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Gene Ontology Classifications
Symbol
Name
ID
Sod1
superoxide dismutase 1, soluble
MGI:98351

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Sod1. (This text reflects annotations as of Thursday, July 24, 2014.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of October 1, 2013. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.
Summary from NCBI RefSeq


[Summary is not available for the mouse gene. This summary is for the human ortholog.] The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. [provided by RefSeq, Jul 2008]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
References
  1. Busuttil RA et al. (2005) Organ-specific increase in mutation accumulation and apoptosis rate in CuZn-superoxide dismutase-deficient mice. Cancer Res, 65:11271-5. (PubMed:16357131)
  2. Didion SP et al. (2002) Increased superoxide and vascular dysfunction in CuZnSOD-deficient mice. Circ Res, 91:938-44. (PubMed:12433839)
  3. Epstein CJ et al. (1987) Transgenic mice with increased Cu/Zn-superoxide dismutase activity: animal model of dosage effects in Down syndrome. Proc Natl Acad Sci U S A, 84:8044-8. (PubMed:2960971)
  4. Flood DG et al. (1999) Hindlimb motor neurons require Cu/Zn superoxide dismutase for maintenance of neuromuscular junctions. Am J Pathol, 155:663-72. (PubMed:10433959)
  5. Francke U et al. (1979) Assignment of the gene for cytoplasmic superoxide dismutase (Sod-1) to a region of chromosome 16 and of Hprt to a region of the X chromosome in the mouse. Proc Natl Acad Sci U S A, 76:5230-3. (PubMed:291939)
  6. Hadjur S et al. (2001) Defective hematopoiesis and hepatic steatosis in mice with combined deficiencies of the genes encoding Fancc and Cu/Zn superoxide dismutase. Blood, 98:1003-11. (PubMed:11493445)
  7. Harraz MM et al. (2008) SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model. J Clin Invest, 118:659-70. (PubMed:18219391)
  8. Ho YS et al. (1998) Reduced fertility in female mice lacking copper-zinc superoxide dismutase. J Biol Chem, 273:7765-9. (PubMed:9516486)
  9. Ho YS et al. (1998) The nature of antioxidant defense mechanisms: a lesson from transgenic studies. Environ Health Perspect, 106 Suppl 5:1219-28. (PubMed:9788901)
  10. Imamura Y et al. (2006) Drusen, choroidal neovascularization, and retinal pigment epithelium dysfunction in SOD1-deficient mice: a model of age-related macular degeneration. Proc Natl Acad Sci U S A, 103:11282-7. (PubMed:16844785)
  11. Ishii T et al. (2005) Accelerated impairment of spermatogenic cells in SOD1-knockout mice under heat stress. Free Radic Res, 39:697-705. (PubMed:16036348)
  12. Iuchi Y et al. (2007) Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production. Biochem J, 402:219-27. (PubMed:17059387)
  13. Kawase M et al. (1999) Exacerbation of delayed cell injury after transient global ischemia in mutant mice with CuZn superoxide dismutase deficiency. Stroke, 30:1962-8. (PubMed:10471451)
  14. Keithley EM et al. (2005) Cu/Zn superoxide dismutase and age-related hearing loss. Hear Res, 209:76-85. (PubMed:16055286)
  15. Kessova IG et al. (2007) Mitochondrial alterations in livers of Sod1-/- mice fed alcohol. Free Radic Biol Med, 42:1470-80. (PubMed:17448893)
  16. Khan JY et al. (2003) Developmental changes in murine brain antioxidant enzymes. Pediatr Res, 54:77-82. (PubMed:12646716)
  17. Lei XG et al. (2006) Mice deficient in Cu,Zn-superoxide dismutase are resistant to acetaminophen toxicity. Biochem J, 399:455-61. (PubMed:16831125)
  18. Levy MA et al. (2001) Cellular response of antioxidant metalloproteins in Cu/Zn SOD transgenic mice exposed to hyperoxia. Am J Physiol Lung Cell Mol Physiol, 281:L172-82. (PubMed:11404260)
