Superoxide dismutase [Mn], mitochondrial

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• 2 H⁺

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  + 2 superoxide

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  = H₂O₂

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  + O₂

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  EC:1.15.1.1
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  Source: Rhea

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  2

  H⁺

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  +

  2

  superoxide

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  zoom

  =

  H₂O₂

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  +

  O₂

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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• DNA binding Source: MGI
• enzyme binding Source: MGI
• identical protein binding Source: MGI
• manganese ion binding Source: UniProtKB
• metal ion binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• oxidoreductase activity Source: CACAO <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness."
    Friedman J.S., Lopez M.F., Fleming M.D., Rivera A., Martin F.M., Welsh M.L., Boyd A., Doctrow S.R., Burakoff S.J.
    Blood 104:2565-2573(2004) [PubMed] [Europe PMC] [Abstract]
• oxygen binding Source: MGI
• superoxide dismutase activity Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Developmental changes in murine brain antioxidant enzymes."
    Khan J.Y., Black S.M.
    Pediatr. Res. 54:77-82(2003) [PubMed] [Europe PMC] [Abstract]
  • "An unexpected functional link between lysosomal thiol reductase and mitochondrial manganese superoxide dismutase."
    Bogunovic B., Stojakovic M., Chen L., Maric M.
    J. Biol. Chem. 283:8855-8862(2008) [PubMed] [Europe PMC] [Abstract]
  • "Mouse mitochondrial superoxide dismutase locus is on chromosome 17."
    Szymura J.M., Wabl M.R., Klein J.
    Immunogenetics 14:231-240(1981) [PubMed] [Europe PMC] [Abstract]
  • "Susceptibility of heterozygous MnSOD gene-knockout mice to oxygen toxicity."
    Tsan M.F., White J.E., Caska B., Epstein C.J., Lee C.Y.
    Am. J. Respir. Cell Mol. Biol. 19:114-120(1998) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure Source: MGIInferred from mutant phenotypeⁱ
  • "MnSOD deficiency increases endothelial dysfunction in ApoE-deficient mice."
    Ohashi M., Runge M.S., Faraci F.M., Heistad D.D.
    Arterioscler. Thromb. Vasc. Biol. 26:2331-2336(2006) [PubMed] [Europe PMC] [Abstract]
• age-dependent response to oxidative stress Source: MGIInferred from mutant phenotypeⁱ
  • "Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis."
    Kokoszka J.E., Coskun P., Esposito L.A., Wallace D.C.
    Proc. Natl. Acad. Sci. U.S.A. 98:2278-2283(2001) [PubMed] [Europe PMC] [Abstract]
• age-dependent response to reactive oxygen species Source: UniProtKB
• apoptotic mitochondrial changes Source: MGIInferred from mutant phenotypeⁱ
  • "Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis."
    Kokoszka J.E., Coskun P., Esposito L.A., Wallace D.C.
    Proc. Natl. Acad. Sci. U.S.A. 98:2278-2283(2001) [PubMed] [Europe PMC] [Abstract]
• cellular response to ethanol Source: Ensembl
• detection of oxygen Source: MGIInferred from mutant phenotypeⁱ
  • "Prolonged hypoxia during cell development protects mature manganese superoxide dismutase-deficient astrocytes from damage by oxidative stress."
    Copin J.C., Gasche Y., Li Y., Chan P.H.
    FASEB J. 15:525-534(2001) [PubMed] [Europe PMC] [Abstract]
• erythrophore differentiation Source: MGIInferred from mutant phenotypeⁱ
