SEPX1

SEPX1

Selenoprotein X, 1, also known as SEPX1, is a human gene.cite web | title = Entrez Gene: SEPX1 selenoprotein X, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51734| accessdate = ]

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.cite web | title = Entrez Gene: SEPX1 selenoprotein X, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51734| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=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=
*cite journal | author=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=
*cite journal | author=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 |year= 2000 |pmid= 10608886 |doi=
*cite journal | author=Zhang QH, Ye M, Wu XY, "et al." |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=
*cite journal | author=Daniels RJ, Peden JF, Lloyd C, "et al." |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=
*cite journal | author=Moskovitz J, Singh VK, Requena J, "et al." |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 | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |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
*cite journal | author=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
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |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

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