SRXN1

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Sulfiredoxin 1 homolog (S. cerevisiae)
PDB rendering based on 1xw3.
Available structures: 1xw3, 1xw4, 1yzs, 2b6f
Identifiers
Symbol(s) SRXN1; C20orf139; Npn3; SRX1; YKL086W; dJ850E9.2
External IDs MGI: 104971 HomoloGene: 32722
Orthologs
Human Mouse
Entrez 140809 76650
Ensembl n/a ENSMUSG00000032802
Uniprot n/a Q9D975
Refseq NM_080725 (mRNA)
NP_542763 (protein)		 NM_029688 (mRNA)
NP_083964 (protein)
Location n/a Chr 2: 151.8 - 151.8 Mb
Pubmed search [1] [2]

Sulfiredoxin 1 homolog (S. cerevisiae), also known as SRXN1, is a human gene.[1]


[edit] References

  1. ^ Entrez Gene: SRXN1 sulfiredoxin 1 homolog (S. cerevisiae).

[edit] Further reading

  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788-95. PMID 11076863. 
  • Venter JC, Adams MD, Myers EW, et al. (2001). "The sequence of the human genome.". Science 291 (5507): 1304-51. doi:10.1126/science.1058040. PMID 11181995. 
  • 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:10.1101/gr.154701. PMID 11230166. 
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865-71. doi:10.1038/414865a. PMID 11780052. 
  • 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. PMID 12477932. 
  • Chang TS, Jeong W, Woo HA, et al. (2005). "Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine.". J. Biol. Chem. 279 (49): 50994-1001. doi:10.1074/jbc.M409482200. PMID 15448164. 
  • 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. 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:10.1101/gr.2576704. PMID 15489336. 
  • Woo HA, Jeong W, Chang TS, et al. (2005). "Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.". J. Biol. Chem. 280 (5): 3125-8. doi:10.1074/jbc.C400496200. PMID 15590625. 
  • Jönsson TJ, Murray MS, Johnson LC, et al. (2005). "Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin.". Biochemistry 44 (24): 8634-42. doi:10.1021/bi050131i. PMID 15952770. 
  • Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415-8. doi:10.1093/nar/gkj139. PMID 16381901. 
  • Jeong W, Park SJ, Chang TS, et al. (2006). "Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin.". J. Biol. Chem. 281 (20): 14400-7. doi:10.1074/jbc.M511082200. PMID 16565085. 
  • Findlay VJ, Townsend DM, Morris TE, et al. (2006). "A novel role for human sulfiredoxin in the reversal of glutathionylation.". Cancer Res. 66 (13): 6800-6. doi:10.1158/0008-5472.CAN-06-0484. PMID 16818657. 
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