  • "SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness."
    Friedman J.S., Lopez M.F., Fleming M.D., Rivera A., Martin F.M., Welsh M.L., Boyd A., Doctrow S.R., Burakoff S.J.
    Blood 104:2565-2573(2004) [PubMed] [Europe PMC] [Abstract]
• glutathione metabolic process Source: MGIInferred from mutant phenotypeⁱ
  • "Characterization of the antioxidant status of the heterozygous manganese superoxide dismutase knockout mouse."
    Van Remmen H., Salvador C., Yang H., Huang T.T., Epstein C.J., Richardson A.
    Arch. Biochem. Biophys. 363:91-97(1999) [PubMed] [Europe PMC] [Abstract]
• heart development Source: MGIInferred from mutant phenotypeⁱ
  • "Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase."
    Li Y., Huang T.T., Carlson E.J., Melov S., Ursell P.C., Olson J.L., Noble L.J., Yoshimura M.P., Berger C., Chan P.H., Wallace D.C., Epstein C.J.
    Nat. Genet. 11:376-381(1995) [PubMed] [Europe PMC] [Abstract]
• hemopoiesis Source: MGIInferred from mutant phenotypeⁱ
  • "Adipocyte differentiation in Sod2(-/-) and Sod2(+/+) murine bone marrow stromal cells is associated with low antioxidant pools."
    Lechpammer S., Epperly M.W., Zhou S., Nie S., Glowacki J., Greenberger J.S.
    Exp. Hematol. 33:1201-1208(2005) [PubMed] [Europe PMC] [Abstract]
  • "Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice."
    Lebovitz R.M., Zhang H., Vogel H., Cartwright J. Jr., Dionne L., Lu N., Huang S., Matzuk M.M.
    Proc. Natl. Acad. Sci. U.S.A. 93:9782-9787(1996) [PubMed] [Europe PMC] [Abstract]
• hydrogen peroxide biosynthetic process Source: MGI
• hydrogen peroxide metabolic process Source: MGI
• intrinsic apoptotic signaling pathway in response to DNA damage Source: MGIInferred from mutant phenotypeⁱ
  • "Effects of variation in superoxide dismutases (SOD) on oxidative stress and apoptosis in lens epithelium."
    Reddy V.N., Kasahara E., Hiraoka M., Lin L.R., Ho Y.S.
    Exp. Eye Res. 79:859-868(2004) [PubMed] [Europe PMC] [Abstract]
• intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGIInferred from mutant phenotypeⁱ
  • "Effects of variation in superoxide dismutases (SOD) on oxidative stress and apoptosis in lens epithelium."
    Reddy V.N., Kasahara E., Hiraoka M., Lin L.R., Ho Y.S.
    Exp. Eye Res. 79:859-868(2004) [PubMed] [Europe PMC] [Abstract]
• iron ion homeostasis Source: MGIInferred from mutant phenotypeⁱ
  • "SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness."
    Friedman J.S., Lopez M.F., Fleming M.D., Rivera A., Martin F.M., Welsh M.L., Boyd A., Doctrow S.R., Burakoff S.J.
    Blood 104:2565-2573(2004) [PubMed] [Europe PMC] [Abstract]
• liver development Source: MGIInferred from mutant phenotypeⁱ
  • "Deficiency of manganese superoxide dismutase in hepatocytes disrupts zonated gene expression in mouse liver."
    Lenart J., Dombrowski F., Gorlach A., Kietzmann T.
    Arch. Biochem. Biophys. 462:238-244(2007) [PubMed] [Europe PMC] [Abstract]
• locomotory behavior Source: MGIInferred from mutant phenotypeⁱ
  • "Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice."
    Lebovitz R.M., Zhang H., Vogel H., Cartwright J. Jr., Dionne L., Lu N., Huang S., Matzuk M.M.
    Proc. Natl. Acad. Sci. U.S.A. 93:9782-9787(1996) [PubMed] [Europe PMC] [Abstract]
• mitochondrion organization Source: MGIInferred from mutant phenotypeⁱ
  • "Ocular pathology in mitochondrial superoxide dismutase (Sod2)-deficient mice."
    Sandbach J.M., Coscun P.E., Grossniklaus H.E., Kokoszka J.E., Newman N.J., Wallace D.C.
    Invest. Ophthalmol. Vis. Sci. 42:2173-2178(2001) [PubMed] [Europe PMC] [Abstract]
  • "SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness."
