SRXN1

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Sulfiredoxin 1 homolog (S. cerevisiae)
File:PBB Protein SRXN1 image.jpg
PDB rendering based on 1xw3.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SRXN1 ; C20orf139; Npn3; SRX1; YKL086W; dJ850E9.2
External IDs Template:MGI HomoloGene32722
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

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


References

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

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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