Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells.
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PAPSS1 accumulates in the nucleus of mammalian cells; nuclear targeting is mediated by the APS kinase domain and a catalytically dispensable N-terminal 21-amino-acid sequence, indicating a nuclear sulfate-activation pathway.
"Nuclear targeting of the enzyme is mediated by its APS kinase domain and requires a catalytically dispensable 21 amino acid sequence at the amino terminus."
Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1.
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Purified full-length human PAPSS1 is a homodimer and is catalytically active, forming 25 nmol PAPS per minute per milligram, confirming both catalytic steps of PAPS synthesis.
"The pure protein migrates as a dimer in gel-filtration chromatography. It is moderately active, forming 25 nmol PAPS per minute per milligram."
Elucidation of the active conformation of the APS-kinase domain of human PAPS synthetase 1.
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Crystal structure of the PAPSS1 APS-kinase domain in the Michaelis complex with ADP-Mg and PAPS defines the active conformation and catalytic residues of the second (APS kinase) step.
"The former reaction is catalyzed by the ATP-sulfurylase domain and the latter by the APS-kinase domain."
Structural mechanism for substrate inhibition of the adenosine 5'-phosphosulfate kinase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 and its ramifications for enzyme regulation.
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The APS kinase domain catalyzes the second step of PAPS synthesis and is uncompetitively inhibited by its substrate APS; the ATP sulfurylase domain influences this regulation, suggesting interdomain communication.
"The APS kinase domain of PAPS synthetase catalyzes the second step in which APS, the product of the ATP-sulfurylase domain, is phosphorylated on its 3'-hydroxyl group to yield PAPS."
Human PAPS synthase isoforms are dynamically regulated enzymes with access to nucleus and cytoplasm.
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Human PAPS synthases (including PAPSS1) are dynamically regulated enzymes with access to both the nucleus and the cytoplasm.
"Human PAPS synthase isoforms are dynamically regulated enzymes with access to nucleus and cytoplasm"
Ethanol sulfation by the human cytosolic sulfotransferases: a systematic analysis.
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Systematic analysis of ethanol sulfation by human cytosolic sulfotransferases (SULTs), using [35S]sulfate metabolic labeling; characterizes SULT enzymes rather than directly assaying PAPSS1 enzymology.
"A systematic analysis revealed four ethanol-sulfating SULTs, SULT1A1, SULT1A2, SULT1A3, and SULT1C4, among the eleven human SULT enzymes previously prepared and purified."
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
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Proteome-scale AP-MS interactome (BioPlex 3.0) reporting a PAPSS1 interaction (with/from PAPSS2); source of a bare "protein binding" annotation.
"Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks."
Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase.
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Cloned human PAPS synthetase is a multifunctional enzyme with both ATP sulfurylase and APS kinase domains; functional expression produces PAPS, required for sulfation of many molecules.
"a multifunctional enzyme containing domains for both ATP sulfurylase and adenosine-5'-phosphosulfate kinase"
cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme.
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The human bifunctional enzyme carries an N-terminal APS kinase domain and a C-terminal ATP sulfurylase domain; recombinant full-length and each isolated domain show their respective enzymatic activities.
"Recombinant full-length enzyme and its constituent APS kinase and ATP sulfurylase domains were individually expressed, purified, and shown to have their respective enzymatic activities."
Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains.
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The 1-268 fragment expresses APS kinase activity and the 220-623 fragment ATP sulfurylase activity; the C-terminal domain exerts a regulatory role over the N-terminal APS kinase.
"A 1-268-amino acid fragment expressed APS kinase activity, whereas a 220-623 fragment evinced ATP sulfurylase activity."
Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse.
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Identifies ATPSK2/Atpsk2 (PAPSS2 orthologs) as the genes mutated in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse; the cartilage/skeletal phenotype reflects PAPSS2, not PAPSS1.
"We identified two orthologous genes, ATPSK2 and Atpsk2, encoding novel ATP sulfurylase/APS kinase orthologues in the respective regions of the human and mouse genomes."
PAPSS1,2 transfer PO4(2-) group from ATP to APS to form PAPS
PAPSS1,2 transfer SO4(2-) group to ATP to form APS
BRAF and RAF fusion mutant dimers are phosphorylated
Dissociation of BRAF/RAF fusion complex
p-BRAF and RAF fusion dimers phosphorylate MAP2Ks
p-BRAF and RAF fusion dimers bind MAP2Ks and MAPKs
MAPKs are phosphorylated downstream of BRAF and RAF fusion dimers