    Friedman J.S., Lopez M.F., Fleming M.D., Rivera A., Martin F.M., Welsh M.L., Boyd A., Doctrow S.R., Burakoff S.J.
    Blood 104:2565-2573(2004) [PubMed] [Europe PMC] [Abstract]
  • "Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice."
    Lebovitz R.M., Zhang H., Vogel H., Cartwright J. Jr., Dionne L., Lu N., Huang S., Matzuk M.M.
    Proc. Natl. Acad. Sci. U.S.A. 93:9782-9787(1996) [PubMed] [Europe PMC] [Abstract]
• negative regulation of apoptotic process Source: MGI
• negative regulation of cell population proliferation Source: MGI
• negative regulation of fat cell differentiation Source: MGIInferred from mutant phenotypeⁱ
  • "Adipocyte differentiation in Sod2(-/-) and Sod2(+/+) murine bone marrow stromal cells is associated with low antioxidant pools."
    Lechpammer S., Epperly M.W., Zhou S., Nie S., Glowacki J., Greenberger J.S.
    Exp. Hematol. 33:1201-1208(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of fibroblast proliferation Source: MGIInferred from direct assayⁱ
  • "An unexpected functional link between lysosomal thiol reductase and mitochondrial manganese superoxide dismutase."
    Bogunovic B., Stojakovic M., Chen L., Maric M.
    J. Biol. Chem. 283:8855-8862(2008) [PubMed] [Europe PMC] [Abstract]
• negative regulation of neuron apoptotic process Source: MGI
• negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
• negative regulation of vascular smooth muscle cell proliferation Source: MGI
• neuron development Source: MGIInferred from mutant phenotypeⁱ
  • "Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice."
    Lebovitz R.M., Zhang H., Vogel H., Cartwright J. Jr., Dionne L., Lu N., Huang S., Matzuk M.M.
    Proc. Natl. Acad. Sci. U.S.A. 93:9782-9787(1996) [PubMed] [Europe PMC] [Abstract]
• oxygen homeostasis Source: MGI
• positive regulation of cell migration Source: MGI
• positive regulation of nitric oxide biosynthetic process Source: MGIInferred from mutant phenotypeⁱ
  • "Increased superoxide leads to decreased flow-induced dilation in resistance arteries of Mn-SOD-deficient mice."
    Yan C., Huang A., Wu Z., Kaminski P.M., Wolin M.S., Hintze T.H., Kaley G., Sun D.
    Am. J. Physiol. Heart Circ. Physiol. 288:H2225-31(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of vascular associated smooth muscle cell apoptotic process Source: MGI
• positive regulation of vascular smooth muscle cell differentiation involved in phenotypic switching Source: MGI
• post-embryonic development Source: MGIInferred from mutant phenotypeⁱ
  • "Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase."
    Li Y., Huang T.T., Carlson E.J., Melov S., Ursell P.C., Olson J.L., Noble L.J., Yoshimura M.P., Berger C., Chan P.H., Wallace D.C., Epstein C.J.
    Nat. Genet. 11:376-381(1995) [PubMed] [Europe PMC] [Abstract]
  • "Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice."
    Lebovitz R.M., Zhang H., Vogel H., Cartwright J. Jr., Dionne L., Lu N., Huang S., Matzuk M.M.
    Proc. Natl. Acad. Sci. U.S.A. 93:9782-9787(1996) [PubMed] [Europe PMC] [Abstract]
• protein homotetramerization Source: MGI
• regulation of blood pressure Source: MGIInferred from mutant phenotypeⁱ
  • "Association of mitochondrial SOD deficiency with salt-sensitive hypertension and accelerated renal senescence."
    Rodriguez-Iturbe B., Sepassi L., Quiroz Y., Ni Z., Wallace D.C., Vaziri N.D.
    J. Appl. Physiol. 102:255-260(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of catalytic activity Source: MGIInferred from mutant phenotypeⁱ
  • "Mitochondrial disease in superoxide dismutase 2 mutant mice."
