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HMDB Protein ID HMDBP03151
Secondary Accession Numbers
  • 8702
Name Extracellular superoxide dismutase [Cu-Zn]
  1. EC-SOD
Gene Name SOD3
Protein Type Unknown
Biological Properties
General Function Involved in metal ion binding
Specific Function Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
  • Degradation of Superoxides
Superoxide + Hydrogen Ion → Oxygen + Hydrogen peroxide details
GO Classification
Biological Process
removal of superoxide radicals
response to hypoxia
response to copper ion
Cellular Component
trans-Golgi network
extracellular space
extracellular matrix
ion binding
cation binding
metal ion binding
Molecular Function
superoxide dismutase activity
zinc ion binding
copper ion binding
heparin binding
metabolic process
cellular metabolic process
oxidation reduction
oxygen and reactive oxygen species metabolic process
superoxide metabolic process
Cellular Location
  1. Secreted
  2. extracellular space
Gene Properties
Chromosome Location 4
Locus 4p15.2
Gene Sequence
>723 bp
Protein Properties
Number of Residues 240
Molecular Weight 25850.675
Theoretical pI 6.604
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Extracellular superoxide dismutase [Cu-Zn]
GenBank ID Protein 338284
UniProtKB/Swiss-Prot ID P08294
UniProtKB/Swiss-Prot Entry Name SODE_HUMAN
GenBank Gene ID J02947
GeneCard ID SOD3
GenAtlas ID SOD3
General References
  1. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed:16335952 ]
  4. Hjalmarsson K, Marklund SL, Engstrom A, Edlund T: Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6340-4. [PubMed:3476950 ]
  5. Folz RJ, Crapo JD: Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene. Genomics. 1994 Jul 1;22(1):162-71. [PubMed:7959763 ]
  6. Adachi T, Ohta H, Hayashi K, Hirano K, Marklund SL: The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro. Free Radic Biol Med. 1992 Sep;13(3):205-10. [PubMed:1505778 ]
  7. Nozik-Grayck E, Suliman HB, Piantadosi CA: Extracellular superoxide dismutase. Int J Biochem Cell Biol. 2005 Dec;37(12):2466-71. Epub 2005 Jul 21. [PubMed:16087389 ]
  8. Antonyuk SV, Strange RW, Marklund SL, Hasnain SS: The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding. J Mol Biol. 2009 May 1;388(2):310-26. doi: 10.1016/j.jmb.2009.03.026. Epub 2009 Mar 14. [PubMed:19289127 ]
  9. Sandstrom J, Nilsson P, Karlsson K, Marklund SL: 10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain. J Biol Chem. 1994 Jul 22;269(29):19163-6. [PubMed:8034674 ]
  10. Yamada H, Yamada Y, Adachi T, Goto H, Ogasawara N, Futenma A, Kitano M, Hirano K, Kato K: Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum. Jpn J Hum Genet. 1995 Jun;40(2):177-84. [PubMed:7662997 ]
  11. Adachi T, Yamada H, Yamada Y, Morihara N, Yamazaki N, Murakami T, Futenma A, Kato K, Hirano K: Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface. Biochem J. 1996 Jan 1;313 ( Pt 1):235-9. [PubMed:8546689 ]
  12. Adachi T, Morihara N, Yamazaki N, Yamada H, Futenma A, Kato K, Hirano K: An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases. J Biochem. 1996 Jul;120(1):184-8. [PubMed:8864862 ]