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Information on EC 6.1.1.21 - histidine-tRNA ligase and Organism(s) Mus musculus and UniProt Accession Q61035

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Mus musculus
UNIPROT: Q61035 not found.
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
histidyl-trna synthetase, hisrs, hars2, jo-1 antigen, histidyl trna synthetase, histidyl-transfer rna synthetase, histidine-trna ligase, class ii histidyl-trna synthetase, hars1, mitochondrial histidyl trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Histidine translase
-
histidine-tRNA ligase
-
histidine-tRNA ligase homolog
-
Histidyl-transfer ribonucleate synthetase
-
Histidyl-tRNA synthetase
-
Jo-1 antigen
-
Synthetase, histidyl-transfer ribonucleate
-
HisRS
Histidine translase
-
-
-
-
Histidine--tRNA ligase
-
-
-
-
Histidine--tRNA ligase homolog
-
-
-
-
Histidyl-transfer ribonucleate synthetase
-
-
-
-
histidyl-transfer RNA synthetase
-
-
Histidyl-tRNA synthetase
-
-
-
-
Jo-1
-
-
-
-
Jo-1 antigen
-
-
-
-
Synthetase, histidyl-transfer ribonucleate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
Aminoacylation
-
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-histidine:tRNAHis ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9068-78-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
mouse HisRS without adjuvant, containing Toll-like receptor TLR-4, can induce sustained muscle inflammation and an adaptive immune response to HisRS. Mice lacking TLR-4 show that the ability of mouse HisRS to produce muscle inflammation does not require TLR-4 signaling, nor is it dependent on recognition of B cell and T cell receptors. When TLR-4-deficient animals are immunized with HisRS, they have a preserved inflammatory response in muscle but fail to generate a HisRS antibody response
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HARS1_MOUSE
509
0
57432
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57400
x * 57400, amino acid sequence determination
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 57400, amino acid sequence determination
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of Egr1 null or defect mutants affects HisRS genes, Egr1, Zif268, is an immediate early gene encoding an inducible transcription factor involved in synaptic plasticity and several forms of memory in rodents, allelic differences between mouse strains can introduce variations in differential proteomic analyses of genetically modified organisms
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis of HisRS gene variants, HisRS genes, which map closely to the Egr1 locus, have conserved the 129/Sv haplotype despite numerous back-crossing of the null mice progeny with C57Bl/6J animals, genetic analysis of isozymes of HisRS encoded by the 129/Sv haplotype, allelic difference for mortalin and HisRS between 129/Sv and C57Bl/6J strains, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Freist, W.; Verhey, J.F.; Ruhlmann, A.; Gauss, D.H.; Arnez, J.G.
Histidyl-tRNA synthetase
Biol. Chem.
380
623-646
1999
Archaeoglobus fulgidus (O28631), Salmonella enterica subsp. enterica serovar Typhimurium (O52765), Mesocricetus auratus (P07178), Saccharomyces cerevisiae (P07263), Homo sapiens (P12081), Homo sapiens (P49590), Streptococcus dysgalactiae subsp. equisimilis (P30053), Caenorhabditis elegans (P34183), Haemophilus influenzae (P43823), Mycobacterium leprae (P46696), Mycoplasma genitalium (P47281), Porphyra purpurea (P51348), Thermus thermophilus (P56194), Thermus thermophilus, Helicobacter pylori (P56455), Escherichia coli (P60906), Escherichia coli, Takifugu rubripes (P70076), Mycoplasma pneumoniae (P75069), Oryza sativa (P93422), Mycobacterium tuberculosis (P9WFV5), Synechococcus sp. (Q55267), Synechocystis sp. (Q55653), Methanocaldococcus jannaschii (Q58406), Mus musculus (Q61035), Mycobacterium tuberculosis H37Rv (P9WFV5)
Manually annotated by BRENDA team
Chardonnet, S.; Decottignies, P.; Amar, L.; Le Caer, J.P.; Davis, S.; Laroche, S.; Le Marechal, P.
New mortalin and histidyl tRNA synthetase isoforms point out a pitfall in proteomic analysis of Egr1 genetically modified mice
Proteomics
7
289-298
2007
Mus musculus
Manually annotated by BRENDA team
Casciola-Rosen, L.
Histidyl-transfer RNA synthetase: A key participant in idiopathic inflammatory myopathies
Arthritis Rheum.
63
331-333
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team