    Melov S., Coskun P., Patel M., Tuinstra R., Cottrell B., Jun A.S., Zastawny T.H., Dizdaroglu M., Goodman S.I., Huang T.T., Miziorko H., Epstein C.J., Wallace D.C.
    Proc. Natl. Acad. Sci. U.S.A. 96:846-851(1999) [PubMed] [Europe PMC] [Abstract]
• regulation of mitochondrial membrane potential Source: MGIInferred from mutant phenotypeⁱ
  • "Deficiency of manganese superoxide dismutase in hepatocytes disrupts zonated gene expression in mouse liver."
    Lenart J., Dombrowski F., Gorlach A., Kietzmann T.
    Arch. Biochem. Biophys. 462:238-244(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of transcription by RNA polymerase II Source: MGIInferred from direct assayⁱ
  • "High glucose increases angiopoietin-2 transcription in microvascular endothelial cells through methylglyoxal modification of mSin3A."
    Yao D., Taguchi T., Matsumura T., Pestell R., Edelstein D., Giardino I., Suske G., Rabbani N., Thornalley P.J., Sarthy V.P., Hammes H.P., Brownlee M.
    J. Biol. Chem. 282:31038-31045(2007) [PubMed] [Europe PMC] [Abstract]
• release of cytochrome c from mitochondria Source: MGIInferred from mutant phenotypeⁱ
  • "Manganese superoxide dismutase mediates the early release of mitochondrial cytochrome C and subsequent DNA fragmentation after permanent focal cerebral ischemia in mice."
    Fujimura M., Morita-Fujimura Y., Kawase M., Copin J.C., Calagui B., Epstein C.J., Chan P.H.
    J. Neurosci. 19:3414-3422(1999) [PubMed] [Europe PMC] [Abstract]
  • "Effects of variation in superoxide dismutases (SOD) on oxidative stress and apoptosis in lens epithelium."
    Reddy V.N., Kasahara E., Hiraoka M., Lin L.R., Ho Y.S.
    Exp. Eye Res. 79:859-868(2004) [PubMed] [Europe PMC] [Abstract]
• removal of superoxide radicals Source: MGIInferred from mutant phenotypeⁱ
  • "MnSOD deficiency increases endothelial dysfunction in ApoE-deficient mice."
    Ohashi M., Runge M.S., Faraci F.M., Heistad D.D.
    Arterioscler. Thromb. Vasc. Biol. 26:2331-2336(2006) [PubMed] [Europe PMC] [Abstract]
• respiratory electron transport chain Source: MGIInferred from mutant phenotypeⁱ
  • "Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis."
    Kokoszka J.E., Coskun P., Esposito L.A., Wallace D.C.
    Proc. Natl. Acad. Sci. U.S.A. 98:2278-2283(2001) [PubMed] [Europe PMC] [Abstract]
  • "Reversal of the mitochondrial phenotype and slow development of oxidative biomarkers of aging in long-lived Mclk1+/- mice."
    Lapointe J., Stepanyan Z., Bigras E., Hekimi S.
    J. Biol. Chem. 284:20364-20374(2009) [PubMed] [Europe PMC] [Abstract]
• response to activity Source: MGIInferred from mutant phenotypeⁱ
  • "Limited exercise capacity in heterozygous manganese superoxide dismutase gene-knockout mice: roles of superoxide anion and nitric oxide."
    Kinugawa S., Wang Z., Kaminski P.M., Wolin M.S., Edwards J.G., Kaley G., Hintze T.H.
    Circulation 111:1480-1486(2005) [PubMed] [Europe PMC] [Abstract]
• response to axon injury Source: MGIInferred from mutant phenotypeⁱ
  • "Conditional knockout of Mn superoxide dismutase in postnatal motor neurons reveals resistance to mitochondrial generated superoxide radicals."
    Misawa H., Nakata K., Matsuura J., Moriwaki Y., Kawashima K., Shimizu T., Shirasawa T., Takahashi R.
    Neurobiol. Dis. 23:169-177(2006) [PubMed] [Europe PMC] [Abstract]
• response to cadmium ion Source: Ensembl
• response to cold Source: Ensembl
• response to drug Source: MGI
• response to electrical stimulus Source: Ensembl
• response to gamma radiation Source: MGI <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Multiple deficiencies in antioxidant enzymes in mice result in a compound increase in sensitivity to oxidative stress."
