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UniProtKB/Swiss-Prot entry P00441

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Entry information
Entry name SODC_HUMAN
Primary accession number P00441
Secondary accession numbers A6NHJ0 Q16669 Q16711 Q16838 Q16839 Q16840 Q6NR85
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 126)
Name and origin of the protein
Protein name Superoxide dismutase [Cu-Zn]
Synonym EC 1.15.1.1
Gene name
Name: SOD1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6577438 [NCBI, ExPASy, EBI, Israel, Japan]
Sherman L., Dafni N., Lieman-Hurwitz J., Groner Y.;
"Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:5465-5469(1983).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3160582 [NCBI, ExPASy, EBI, Israel, Japan]
Levanon D., Lieman-Hurwitz J., Dafni N., Wigderson M., Sherman L., Bernstein Y., Laver-Rudich Z., Danciger E., Stein O., Groner Y.;
"Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase.";
EMBO J. 4:77-84(1985).
[3]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/13.6.2017; PubMed=3889846 [NCBI, ExPASy, EBI, Israel, Japan]
Hallewell R.A., Masiarz F.R., Najarian R.C., Puma J.P., Quiroga M.R., Randolph A., Sanchez-Pescador R., Scandella C.J., Smith B., Steimer K.S., Mullenbach G.T.;
"Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising high levels of active or inactive enzyme from an expression library.";
Nucleic Acids Res. 13:2017-2034(1985).
[4]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2853161 [NCBI, ExPASy, EBI, Israel, Japan]
Kajihara J., Enomoto M., Nishijima K., Yabuuchi M., Katoh K.;
"Comparison of properties between human recombinant and placental copper-zinc SOD.";
J. Biochem. 104:851-854(1988).
[5]
 NUCLEOTIDE SEQUENCE [MRNA].
Xu Y., Hu X., Zhou Y., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[6]
 NUCLEOTIDE SEQUENCE [MRNA].
Lu X., Hui L.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[7]
 NUCLEOTIDE SEQUENCE [MRNA].
Staege M.S., Bergmann S., Heins S.;
"Direct sequencing and cloning of superoxide dismutase 1 from peripheral blood.";
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[8]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[10]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[11]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[12]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[13]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/35012518; PubMed=10830953 [NCBI, ExPASy, EBI, Israel, Japan]
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[14]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[15]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[16]
 PROTEIN SEQUENCE OF 2-154.
DOI=10.1021/bi00552a005; PubMed=6770891 [NCBI, ExPASy, EBI, Israel, Japan]
Jabusch J.R., Farb D.L., Kerschensteiner D.A., Deutsch H.F.;
"Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase.";
Biochemistry 19:2310-2316(1980).
[17]
 PROTEIN SEQUENCE OF 2-154.
DOI=10.1016/0014-5793(80)81044-1; PubMed=7002610 [NCBI, ExPASy, EBI, Israel, Japan]
Barra D., Martini F., Bannister J.V., Schinina M.E., Rotilio G., Bannister W.H., Bossa F.;
"The complete amino acid sequence of human Cu/Zn superoxide dismutase.";
FEBS Lett. 120:53-56(1980).
[18]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-56 AND 120-154, AND VARIANTS ALS1 GLN-49; ARG-94; THR-113; THR-114; HIS-126 AND THR-150.
DOI=10.1093/hmg/4.7.1239; PubMed=8528216 [NCBI, ExPASy, EBI, Israel, Japan]
Enayat Z.E., Orrell R.W., Claus A., Ludolph A., Bachus R., Brockmueller J., Ray-Chaudhuri K., Radunovic A., Shaw C., Wilkinson J., King A., Swash M., Leigh P.N., de Belleroche J., Powell J.;
"Two novel mutations in the gene for copper zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis.";
Hum. Mol. Genet. 4:1239-1240(1995).
[19]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-154, AND VARIANT ALS1 THR-152.
DOI=10.1007/s004390050157; PubMed=8682505 [NCBI, ExPASy, EBI, Israel, Japan]
Kostrzewa M., Daamian M., Mueller U.;
"Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis.";
Hum. Genet. 98:48-50(1996).
[20]
 SUBUNIT, AND DISULFIDE BOND.
DOI=10.1074/jbc.M406021200; PubMed=15326189 [NCBI, ExPASy, EBI, Israel, Japan]
Arnesano F., Banci L., Bertini I., Martinelli M., Furukawa Y., O'Halloran T.V.;
"The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status.";
J. Biol. Chem. 279:47998-48003(2004).
[21]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=1463506 [NCBI, ExPASy, EBI, Israel, Japan]
Parge H.E., Hallewell R.A., Tainer J.A.;
"Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.";
Proc. Natl. Acad. Sci. U.S.A. 89:6109-6113(1992).
[22]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ALS1 ARG-38.
