGI:5513940 | C57BL/6N-Dtnbp1<tm1c(EUCOMM)Hmgu>/Tcp
Attribute String: targeted mutation
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Protein
Q3UD67
Organism: Mus musculus/domesticus
Length: 968  
Fragment?: false
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Protein
Q3TZ32
Organism: Mus musculus/domesticus
Length: 968  
Fragment?: false
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Protein
Q6XMP4
Organism: Mus musculus/domesticus
Length: 968  
Fragment?: false
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Protein
Q6PDM7
Organism: Mus musculus/domesticus
Length: 507  
Fragment?: true
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Protein
Q8R346
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: true
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Protein
Q8BGQ7
Organism: Mus musculus/domesticus
Length: 968  
Fragment?: false
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DO Term
DOID:0110177 | Charcot-Marie-Tooth disease axonal type 2N
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Protein Coding Gene
MGI:2384560 | Aars1
Type: protein_coding_gene
Organism: mouse, laboratory
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Gene
16 | AARS1
Type: gene
Organism: human
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Allele
Aars1<sti> | MGI:3618596
 
Name: alanyl-tRNA synthetase 1; sticky
Allele Type: Spontaneous
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Publication
29769718 | J:262421
First Author: Vo MN
Year: 2018
Journal: Nature
Title: ANKRD16 prevents neuron loss caused by an editing-defective tRNA synthetase.
Volume: 557
Issue: 7706
Pages: 510-515
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Publication
16906134 | J:110647
First Author: Lee JW
Year: 2006
Journal: Nature
Title: Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration.
Volume: 443
Issue: 7107
Pages: 50-5
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Strain
MGI:2173990 | B6.Cg-Aars1<sti>/J
Attribute String: congenic, mutant strain, spontaneous mutation
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Publication
21645134 | J:177943
First Author: Sarna JR
Year: 2011
Journal: Eur J Neurosci
Title: Patterned Purkinje cell loss in the ataxic sticky mouse.
Volume: 34
Issue: 1
Pages: 79-86
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Genotype
Genotype
Symbol: Aars1/Aars1
Background: B6.Cg-Aars1/J
Zygosity: hm
Has Mutant Allele: true
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Publication
21115117 | J:171297
First Author: Stum M
Year: 2011
Journal: Mol Cell Neurosci
Title: An assessment of mechanisms underlying peripheral axonal degeneration caused by aminoacyl-tRNA synthetase mutations.
Volume: 46
Issue: 2
Pages: 432-43
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Strain
MGI:6197720 | B6.Cg-Ankrd16<tm1.1Slac> Aars1<sti>
Attribute String: congenic, mutant strain
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Genotype
Genotype
Symbol: Aars1/Aars1 Ankrd16/Ankrd16
Background: B6.Cg-Ankrd16 Aars1
Zygosity: cx
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Aars1/Aars1
Background: involves: C57BL/6J
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Aars1/Aars1
Background: involves: C57BL/6J * FVB/N
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Aars1/Aars1 Ankrd16/Ankrd16
Background: involves: C57BL/6J * CAST/Ei
Zygosity: cx
Has Mutant Allele: true
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Protein
G8DYH7
Organism: Mus musculus/domesticus
Length: 44  
Fragment?: true
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Protein Domain
IPR009080 | tRNAsynth_Ia_anticodon-bd
Type: Homologous_superfamily
Description: Aminoacyl-tRNA synthetase (aaRS) is a key enzyme during protein biosynthesis. Each aaRS contains a catalytic central domain (CCD), responsible for activating amino acid, and an anticodon-binding domain (ABD), necessary for binding the anticodon in cognate tRNA. aaRSs are classified into class I and II (aaRS-I and aaRS-II) based on the topologies of CCDs. Whereas the structure of the CCDs is similar among the members of each of the two different aaRS classes, the ABDs are diverse in structure [].The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases. Both classes of tRNA synthetases have been subdivided into three subclasses, designated Ia, Ib, Ic and IIa, IIb, IIc.This superfamily represents the anticodon binding domain (ABD) of class Ia aminoacyl-tRNA synthetases, and also matches the ABD of glycine tRNA synthetases.
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Protein
Q6PJN8
Organism: Mus musculus/domesticus
Length: 538  
Fragment?: false
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Protein
A0A0A6YWX9
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Publication
15733854 | -
First Author: Tang SN
Year: 2005
Journal: FEBS Lett
Title: Evolution of different oligomeric glycyl-tRNA synthetases.