    Van Remmen H., Qi W., Sabia M., Freeman G., Estlack L., Yang H., Mao Guo Z., Huang T.T., Strong R., Lee S., Epstein C.J., Richardson A.
    Free Radic. Biol. Med. 36:1625-1634(2004) [PubMed] [Europe PMC] [Abstract]
• response to hydrogen peroxide Source: MGIInferred from mutant phenotypeⁱ
  • "Effects of variation in superoxide dismutases (SOD) on oxidative stress and apoptosis in lens epithelium."
    Reddy V.N., Kasahara E., Hiraoka M., Lin L.R., Ho Y.S.
    Exp. Eye Res. 79:859-868(2004) [PubMed] [Europe PMC] [Abstract]
• response to hyperoxia Source: MGIInferred from mutant phenotypeⁱ
  • "Increased sensitivity of homozygous Sod2 mutant mice to oxygen toxicity."
    Asikainen T.M., Huang T.T., Taskinen E., Levonen A.L., Carlson E., Lapatto R., Epstein C.J., Raivio K.O.
    Free Radic. Biol. Med. 32:175-186(2002) [PubMed] [Europe PMC] [Abstract]
• response to hypoxia Source: Ensembl
• response to immobilization stress Source: Ensembl
• response to isolation stress Source: Ensembl
• response to L-ascorbic acid Source: Ensembl
• response to lipopolysaccharide Source: Ensembl
• response to magnetism Source: Ensembl
• response to manganese ion Source: Ensembl
• response to nutrient levels Source: MGI
• response to oxidative stress Source: MGIInferred from mutant phenotypeⁱ
  • "Multiple deficiencies in antioxidant enzymes in mice result in a compound increase in sensitivity to oxidative stress."
    Van Remmen H., Qi W., Sabia M., Freeman G., Estlack L., Yang H., Mao Guo Z., Huang T.T., Strong R., Lee S., Epstein C.J., Richardson A.
    Free Radic. Biol. Med. 36:1625-1634(2004) [PubMed] [Europe PMC] [Abstract]
  • "Reversal of the mitochondrial phenotype and slow development of oxidative biomarkers of aging in long-lived Mclk1+/- mice."
    Lapointe J., Stepanyan Z., Bigras E., Hekimi S.
    J. Biol. Chem. 284:20364-20374(2009) [PubMed] [Europe PMC] [Abstract]
• response to reactive oxygen species Source: MGIInferred from mutant phenotypeⁱ
  • "SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness."
    Friedman J.S., Lopez M.F., Fleming M.D., Rivera A., Martin F.M., Welsh M.L., Boyd A., Doctrow S.R., Burakoff S.J.
    Blood 104:2565-2573(2004) [PubMed] [Europe PMC] [Abstract]
  • "Adipocyte differentiation in Sod2(-/-) and Sod2(+/+) murine bone marrow stromal cells is associated with low antioxidant pools."
    Lechpammer S., Epperly M.W., Zhou S., Nie S., Glowacki J., Greenberger J.S.
    Exp. Hematol. 33:1201-1208(2005) [PubMed] [Europe PMC] [Abstract]
  • "Genetic modification of the manganese superoxide dismutase/glutathione peroxidase 1 pathway influences intracellular ROS generation in quiescent, but not contracting, skeletal muscle cells."
    Vasilaki A., Csete M., Pye D., Lee S., Palomero J., McArdle F., Van Remmen H., Richardson A., McArdle A., Faulkner J.A., Jackson M.J.
    Free Radic. Biol. Med. 41:1719-1725(2006) [PubMed] [Europe PMC] [Abstract]
  • "A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase."
    Melov S., Schneider J.A., Day B.J., Hinerfeld D., Coskun P., Mirra S.S., Crapo J.D., Wallace D.C.
    Nat. Genet. 18:159-163(1998) [PubMed] [Europe PMC] [Abstract]
  • "Mitochondrial disease in superoxide dismutase 2 mutant mice."
    Melov S., Coskun P., Patel M., Tuinstra R., Cottrell B., Jun A.S., Zastawny T.H., Dizdaroglu M., Goodman S.I., Huang T.T., Miziorko H., Epstein C.J., Wallace D.C.
    Proc. Natl. Acad. Sci. U.S.A. 96:846-851(1999) [PubMed] [Europe PMC] [Abstract]
• response to selenium ion Source: Ensembl
• response to silicon dioxide Source: Ensembl