PubMed=9541385 [NCBI, ExPASy, EBI, Israel, Japan]
Hart P.J., Liu H., Pellegrini M., Nersissian A.M., Gralla E.B., Valentine J.S., Eisenberg D.;
"Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis.";
Protein Sci. 7:545-555(1998).
[23]
 STRUCTURE BY NMR.
DOI=10.1021/bi9803473; PubMed=9718300 [NCBI, ExPASy, EBI, Israel, Japan]
Banci L., Benedetto M., Bertini I., del Conte R., Piccioli M., Viezzoli M.S.;
"Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?";
Biochemistry 37:11780-11791(1998).
[24]
 X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF MUTANT GLU-51/GLU-52/GLN-134, SUBUNIT, AND MUTAGENESIS OF 51-PHE-GLY-52 AND GLU-134.
DOI=10.1006/jmbi.1999.2681; PubMed=10329151 [NCBI, ExPASy, EBI, Israel, Japan]
Ferraroni M., Rypniewski W., Wilson K.S., Viezzoli M.S., Banci L., Bertini I., Mangani S.;
"The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited.";
J. Mol. Biol. 288:413-426(1999).
[25]
 STRUCTURE BY NMR OF MUTANT GLU51/GLU-52/GLN-134, AND SUBUNIT.
DOI=10.1021/bi034324m; PubMed=12911296 [NCBI, ExPASy, EBI, Israel, Japan]
Banci L., Bertini I., Cramaro F., Del Conte R., Viezzoli M.S.;
"Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding.";
Biochemistry 42:9543-9553(2003).
[26]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS, DISULFIDE BOND, SUBUNIT, AND CHARACTERIZATION OF VARIANTS ALS1 VAL-5 AND ARG-44.
DOI=10.1016/S0022-2836(03)00889-1; PubMed=12963370 [NCBI, ExPASy, EBI, Israel, Japan]
DiDonato M., Craig L., Huff M.E., Thayer M.M., Cardoso R.M., Kassmann C.J., Lo T.P., Bruns C.K., Powers E.T., Kelly J.W., Getzoff E.D., Tainer J.A.;
"ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization.";
J. Mol. Biol. 332:601-615(2003).
[27]
 X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANTS ALS1 ASN-135 AND ARG-47, AND FORMATION OF FIBRILLAR AGGREGATES.
DOI=10.1038/nsb935; PubMed=12754496 [NCBI, ExPASy, EBI, Israel, Japan]
Elam J.S., Taylor A.B., Strange R., Antonyuk S., Doucette P.A., Rodriguez J.A., Hasnain S.S., Hayward L.J., Valentine J.S., Yeates T.O., Hart P.J.;
"Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS.";
Nat. Struct. Biol. 10:461-467(2003).
[28]
 X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF VARIANTS ALS1 VAL-5 AND THR-114, AND CHARACTERIZATION OF VARIANTS ALS1 VAL-5 AND THR-114.
DOI=10.1073/pnas.0305143101; PubMed=15056757 [NCBI, ExPASy, EBI, Israel, Japan]
Hough M.A., Grossmann J.G., Antonyuk S.V., Strange R.W., Doucette P.A., Rodriguez J.A., Whitson L.J., Hart P.J., Hayward L.J., Valentine J.S., Hasnain S.S.;
"Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants.";
Proc. Natl. Acad. Sci. U.S.A. 101:5976-5981(2004).
[29]
 STRUCTURE BY NMR OF MUTANT ALA-7/SER-112, AND SUBUNIT.
DOI=10.1074/jbc.M506497200; PubMed=16291742 [NCBI, ExPASy, EBI, Israel, Japan]
Banci L., Bertini I., Cantini F., D'Amelio N., Gaggelli E.;
"Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form.";
J. Biol. Chem. 281:2333-2337(2006).
[30]
 X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEXES WITH COPPER AND ZINC IONS, DISULFIDE BOND, AND SUBUNIT.
DOI=10.1016/j.jmb.2005.11.081; PubMed=16406071 [NCBI, ExPASy, EBI, Israel, Japan]
Strange R.W., Antonyuk S.V., Hough M.A., Doucette P.A., Valentine J.S., Hasnain S.S.;
"Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes.";
J. Mol. Biol. 356:1152-1162(2006).
[31]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ALA-7/ALA-112 AND ALA-7/ALA-58/ALA-112/ALA-147, AND MUTAGENESIS OF CYS-7; CYS-58; CYS-112 AND CYS-147.
DOI=10.1016/j.jmb.2006.09.048; PubMed=17070542 [NCBI, ExPASy, EBI, Israel, Japan]
Hoernberg A., Logan D.T., Marklund S.L., Oliveberg M.;
"The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase.";
J. Mol. Biol. 365:333-342(2007).
[32]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT SER-81/SER-84 IN COMPLEX WITH COPPER IONS, SUBUNIT, MUTAGENESIS OF HIS-81 AND ASP-84, AND COFACTOR.