Volume: 579
Issue: 6
Pages: 1441-5
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Protein Domain
IPR036690 | Fdx_antiC-bd_sf
Type: Homologous_superfamily
Description: Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in the translation of the genetic code by means of covalent attachment of amino acids to theircognate tRNAs. Phenylalanine-tRNA synthetase (PheRS, also known as Phenylalanine-tRNA ligase) is known to be among themost complex enzymes of the aaRS family. Bacterial and mitochondrial PheRSsshare a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents acanonical double split alpha+beta motif having no insertions. The FDX-ACBdomain displays a typical RNA recognition fold (RRM) (see ) formed by the four-stranded antiparallel beta sheet, with two helices packed against it [, , , , ].
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Protein Domain
IPR005121 | Fdx_antiC-bd
Type: Domain
Description: Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in the translation of the genetic code by means of covalent attachment of amino acids to theircognate tRNAs. Phenylalanine-tRNA synthetase (PheRS, also known as Phenylalanine-tRNA ligase) is known to be among themost complex enzymes of the aaRS family. Bacterial and mitochondrial PheRSsshare a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents acanonical double split alpha+beta motif having no insertions. The FDX-ACBdomain displays a typical RNA recognition fold (RRM) (see ) formed by the four-stranded antiparallel beta sheet, with two helices packed against it [, , , , ].
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Publication
25422440 | J:216802
First Author: Liu Y
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: Deficiencies in tRNA synthetase editing activity cause cardioproteinopathy.
Volume: 111
Issue: 49
Pages: 17570-5
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Genotype
Genotype
Symbol: Aars1/Aars1 Ankrd16/Ankrd16
Background: involves: C57BL/6J * CAST/Ei
Zygosity: cx
Has Mutant Allele: true
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Protein
Q7TNP6
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: true
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Publication
18611382 | -
First Author: Klipcan L
Year: 2008
Journal: Structure
Title: The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase.
Volume: 16
Issue: 7
Pages: 1095-104
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Publication
10049785 | -
First Author: Rodova M
Year: 1999
Journal: Biochem Biophys Res Commun
Title: 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.
Volume: 255
Issue: 3
Pages: 765-73
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Publication
12962494 | -
First Author: Moor N
Year: 2003
Journal: Biochemistry
Title: Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end.
Volume: 42
Issue: 36
Pages: 10697-708
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Protein Domain
IPR008909 | DALR_anticod-bd
Type: Domain
Description: Aminoacyl-tRNA synthetase (aaRS) is a key enzyme during protein biosynthesis. Each aaRS contains a catalytic central domain (CCD), responsible for activating amino acid, and an anticodon-binding domain (ABD), necessary for binding the anticodon in cognate tRNA. aaRSs are classified into class I and II (aaRS-I and aaRS-II) based on the topologies of CCDs. Whereas the structure of the CCDs is similar among the members of each of the two different aaRS classes, the ABDs are diverse in structure [].The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases. Both classes of tRNA synthetases have been subdivided into three subclasses, designated Ia, Ib, Ic and IIa, IIb, IIc.This all alpha helical domain is the anticodon binding domain (ABD) of arginyl tRNA synthetase, and also matches the ABD of some glycine tRNA synthetases. This domain is known as the DALR domain after characteristic conserved amino acids [].
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Publication
32253314 | J:293889
First Author: Kim Y
Year: 2020
Journal: Proc Natl Acad Sci U S A
Title: Aminoacyl-tRNA synthetase inhibition activates a pathway that branches from the canonical amino acid response in mammalian cells.
Volume: 117
Issue: 16
Pages: 8900-8911
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Publication
37059185 | J:341137
First Author: Zeng QY
Year: 2023
Journal: J Biol Chem
Title: Loss of threonyl-tRNA synthetase-like protein Tarsl2 has little impact on protein synthesis but affects mouse development.
Volume: 299
Issue: 5
Pages: 104704
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Publication
32484546 | J:291116
First Author: Zheng WQ
Year: 2020
Journal: Nucleic Acids Res
Title: Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation.
Volume: 48
Issue: 12
Pages: 6799-6810
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Publication
12572618 | J:50728
First Author: Diaz-Lazcoz Y
Year: 1998
Journal: Mol Biol Evol
Title: Evolution of genes, evolution of species: the case of aminoacyl-tRNA synthetases.
Volume: 15
Issue: 11
Pages: 1548-61
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Publication
9016717 | -
First Author: Goldgur Y
Year: 1997
Journal: Structure
Title: The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe.
Volume: 5
Issue: 1
Pages: 59-68
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Genotype
Genotype
Symbol: Aars1/Aars1 Ankrd16/Ankrd16
Background: involves: C57BL/6J * CASA/RkJ
Zygosity: cx
Has Mutant Allele: true
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Protein
Q810V2
Organism: Mus musculus/domesticus
Length: 296  
Fragment?: true
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Protein
G3UZX1
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: true
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Protein
Q3UAZ3
Organism: Mus musculus/domesticus
Length: 397  
Fragment?: true
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Publication
31914399 | J:287620
First Author: Hidalgo San Jose L
Year: 2020
Journal: Cell Rep
Title: Modest Declines in Proteome Quality Impair Hematopoietic Stem Cell Self-Renewal.
