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

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:10801173

Identification of target antigen for SLA/LP autoantibodies in autoimmune hepatitis.

Identified SEPSECS (SLA/LP) as the sole target antigen of SLA/LP autoantibodies in autoimmune hepatitis and as the UGA-suppressor tRNA-associated protein component of the tRNP(Ser)Sec ribonucleoprotein.

PMID:17142313

RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea.

SEPSECS (Sep-tRNA:Sec-tRNA synthase) is the terminal enzyme of the eukaryal/archaeal Sec pathway; purified recombinant SepSecS converts Sep-tRNA(Sec) to Sec-tRNA(Sec) in vitro and complements an E. coli SelA deletion in vivo.

PMID:19608919

The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation.

Crystal structure of human SepSecS with tRNA(Sec), phosphoserine and thiophosphate defines a PLP-dependent mechanism; SepSecS is a homotetramer (catalytic + non-catalytic dimer) binding two tRNA(Sec) via their acceptor-TPsiC-variable arms, with PLP covalently linked to Lys284.

PMID:22190034

Global landscape of HIV-human protein complexes.

Large-scale HIV-host affinity-capture/MS screen; source of the IPI "protein binding" annotation reporting an interaction of SEPSECS with the HIV-1 Gag polyprotein (a xeno interaction).

PMID:28414460

Analysis of Novel Interactions between Components of the Selenocysteine Biosynthesis Pathway, SEPHS1, SEPHS2, SEPSECS, and SECp43.

SEPSECS, SECp43 (TRNAU1AP) and selenophosphate synthetases SEPHS1/SEPHS2 form oligomers in eukaryotic cells; SEPHS2 interacts with SEPSECS. Basis for the experimentally determined cytoplasmic localization.

PMID:36929010

Structural basis for the tRNA-dependent activation of the terminal complex of selenocysteine synthesis in humans.

High-resolution structures show tRNA(Sec) binding drives conformational changes that organize the catalytic protomer's active site, supporting a tRNA-dependent activation model. Reference for ComplexPortal cytosol and transferase-complex annotations.

Reactome:R-HSA-2408555

Sep-tRNA(Sec) is converted to Sec-tRNA(Sec) by PXLP-K284-SEPSECS tetramer

Reactome reaction: the SEPSECS tetramer converts Sep-tRNA(Sec) to Sec-tRNA(Sec) using selenophosphate as selenium donor, in the cytosol.

PMID:20920667

Mutations disrupting selenocysteine formation cause progressive cerebello-cerebral atrophy.

Biallelic SEPSECS founder mutations cause autosomal-recessive progressive cerebellocerebral atrophy by disrupting the sole route to Sec biosynthesis and selenoprotein generation.

"In the final step of selenocysteine formation, the essential enzyme SepSecS catalyzes the conversion of Sep-tRNA to Sec-tRNA."