  19. Matzuk MM et al. (1998) Ovarian function in superoxide dismutase 1 and 2 knockout mice. Endocrinology, 139:4008-11. (PubMed:9724058)
  20. McFadden SL et al. (1999) Cu/Zn SOD deficiency potentiates hearing loss and cochlear pathology in aged 129,CD-1 mice. J Comp Neurol, 413:101-12. (PubMed:10464373)
  21. McFadden SL et al. (1999) Age-related cochlear hair cell loss is enhanced in mice lacking copper/zinc superoxide dismutase. Neurobiol Aging, 20:1-8. (PubMed:10466888)
  22. Mootha VK et al. (2003) Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell, 115:629-40. (PubMed:14651853)
  23. Morikawa K et al. (2003) Pivotal role of Cu,Zn-superoxide dismutase in endothelium-dependent hyperpolarization. J Clin Invest, 112:1871-9. (PubMed:14679182)
  24. Muller FL et al. (2004) Complex III releases superoxide to both sides of the inner mitochondrial membrane. J Biol Chem, 279:49064-73. (PubMed:15317809)
  25. Muller FL et al. (2006) Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy. Free Radic Biol Med, 40:1993-2004. (PubMed:16716900)
  26. Nguyen MD et al. (2001) Deregulation of Cdk5 in a mouse model of ALS: toxicity alleviated by perikaryal neurofilament inclusions. Neuron, 30:135-47. (PubMed:11343650)
  27. Noshita N et al. (2002) Copper/zinc superoxide dismutase attenuates neuronal cell death by preventing extracellular signal-regulated kinase activation after transient focal cerebral ischemia in mice. J Neurosci, 22:7923-30. (PubMed:12223545)
  28. Ohlemiller KK et al. (1999) Targeted deletion of the cytosolic Cu/Zn-superoxide dismutase gene (Sod1) increases susceptibility to noise-induced hearing loss. Audiol Neurootol, 4:237-46. (PubMed:10436316)
  29. Pagliarini DJ et al. (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell, 134:112-23. (PubMed:18614015)
  30. Prohaska JR et al. (2003) Copper, zinc-superoxide dismutase protein but not mRNA is lower in copper-deficient mice and mice lacking the copper chaperone for superoxide dismutase. Exp Biol Med (Maywood), 228:959-66. (PubMed:12968068)
  31. Reaume AG et al. (1996) Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat Genet, 13:43-7. (PubMed:8673102)
  32. Reddy VN et al. (2004) Effects of variation in superoxide dismutases (SOD) on oxidative stress and apoptosis in lens epithelium. Exp Eye Res, 79:859-68. (PubMed:15642323)
  33. Schafer R et al. (1980) Assignment of the gene for cytoplasmic glutamate-oxaloacetate transaminase to mouse chromosome 19 using chinese hamster x mouse somatic cell hybrids. Somatic Cell Genet, 6:709-17. (PubMed:7444718)
  34. Schmidt-Ott KM et al. (2006) c-kit delineates a distinct domain of progenitors in the developing kidney. Dev Biol, 299:238-49. (PubMed:16942767)
  35. Sentman ML et al. (2006) Phenotypes of mice lacking extracellular superoxide dismutase and copper- and zinc-containing superoxide dismutase. J Biol Chem, 281:6904-9. (PubMed:16377630)
  36. Shi P et al. (2010) Effects of ALS-related SOD1 mutants on dynein- and KIF5-mediated retrograde and anterograde axonal transport. Biochim Biophys Acta, 1802:707-16. (PubMed:20510358)
  37. Turner BJ et al. (2005) Impaired extracellular secretion of mutant superoxide dismutase 1 associates with neurotoxicity in familial amyotrophic lateral sclerosis. J Neurosci, 25:108-17. (PubMed:15634772)
  38. Yoshida T et al. (2000) Targeted disruption of the mouse Sod I gene makes the hearts vulnerable to ischemic reperfusion injury. Circ Res, 86:264-9. (PubMed:10679476)



Go Annotations in Tabular Form (Text View) (GO Graph)

 
 


Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IMP Inferred from mutant phenotype
  IPI Inferred from physical interaction
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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last database update
09/09/2014
MGI 5.19
The Jackson Laboratory