• response to superoxide Source: MGIInferred from mutant phenotypeⁱ
  • "Prolonged hypoxia during cell development protects mature manganese superoxide dismutase-deficient astrocytes from damage by oxidative stress."
    Copin J.C., Gasche Y., Li Y., Chan P.H.
    FASEB J. 15:525-534(2001) [PubMed] [Europe PMC] [Abstract]
  • "Effects of variation in superoxide dismutases (SOD) on oxidative stress and apoptosis in lens epithelium."
    Reddy V.N., Kasahara E., Hiraoka M., Lin L.R., Ho Y.S.
    Exp. Eye Res. 79:859-868(2004) [PubMed] [Europe PMC] [Abstract]
• response to zinc ion Source: Ensembl
• superoxide anion generation Source: MGIInferred from mutant phenotypeⁱ
  • "Manganese superoxide dismutase mediates the early release of mitochondrial cytochrome C and subsequent DNA fragmentation after permanent focal cerebral ischemia in mice."
    Fujimura M., Morita-Fujimura Y., Kawase M., Copin J.C., Calagui B., Epstein C.J., Chan P.H.
    J. Neurosci. 19:3414-3422(1999) [PubMed] [Europe PMC] [Abstract]
  • "Limited exercise capacity in heterozygous manganese superoxide dismutase gene-knockout mice: roles of superoxide anion and nitric oxide."
    Kinugawa S., Wang Z., Kaminski P.M., Wolin M.S., Edwards J.G., Kaley G., Hintze T.H.
    Circulation 111:1480-1486(2005) [PubMed] [Europe PMC] [Abstract]
  • "Conditional knockout of Mn superoxide dismutase in postnatal motor neurons reveals resistance to mitochondrial generated superoxide radicals."
    Misawa H., Nakata K., Matsuura J., Moriwaki Y., Kawashima K., Shimizu T., Shirasawa T., Takahashi R.
    Neurobiol. Dis. 23:169-177(2006) [PubMed] [Europe PMC] [Abstract]
• superoxide metabolic process Source: MGIInferred from mutant phenotypeⁱ
  • "Characterization of the antioxidant status of the heterozygous manganese superoxide dismutase knockout mouse."
    Van Remmen H., Salvador C., Yang H., Huang T.T., Epstein C.J., Richardson A.
    Arch. Biochem. Biophys. 363:91-97(1999) [PubMed] [Europe PMC] [Abstract]
  • "Model mice for tissue-specific deletion of the manganese superoxide dismutase (MnSOD) gene."
    Ikegami T., Suzuki Y., Shimizu T., Isono K., Koseki H., Shirasawa T.
    Biochem. Biophys. Res. Commun. 296:729-736(2002) [PubMed] [Europe PMC] [Abstract]
  • "Increased superoxide leads to decreased flow-induced dilation in resistance arteries of Mn-SOD-deficient mice."
    Yan C., Huang A., Wu Z., Kaminski P.M., Wolin M.S., Hintze T.H., Kaley G., Sun D.
    Am. J. Physiol. Heart Circ. Physiol. 288:H2225-31(2005) [PubMed] [Europe PMC] [Abstract]
• vasodilation Source: MGIInferred from mutant phenotypeⁱ
  • "Increased superoxide leads to decreased flow-induced dilation in resistance arteries of Mn-SOD-deficient mice."
    Yan C., Huang A., Wu Z., Kaminski P.M., Wolin M.S., Hintze T.H., Kaley G., Sun D.
    Am. J. Physiol. Heart Circ. Physiol. 288:H2225-31(2005) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• enzyme binding Source: MGI
• identical protein binding Source: MGI

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MLCRAACSTG RRLGPVAGAA GSRHKHSLPD LPYDYGALEP HINAQIMQLH 
        60         70         80         90        100
HSKHHAAYVN NLNATEEKYH EALAKGDVTT QVALQPALKF NGGGHINHTI 
       110        120        130        140        150
FWTNLSPKGG GEPKGELLEA IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL 
       160        170        180        190        200
GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY 
       210        220 
LKAIWNVINW ENVTERYTAC KK                               

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families
2. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot