Recombinant Human Selenocysteine insertion sequence-binding protein 2 (SECISBP2), partial

1. functions as a vital factor in selenoprotein translation and regulates the pro-oxidant/antioxidant balance in trophoblasts PMID: 28623977
2. SBP2 interacts directly with four proteins of the SMN complex and the methylosome core proteins. PMID: 28115638
3. SBP2 makes direct contacts with a discrete region of the human 28S rRNA. PMID: 24850884
4. The patient showed typical symptoms of SBP2 deficiency, and novel compound heterozygous mutations were identified in SBP2 (p.M515fsX563/p.Q79X). PMID: 22247018
5. Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes. PMID: 22308032
6. Describe subjects with compound heterozygous defects in the SECISBP2 gene. These individuals have reduced synthesis of most of the 25 known human selenoproteins, resulting in a complex phenotype. PMID: 21084748
7. Results demonstrate that SECIS-binding protein 2 is required for protection against reactive oxygen species-induced cellular damage and cell survival. PMID: 19803747
8. In addition to identifying key amino acids for SECIS recognition by SBP2, our findings led to the proposal that some of the recognition principles governing the 15.5 kD-U4 snRNA interaction must be similar in the SBP2-SECIS RNA complex PMID: 12403468
9. Oxidative stress induces nuclear accumulation of SBP2 via oxidation of cysteine residues within a redox-sensitive cysteine-rich domain. PMID: 16782878
10. Data suggest that SBP2 is a major determinant in dictating the hierarchy of selenoprotein synthesis via differential selenoprotein mRNA translation and sensitivity to nonsense-mediated decay. PMID: 17846120
11. A report of a complex splicing pattern in the 5'-region of human SECISBP2, wherein at least eight splice variants encode five isoforms with varying N-terminal sequence. PMID: 19004874
12. CUG-BP1 and HuR act as factors that bind to the SBP2 3' UTR, which suggests that TTR-RBPs play a role in the regulation of SBP2 PMID: 19106619
13. Seleniuim is obviously not a limiting factor in the SBP2 deficient individuals when regular daily selenium intake is provided PMID: 19265499
14. ca. 70% of the SBP2 sequence is disordered, whereas the RNA binding domain appears to be folded and functional. PMID: 19467292
15. SBP2 gene mutation producing early arrest in synthesis of full-length molecule. Demonstration that SBP2 isoforms containing all functional domains could be synthesized from three downstream ATGs explains the relatively mild phenotype caused by this defect PMID: 19602558

Show More

Hide All

HGNC: 30972

OMIM: 607693

KEGG: hsa:79048

STRING: 9606.ENSP00000364965

UniGene: Hs.59804