SECISBP2
From Wikipedia, the free encyclopedia
SECIS binding protein 2
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Identifiers | ||||||||||||||
Symbol(s) | SECISBP2; DKFZp686C09169; SBP2 | |||||||||||||
External IDs | OMIM: 607693 MGI: 1922670 HomoloGene: 11415 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 79048 | 75420 | ||||||||||||
Ensembl | ENSG00000187742 | ENSMUSG00000035139 | ||||||||||||
Uniprot | Q96T21 | n/a | ||||||||||||
Refseq | NM_024077 (mRNA) NP_076982 (protein) |
XM_127336 (mRNA) XP_127336 (protein) |
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Location | Chr 9: 91.12 - 91.16 Mb | Chr 13: 51.66 - 51.7 Mb | ||||||||||||
Pubmed search | [1] | [2] |
SECIS binding protein 2, also known as SECISBP2, is a human gene.[1]
The incorporation of selenocysteine into a protein requires the concerted action of an mRNA element called a sec insertion sequence (SECIS), a selenocysteine-specific translation elongation factor and a SECIS binding protein. With these elements in place, a UGA codon can be decoded as selenocysteine. The gene described in this record encodes a nuclear protein that functions as a SECIS binding protein. Mutations in this gene have been associated with a reduction in activity of a specific thyroxine deiodinase, a selenocysteine-containing enzyme, and abnormal thyroid hormone metabolism.[1]
[edit] See also
[edit] References
[edit] Further reading
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791-806. PMID 8889548.
- Copeland PR, Fletcher JE, Carlson BA, et al. (2000). "A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs.". EMBO J. 19 (2): 306-14. doi: . PMID 10637234.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788-95. PMID 11076863.
- Low SC, Grundner-Culemann E, Harney JW, Berry MJ (2001). "SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy.". EMBO J. 19 (24): 6882-90. doi: . PMID 11118223.
- Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422-35. doi: . PMID 11230166.
- Lescure A, Allmang C, Yamada K, et al. (2002). "cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2.". Gene 291 (1-2): 279-85. PMID 12095701.
- Allmang C, Carbon P, Krol A (2002). "The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding.". RNA 8 (10): 1308-18. PMID 12403468.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi: . PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi: . PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi: . PMID 15489334.
- Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136-44. doi: . PMID 15489336.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi: . PMID 16189514.
- Dumitrescu AM, Liao XH, Abdullah MS, et al. (2006). "Mutations in SECISBP2 result in abnormal thyroid hormone metabolism.". Nat. Genet. 37 (11): 1247-52. doi: . PMID 16228000.
- Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415-8. doi: . PMID 16381901.
- Papp LV, Lu J, Striebel F, et al. (2006). "The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function.". Mol. Cell. Biol. 26 (13): 4895-910. doi: . PMID 16782878.