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
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
Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation.
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Human Sps2 (SEPHS2) was cloned from lung adenocarcinoma cells and shown to be a selenophosphate synthetase that makes monoselenophosphate from selenide and ATP, functionally complementing an E. coli selD mutant in a selenite assimilation role.
"A labile selenium donor compound monoselenophosphate is synthesized from selenide and ATP by selenophosphate synthetase ... the Sps2 enzyme can function with a selenite assimilation system"
Analysis of Novel Interactions between Components of the Selenocysteine Biosynthesis Pathway, SEPHS1, SEPHS2, SEPSECS, and SECp43.
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SEPHS2 forms oligomers with SEPHS1 and interacts with SEPSECS and SEPHS1 in mammalian cells (BRET, confirmed by co-immunoprecipitation); SEPHS2 localizes to the cytoplasm.
"selenophosphate synthetases SEPHS1 and SEPHS2 form oligomers in eukaryotic cells ... SEPHS2 interacts with SEPSECS and SEPHS1; these interactions were confirmed by co-immunoprecipitation"
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
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High-throughput AP-MS (BioPlex 3.0) reporting a SEPHS2 physical interaction (WITH/FROM SEPHS1, P49903); provides evidence of interaction, not a specific molecular function.
"affinity-purification mass spectrometry ... BioPlex suggests function, localization, and complex membership for thousands of proteins"
Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism?
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Original cloning of human/mouse Sps2 as a selD (selenophosphate synthetase) homolog; selenophosphate synthetase makes monoselenophosphate, the selenium donor for selenocysteine synthesis. SPS2 is itself a selenoenzyme (in-frame TGA read through; 75Se incorporation), suggesting autoregulation of selenocysteine metabolism.
"the selenium donor compound required for synthesis of selenocysteine ... the incorporation of 75Se into SPS2 ... SPS2 is a selenoenzyme"
SEPHS2 phosphorylates H2Se to form SELP