DOI=10.1016/j.jmb.2007.07.043; PubMed=17888947 [NCBI, ExPASy, EBI, Israel, Japan]
Roberts B.R., Tainer J.A., Getzoff E.D., Malencik D.A., Anderson S.R., Bomben V.C., Meyers K.R., Karplus P.A., Beckman J.S.;
"Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS.";
J. Mol. Biol. 373:877-890(2007).
[33]
 X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS, SUBUNIT, AND FORMATION OF FIBRILLAR AGGREGATES BY ZINC-DEPLETED SOD1.
DOI=10.1073/pnas.0703857104; PubMed=17548825 [NCBI, ExPASy, EBI, Israel, Japan]
Strange R.W., Yong C.W., Smith W., Hasnain S.S.;
"Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.";
Proc. Natl. Acad. Sci. U.S.A. 104:10040-10044(2007).
[34]
 X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANT ALS1 ARG-86, AND CHARACTERIZATION OF VARIANT ALS1 ARG-86.
DOI=10.1074/jbc.M801522200; PubMed=18378676 [NCBI, ExPASy, EBI, Israel, Japan]
Cao X., Antonyuk S.V., Seetharaman S.V., Whitson L.J., Taylor A.B., Holloway S.P., Strange R.W., Doucette P.A., Valentine J.S., Tiwari A., Hayward L.J., Padua S., Cohlberg J.A., Hasnain S.S., Hart P.J.;
"Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis.";
J. Biol. Chem. 283:16169-16177(2008).
[35]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ALS1 ARG-86.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of human Cu-Zn superoxide dismutase mutant G85R (P21).";
Submitted (APR-2008) to the PDB data bank.
[36]
 REVIEW ON VARIANTS.
PubMed=8592323 [NCBI, ExPASy, EBI, Israel, Japan]
de Belleroche J., Orrell R., King A.;
"Familial amyotrophic lateral sclerosis/motor neurone disease (FALS): a review of current developments.";
J. Med. Genet. 32:841-847(1995).
[37]
 VARIANTS ALS1.
DOI=10.1038/362059a0; PubMed=8446170 [NCBI, ExPASy, EBI, Israel, Japan]
Rosen D.R., Siddique T., Patterson D., Figlewicz D.A., Sapp P., Hentati A., Donaldson D., Goto J., O'Regan J.P., Deng H.-X., Rahmani Z., Krizus A., McKenna-Yasek D., Cayabyab A., Gaston S.M., Berger R., Tanzi R.E., Halperin J.J., Herzfeldt B., van den Bergh R., Hung W.-Y., Bird T., Deng G., Mulder D.W., Smyth C., Laing N.G., Soriano E., Pericak-Vance M.A., Haines J., Rouleau G.A., Gusella J.S., Horvitz H.R., Brown R.H. Jr.;
"Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis.";
Nature 362:59-62(1993).
[38]
 ERRATUM.
PubMed=8332197 [NCBI, ExPASy, EBI, Israel, Japan]
Rosen D.R.;
Nature 364:362-362(1993).
[39]
 VARIANTS ALS1.
PubMed=8351519 [NCBI, ExPASy, EBI, Israel, Japan]
Deng H.-X., Hentati A., Tainer J.A., Iqbal Z., Cayabyab A., Hung W.-Y., Getzoff E.D., Hu P., Herzfeldt B., Roos R.P., Warner C., Deng G., Soriano E., Smyth C., Parge H.E., Ahmed A., Roses A.D., Hallewell R.A., Pericak-Vance M.A., Siddique T.;
"Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.";
Science 261:1047-1051(1993).
[40]
 VARIANT ALS1 THR-5.
DOI=10.1006/bbrc.1994.1506; PubMed=8179602 [NCBI, ExPASy, EBI, Israel, Japan]
Nakano R., Sato S., Inuzuka T., Sakimura K., Mishina M., Takahashi H., Ikuta F., Honma Y., Fujii J., Taniguchi N., Tsuji S.;
"A novel mutation in Cu/Zn superoxide dismutase gene in Japanese familial amyotrophic lateral sclerosis.";
Biochem. Biophys. Res. Commun. 200:695-703(1994).
[41]
 VARIANT ALS1 GLU-8.
DOI=10.1006/bbrc.1994.2497; PubMed=7980516 [NCBI, ExPASy, EBI, Israel, Japan]
Hirano M., Fujii J., Nagai Y., Sonobe M., Okamoto K., Araki H., Taniguchi N., Ueno S.;
"A new variant Cu/Zn superoxide dismutase (Val7-->Glu) deduced from lymphocyte mRNA sequences from Japanese patients with familial amyotrophic lateral sclerosis.";
Biochem. Biophys. Res. Commun. 204:572-577(1994).
