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Here, we report that SECIS elements in the coding regions of selenoprotein mRNAs support Sec insertion in higher eukaryotes. Paper-12448141.
Thus, SELB could be an amino acid-specific elongation factor, replacing EF-Tu in a special translational step. Paper-6449682.
However, a resolving Cys was required for the thioredoxin (Trx)-dependent recycling process of the Sec-containing form. Paper-12951212.
Previous studies have shown that SBP2 is required for the Sec-incorporation mechanism; however, additional roles of SBP2 in the cell have remained undefined. Paper-14094401.
We report that co-expression of SBP2 overcomes the limitation produced by selenoprotein mRNA overexpression, whereas selenocysteyl-tRNA and the selenocysteine-specific elongation factor do not. Paper-8515508.
The incorporation of selenocysteine ( Sec) into proteins in mammalian cells requires the Sec insertion sequence (SECIS) binding protein 2 ( SBP2). Paper-13947561.
Thirty-six patients carried known MLL fusions (34 with der(11) and 2 with reciprocal alleles), whereas 3 patients were found to carry novel MLL fusions to ACACA, SELB, and SMAP1, respectively. Paper-10778648.
This process requires multiple features, such as the Sec-insertion sequence (SECIS) element and protein factors, including a specific elongation factor EFSec and the SECIS-binding protein 2, SBP2. Paper-14184877.
Mammalian thioredoxin reductase ( TR) contains a rare selenocysteine ( Sec) residue in a conserved redox-active tetrapeptide of sequence Gly-Cys(1)-Sec(2)-Gly. Paper-13862721.
Selenoproteins are poorly characterized enzymes and reports on the functional exchangeability of Sec with Cys are limited and controversial. Paper-13931492.
In bacteria, this structure is located in the coding region immediately downstream of the Sec-encoding UGA codon, whereas in eukaryotes a completely different SECIS element has evolved in the 3'-untranslated region. Paper-12448141.
The Sec-containing Clostridium MsrB form exhibited 100-fold higher activity than its Cys-containing form, revealing that Sec provided the catalytic advantage of higher activity. Paper-12951212.
Since SPS1 evolved from a protein that utilizes selenium for Sec biosynthesis, an attractive possibility is that SPS1 may define a new pathway of selenium utilization in animals. Paper-12669691.
Systematic linkage analysis of genes involved in DIO2 synthesis and degradation led to the identification of an inherited Sec incorporation defect, caused by a homozygous missense mutation in SECISBP2 (also called SBP2). Paper-11471752.
We verified and generalized the catalytic features that selenocysteine ( Sec) and cysteine ( Cys) contribute to the reduction of methionine-R-sulfoxide using an anaerobic bacterial MsrB from Clostridium sp. OhILA as a model protein. Paper-12951212.
These insects also lost the Sec biosynthesis and insertion machinery, but selenophosphate synthetase 1 ( SPS1), an enzyme previously implicated in Sec biosynthesis, is present in all insects, including T. castaneum and B. mori. Paper-12669691.
These data agreed well with our previous data on mammalian MsrBs, and therefore suggested that the catalytic mechanisms, as well as the catalytic advantages and disadvantages provided by the Sec and Cys residues, are most likely conserved from anaerobic bacteria to mammals. Paper-12951212.
Sec is a rare amino acid in extant proteins, chemically similar to cysteine ( Cys), found in homologous position to Cys of nonselenoprotein families. Paper-13931492.
Sec could be synthesized on tRNA [Ser]Sec from selenide, adenosine triphosphate ( ATP), and serine using tRNA[Ser]Sec, seryl-tRNA synthetase, PSTK, selenophosphate synthetase, and SecS. Paper-12567521.
The selenocysteine ( Sec) and cysteine ( Cys) residues (Cys-496/Sec-497) in the active site of TrxR and a pair of Cys residues (Cys-32/Cys-35) in Trx are sensitive to various alkylating reagents. Paper-11393835.
Our results indicate concerted purifying selection across Sec and Cys sites in all selenoproteomes, consistent with a unique role of Sec in protein function, low exchangeability, and an unknown degree of functional divergence with Cys homologs. Paper-13931492.
These synonyms are used for gene EEFSEC (eukaryotic elongation factor, selenocysteine-tRNA-specific): Selenocysteine-specific elongation factor, SELB, Eukaryotic elongation factor, selenocysteine-tRNA-specific, Elongation factor sec, EFSEC.
These accession numbers are used for gene EEFSEC: Q96HZ6 (UNIPROT__AC), DQ896587 (NCBI_GENBANK__AC), C9J8T0 (UNIPROT__AC), AAG13375 (NCBI_GENBANK__AC).
EEFSEC is a homologue of selb-1 (SELB (SelB homolog) translation factor for selenocysteine incorporation) from Caenorhabditis elegans.
EEFSEC is a homologue of EfSec (CG9841 gene product from transcript CG9841-RA) from Drosophila melanogaster.
EEFSEC is a homologue of EEFSEC (eukaryotic elongation factor, selenocysteine-tRNA-specific) from Bos taurus.
EEFSEC is a homologue of EEFSEC (eukaryotic elongation factor, selenocysteine-tRNA-specific) from Canis lupus familiaris.
EEFSEC is a homologue of Eefsec (eukaryotic elongation factor, selenocysteine-tRNA-specific) from Mus musculus.
EEFSEC is a homologue of Eefsec (eukaryotic elongation factor, selenocysteine-tRNA-specific) from Rattus norvegicus.
EEFSEC is a homologue of eefsec (eukaryotic elongation factor, selenocysteine-tRNA-specific) from Danio rerio.
EEFSEC is a homologue of AgaP_AGAP006250 (AGAP006250-PA) from Anopheles gambiae str. PEST.
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Concept & Implementation by Robert Hoffmann.