Search results for ASNS

Showing 16 results out of 32

×

Species

Types

Compartments

Reaction types

Search properties

Species

Types

Compartments

Reaction types

Search properties

Protein (1 results from a total of 1)

Identifier: R-HSA-70597
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: ASNS: P08243

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-5642307
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000070669

Complex (3 results from a total of 7)

Identifier: R-HSA-507865
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-532669
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Identifier: R-HSA-901051
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen

Reaction (3 results from a total of 6)

Identifier: R-HSA-1791118
Species: Homo sapiens
Compartment: nucleoplasm, cytosol
The Asparagine Synthetase (ASNS) gene is transcribed to yield mRNA and the mRNA is translated to yield protein (Chen et al. 2004, Lee et al. 2008, Gjymishka et al. 2009, Sikalidis et al. 2011, Balasubramanian et al. 2013, inferred from the mouse homolog). Transcription of ASNS is activated by the unfolded protein response (Gjymishka et al. 2009), amino acid deficiency (Chen et al. 2004, Lee et al. 2008, Sikalidis et al. 2011, Balasubramanian et al. 2013, inferred from the mouse homolog), and heme deficiency (inferred from the mouse homolog).
Identifier: R-HSA-9635915
Species: Homo sapiens
Compartment: nucleoplasm
ATF4 and CEBPB or CEBPG bind a CEBP-ATF regulatory element (CARE) in the promoter of the ASNS gene (Siu et al 2001, Chen et al. 2004, inferred from mouse homologs). ATF4 binds rapidly during the first 2 hours after amino acid deprivation (Chen et al. 2004). ATF3 and CEBPB accumulate on the ASNS promoter more slowly and appear to correlate with decreasing transcription of ASNS (Chen et al. 2004). EIF2AK1 acts via ATF4 to activate transcription of ASNS in response to heme deficiency (inferred from mouse homologs).
Identifier: R-HSA-70599
Species: Homo sapiens
Compartment: cytosol
Cytosolic asparagine synthase (ASNS) catalyzes the reaction of aspartate, glutamine, and ATP to form asparagine, glutamate, AMP, and pyrophosphate. Studies of the recombinant protein expressed in E. coli suggest that the active form of the enzyme is a dimer (Van Heeke and Schuster 1989).

Genes and Transcripts (3 results from a total of 4)

Identifier: R-HSA-379728
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-379718
Species: Homo sapiens
Compartment: mitochondrial matrix
Identifier: R-HSA-379722
Species: Homo sapiens
Compartment: cytosol

Chemical Compound (3 results from a total of 11)

Identifier: R-ALL-351980
Compartment: extracellular region
Primary external reference: ChEBI: L-asparagine zwitterion: 58048
Identifier: R-ALL-29642
Compartment: cytosol
Primary external reference: ChEBI: L-asparagine zwitterion: 58048
Identifier: R-ALL-379703
Compartment: mitochondrial matrix
Primary external reference: ChEBI: L-asparagine zwitterion: 58048

Set (1 results from a total of 1)

Identifier: R-ALL-5687524
Compartment: cytosol

Pathway (1 results from a total of 1)

Identifier: R-HSA-9633012
Species: Homo sapiens
EIF2AK4 (GCN2) senses amino acid deficiency by binding uncharged tRNAs near the ribosome and responds by phosphorylating EIF2S1, the alpha subunit of the translation initiation factor EIF2 (inferred from yeast homologs and mouse homologs, reviewed in Chaveroux et al. 2010, Castilho et al. 2014, Gallinetti et al. 2013, Bröer and Bröer 2017, Wek 2018). Phosphorylated EIF2S1 reduces translation of most mRNAs but increases translation of downstream ORFs in mRNAs such as ATF4 that contain upstream ORFs (inferred from mouse homologs in Vattem and Wek 2004, reviewed in Hinnebusch et al. 2016, Sonenberg and Hinnebusch 2009). ATF4, in turn, activates expression of genes involved in responding to amino acid deficiency such as DDIT3 (CHOP), ASNS (asparagine synthetase), CEBPB, and ATF3 (reviewed in Kilberg et al. 2012, Wortel et al. 2017). In mice, EIF2AK4 in the brain may responsible for avoidance of diets lacking essential amino acids (Hao et al. 2005, Maurin et al. 2005, see also Leib and Knight 2015, Gietzen et al. 2016, reviewed in Dever and Hinnebusch 2005).
EIF2AK4 is bound to both the ribosome and GCN1, which is required for activation of EIF2AK4 and may act by shuttling uncharged tRNAs from the A site of the ribosome to EIF2AK4. Upon binding tRNA, EIF2AK4 trans-autophosphorylates. Phosphorylated EIF2AK4 then phosphorylates EIF2S1 on serine-52, the same serine residue phosphorylated by other kinases of the integrated stress response: EIF2AK1 (HRI, activated by heme deficiency and other stresses), EIF2AK2 (PKR, activated by double-stranded RNA), and EIF2AK3 (PERK, activated by unfolded proteins) (reviewed in Hinnebusch 1994, Wek et al. 2006, Donnelly et al. 2013, Pakos-Zebrucka et al. 2016, Wek 2018),
Cite Us!