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SEPW1 encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. Additionally we are shipping Selenoprotein W, 1 Antibodies (28) and many more products for this protein.
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Selenoprotein W is conserved in human, rhesus monkey, sheep, rat, and mouse.
SelW may have a regulatory function in redox cell signaling by interacting with 14-3-3 protein (show YWHAE Proteins).
Suppression of EGFR (show EGFR Proteins) ubiquitination by SEPW1 may be related to the putative increase in cancer risk associated with high selenium intakes.
In response to selenium compounds, SepW1 synthesis increased at the protein and the mRNA levels.
SEPW1 silencing increases MKK4 (show MAP2K4 Proteins), which activates p38gamma (show MAPK12 Proteins), p38delta, and JNK2 (show MAPK9 Proteins) to phosphorylate p53 (show TP53 Proteins) on Ser (show SIGLEC1 Proteins)-33 and cause a transient G(1) arrest.
p53 (show TP53 Proteins) was increased in SEPW1 silenced cells and was inversely correlated with SEPW1 mRNA in cell lines with altered SEPW1 expression.
The present work shows that SEPW1 facilitates the G1 to S-phase transition by down-regulating expression of the cyclin-dependent kinase (show CDK1 Proteins) inhibitor p21 (show CDKN1A Proteins)
The gene lacks canonical TATA and CAAT boxes, but has numerous Sp1 (show PSG1 Proteins) consensus binding sites upstream of multiple transcription start sites. SEPW1 is expressed in all of the 22 tissues assayed, and shows highest expression in skeletal muscle and heart.
SelW expression in the colon is highly sensitive to Se-depletion
SeW is the novel molecular target of MeHg in human neuronal cells and down-regulation of this selenoenzyme by MeHg is dependent not on generation of ROS (show ROS1 Proteins) but on depletion of GSH.
SEPW1 mRNA levels were maximal during G1-phase, dropped after the G1/S transition and increased again after G2/M-phase.
SelW enhances myoblast differentiation by inhibiting TAZ (show TAZ Proteins) binding to 14-3-3 (show YWHAQ Proteins).
SelW gene was activated by the binding of MyoD (show MYOD1 Proteins) to a specific E-box during early skeletal muscle differentiation.
The main function of SelW in muscle cells is not in the antioxidative system.
Data show that the loss of SelT (show SELT Proteins) elevates expression of another selenoprotein, selenoprotein W, suggesting that SepW1 may functionally compensate for SelT (show SELT Proteins).
Selenoprotein W is involved in muscle growth and differentiation by protecting the developing myoblasts from oxidative stress
increased in mouse brains of postnatal day 8 and 20 relative to embryonic day 15; siRNA-transfected neurons are more sensitive to the oxidative stress-induced (show SQSTM1 Proteins) apoptosis
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This protein shows highest expression in skeletal muscle and heart, and may be involved in oxidation-reduction reactions. A retroprocessed pseudogene, SEPW1P, has been identified and mapped to chromosome 1p35-34.
, selenoprotein W, 1
, selenoprotein W, muscle 1