SEPX1
Methionine sulfoxide reductase B1 | |||||||||||||
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Identifiers | |||||||||||||
Symbols | MSRB1 ; SELR; SELX; SEPX1; SepR | ||||||||||||
External IDs | OMIM: 606216 MGI: 1351642 HomoloGene: 8455 GeneCards: MSRB1 Gene | ||||||||||||
EC number | 1.8.4.- | ||||||||||||
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Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 51734 | 27361 | |||||||||||
Ensembl | ENSG00000198736 | ENSMUSG00000075705 | |||||||||||
UniProt | Q9NZV6 | Q9JLC3 | |||||||||||
RefSeq (mRNA) | NM_016332 | NM_013759 | |||||||||||
RefSeq (protein) | NP_057416 | NP_038787 | |||||||||||
Location (UCSC) | Chr 16: 1.99 – 1.99 Mb | Chr 17: 24.74 – 24.74 Mb | |||||||||||
PubMed search | |||||||||||||
Methionine-R-sulfoxide reductase B1 is an enzyme that in humans is encoded by the SEPX1 gene.[1][2]
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
References
- ↑ Lescure A, Gautheret D, Carbon P, Krol A (Feb 2000). "Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif". J Biol Chem 274 (53): 38147–54. doi:10.1074/jbc.274.53.38147. PMID 10608886.
- ↑ 2.0 2.1 "Entrez Gene: SEPX1 selenoprotein X, 1".
Further reading
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Kryukov GV, Kryukov VM, Gladyshev VN (1999). "New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements.". J. Biol. Chem. 274 (48): 33888–97. doi:10.1074/jbc.274.48.33888. PMID 10567350.
- Zhang QH, Ye M, Wu XY et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
- Daniels RJ, Peden JF, Lloyd C et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.". Hum. Mol. Genet. 10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID 11157797.
- Moskovitz J, Singh VK, Requena J et al. (2002). "Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity.". Biochem. Biophys. Res. Commun. 290 (1): 62–5. doi:10.1006/bbrc.2001.6171. PMID 11779133.
- 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:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Kim HY, Gladyshev VN (2004). "Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases.". Mol. Biol. Cell 15 (3): 1055–64. doi:10.1091/mbc.E03-08-0629. PMC 363075. PMID 14699060.
- 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:10.1101/gr.2596504. PMC 528928. PMID 15489334.