| 释义 |
- See also
- References
- Further reading
{{Infobox_gene}}Methionine-R-sulfoxide reductase B1 is an enzyme that in humans is encoded by the SEPX1 gene.[1][2]{{PBB_Summary
| section_title =
| summary_text = 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 belongs to the methionine sulfoxide reductase B (MsrB) family, and it is expressed in a variety of adult and fetal tissues.[2]
}}See also- MSRA (gene)
- MSRB2
- Methionine oxidation
References1. ^{{cite journal | vauthors = Lescure A, Gautheret D, Carbon P, Krol A | title = Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif | journal = J Biol Chem | volume = 274 | issue = 53 | pages = 38147–54 |date=Feb 2000 | pmid = 10608886 | pmc = | doi =10.1074/jbc.274.53.38147 }}
2. ^1 {{cite web | title = Entrez Gene: SEPX1 selenoprotein X, 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51734| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
- {{cite journal | vauthors=Kryukov GV, Kryukov VM, Gladyshev VN |title=New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 33888–97 |year= 1999 |pmid= 10567350 |doi=10.1074/jbc.274.48.33888 }}
- {{cite journal |vauthors=Zhang QH, Ye M, Wu XY, etal |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546–60 |year= 2001 |pmid= 11042152 |doi=10.1101/gr.140200 | pmc=310934 }}
- {{cite journal |vauthors=Daniels RJ, Peden JF, Lloyd C, etal |title=Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. |journal=Hum. Mol. Genet. |volume=10 |issue= 4 |pages= 339–52 |year= 2001 |pmid= 11157797 |doi=10.1093/hmg/10.4.339 }}
- {{cite journal |vauthors=Moskovitz J, Singh VK, Requena J, etal |title=Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity. |journal=Biochem. Biophys. Res. Commun. |volume=290 |issue= 1 |pages= 62–5 |year= 2002 |pmid= 11779133 |doi= 10.1006/bbrc.2001.6171 }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
- {{cite journal | vauthors=Kim HY, Gladyshev VN |title=Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. |journal=Mol. Biol. Cell |volume=15 |issue= 3 |pages= 1055–64 |year= 2004 |pmid= 14699060 |doi= 10.1091/mbc.E03-08-0629 | pmc=363075 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
{{refend}}{{protein-stub}} 1 : Selenoproteins |