Volume: 30
Issue: 1
Pages: 69-80.e6
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Publication
25788676 | J:220153
First Author: Liu Y
Year: 2015
Journal: J Neurosci
Title: Mutations in the microtubule-associated protein 1A (Map1a) gene cause Purkinje cell degeneration.
Volume: 35
Issue: 11
Pages: 4587-98
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Protein
Q3UY23
Organism: Mus musculus/domesticus
Length: 622  
Fragment?: false
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Protein
F6W0G8
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: true
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Publication
7664121 | -
First Author: Mosyak L
Year: 1995
Journal: Nat Struct Biol
Title: Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.
Volume: 2
Issue: 7
Pages: 537-47
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Protein
Q3U186
Organism: Mus musculus/domesticus
Length: 578  
Fragment?: false
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Protein
Q9D0I9
Organism: Mus musculus/domesticus
Length: 660  
Fragment?: false
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Protein
Q8BYM8
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
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Protein
Q9ER72
Organism: Mus musculus/domesticus
Length: 831  
Fragment?: false
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Protein
Q3U716
Organism: Mus musculus/domesticus
Length: 748  
Fragment?: false
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Protein
G8DYE4
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: true
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Protein
Q8R2M5
Organism: Mus musculus/domesticus
Length: 536  
Fragment?: true
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Protein
Q99JK2
Organism: Mus musculus/domesticus
Length: 438  
Fragment?: false
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Protein
G8DYK0
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: true
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Protein
A0A494B919
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: true
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Protein
Q3UXN3
Organism: Mus musculus/domesticus
Length: 831  
Fragment?: false
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Protein
G3X975
Organism: Mus musculus/domesticus
Length: 552  
Fragment?: false
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Protein
G8DYH0
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: true
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Protein
G8DYL3
Organism: Mus musculus/domesticus
Length: 75  
Fragment?: true
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Protein
Q499X9
Organism: Mus musculus/domesticus
Length: 586  
Fragment?: false
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Protein
A2RT28
Organism: Mus musculus/domesticus
Length: 586  
Fragment?: false
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Protein
F6YJY2
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: true
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Protein
Q3U2A8
Organism: Mus musculus/domesticus
Length: 1060  
Fragment?: false
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Protein
Q8VDC0
Organism: Mus musculus/domesticus
Length: 902  
Fragment?: false
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Protein
Q8BU30
Organism: Mus musculus/domesticus
Length: 1262  
Fragment?: false
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Protein
Q8BIJ6
Organism: Mus musculus/domesticus
Length: 1012  
Fragment?: false
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Protein
Q8BMJ2
Organism: Mus musculus/domesticus
Length: 1178  
Fragment?: false
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Protein
Q99M01
Organism: Mus musculus/domesticus
Length: 451  
Fragment?: false
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Protein
G3X9Q4
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
Q3TII4
Organism: Mus musculus/domesticus
Length: 895  
Fragment?: true
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Protein
Q14DP3
Organism: Mus musculus/domesticus
Length: 902  
Fragment?: false
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Protein
Q14DS6
Organism: Mus musculus/domesticus
Length: 902  
Fragment?: false
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Protein
Q6ZPT2
Organism: Mus musculus/domesticus
Length: 1210  
Fragment?: true
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Protein
A0A286YCZ5
Organism: Mus musculus/domesticus
Length: 470  
Fragment?: false
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Protein
Q7TSZ3
Organism: Mus musculus/domesticus
Length: 1178  
Fragment?: false
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Protein
Q9Z1Q9
Organism: Mus musculus/domesticus
Length: 1263  
Fragment?: false
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Protein
Q68FL6
Organism: Mus musculus/domesticus
Length: 902  
Fragment?: false
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Protein
E9QB02
Organism: Mus musculus/domesticus
Length: 910  
Fragment?: false
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Protein
Q7TPT7
Organism: Mus musculus/domesticus
Length: 1263  
Fragment?: false
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Protein
Q3U3D3
Organism: Mus musculus/domesticus
Length: 1263  
Fragment?: false
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Protein
G3UY93
Organism: Mus musculus/domesticus
Length: 1278  
Fragment?: true
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Protein
Q790I0
Organism: Mus musculus/domesticus
Length: 1263  
Fragment?: false
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Publication
10447505 | -
First Author: Wolf YI
Year: 1999
Journal: Genome Res
Title: Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events.
Volume: 9
Issue: 8
Pages: 689-710
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom