Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Analysis of sulfur and selenium assimilation in Astragalus plants with varying capacities to accumulate selenium.
The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts.
Proteome changes in Arabidopsis thaliana roots upon exposure to Cd2+.
Sorting signals, N-terminal modifications and abundance of the chloroplast proteome.
Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis.
AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins.
Analysis of the Arabidopsis cytosolic proteome highlights subcellular partitioning of central plant metabolism.
Adenosine-5'-triphosphate-sulfurylase from Arabidopsis thaliana and Escherichia coli are functionally equivalent but structurally and kinetically divergent: nucleotide sequence of two adenosine-5'-triphosphate-sulfurylase cDNAs from Arabidopsis thaliana and analysis of a recombinant enzyme.
Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae.
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Activates sulfate to APS in chloroplast stroma, supplying the direct APS-reduction branch and other activated-sulfate metabolism.
"Expression of APS1 correlated with the presence of ATP sulfurylase
enzyme activity in cell extracts."
Natural variation in the ATPS1 isoform of ATP sulfurylase contributes to the control of sulfate levels in Arabidopsis.
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Activates sulfate to APS in chloroplast stroma, supplying the direct APS-reduction branch and other activated-sulfate metabolism.
"Disruption of the ATPS1 gene in Col-0 resulted in the reduction of ATPS enzyme activity by approximately 50%"
Alternative translational initiation of ATP sulfurylase underlying dual localization of sulfate assimilation pathways in plastids and cytosol in Arabidopsis thaliana.
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ATPS1 (APS1, At3g22890) GFP fusions are exclusively plastidic in protoplasts and in stable transgenic leaves and roots; the cytosolic ATP sulfurylase isoform is ATPS2.
"while they were present only in plastids in ATPS1-GFP lines (Figure 4D)."
Overexpression of ATP sulfurylase in indian mustard leads to increased selenate uptake, reduction, and tolerance.
file:ARATH/APS1/APS1-uniprot.txt