[42]
 VARIANT ALS1 LYS-22.
DOI=10.1093/hmg/3.4.649; PubMed=8069312 [NCBI, ExPASy, EBI, Israel, Japan]
Jones C.T., Swinger R.J., Brock D.J.H.;
"Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of Ile113Thr in three others.";
Hum. Mol. Genet. 3:649-650(1994).
[43]
 VARIANTS ALS1 ASP-94 AND THR-113.
DOI=10.1093/hmg/3.6.997; PubMed=7951252 [NCBI, ExPASy, EBI, Israel, Japan]
Esteban J., Rosen D.R., Bowling A.C., Sapp P., McKenna-Yasek D., O'Regan J.P., Beal M.F., Horvitz H.R., Brown R.H. Jr.;
"Identification of two novel mutations and a new polymorphism in the gene for Cu/Zn superoxide dismutase in patients with amyotrophic lateral sclerosis.";
Hum. Mol. Genet. 3:997-998(1994).
[44]
 VARIANT ALS1 GLY-116.
DOI=10.1093/hmg/3.12.2261; PubMed=7881433 [NCBI, ExPASy, EBI, Israel, Japan]
Kostrzewa M., Burck-Lehmann U., Mueller U.;
"Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in the Cu/Zn superoxide dismutase-1 gene.";
Hum. Mol. Genet. 3:2261-2262(1994).
[45]
 VARIANT ALS1 ARG-47.
DOI=10.1016/0022-510X(94)90097-3; PubMed=7836951 [NCBI, ExPASy, EBI, Israel, Japan]
Aoki M., Ogasawara M., Matsubara Y., Narisawa K., Nakamura S., Itoyama Y., Abe K.;
"Familial amyotrophic lateral sclerosis (ALS) in Japan associated with H46R mutation in Cu/Zn superoxide dismutase gene: a possible new subtype of familial ALS.";
J. Neurol. Sci. 126:77-83(1994).
[46]
 VARIANT ALS1 THR-114.
DOI=10.1016/S0140-6736(94)92913-0; PubMed=7997024 [NCBI, ExPASy, EBI, Israel, Japan]
Suthers G., Laing N., Wilton S., Dorosz S., Waddy H.;
"'Sporadic' motoneuron disease due to familial SOD1 mutation with low penetrance.";
Lancet 344:1773-1773(1994).
[47]
 VARIANT ALS1 ASN-102.
DOI=10.1006/mcpr.1994.1046; PubMed=7870076 [NCBI, ExPASy, EBI, Israel, Japan]
Jones C.T., Shaw P.J., Chari G., Brock D.J.;
"Identification of a novel exon 4 SOD1 mutation in a sporadic amyotrophic lateral sclerosis patient.";
Mol. Cell. Probes 8:329-330(1994).
[48]
 VARIANTS ALS1.
PubMed=7887412 [NCBI, ExPASy, EBI, Israel, Japan]
Pramatarova A., Figlewicz D.A., Krizus A., Han F.Y., Ceballos-Picot I., Nicole A., Dib M., Meininger V., Brown R.H. Jr., Rouleau G.A.;
"Identification of new mutations in the Cu/Zn superoxide dismutase gene of patients with familial amyotrophic lateral sclerosis.";
Am. J. Hum. Genet. 56:592-596(1995).
[49]
 VARIANT ALS1 ILE-149.
DOI=10.1093/hmg/4.3.491; PubMed=7795609 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda M., Abe K., Aoki M., Ogasawara M., Kameya T., Watanabe M., Shoji M., Hirai S., Itoyama Y.;
"A novel point mutation in the Cu/Zn superoxide dismutase gene in a patient with familial amyotrophic lateral sclerosis.";
Hum. Mol. Genet. 4:491-492(1995).
[50]
 VARIANT ALS1 GLY-102.
DOI=10.1093/hmg/4.6.1101; PubMed=7655468 [NCBI, ExPASy, EBI, Israel, Japan]
Yulug I.G., Katsanis N., de Belleroche J., Collinge J., Fisher E.M.C.;
"An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4.";
Hum. Mol. Genet. 4:1101-1104(1995).
[51]
 VARIANT ALS1 ALA-91.
DOI=10.1093/hmg/4.6.1105; PubMed=7655469 [NCBI, ExPASy, EBI, Israel, Japan]
Sjaelander A., Beckman G., Deng H.-X., Iqbal Z., Tainer J.A., Siddique T.;
"The D90A mutation results in a polymorphism of Cu,Zn superoxide dismutase that is prevalent in northern Sweden and Finland.";
Hum. Mol. Genet. 4:1105-1108(1995).
[52]
 VARIANTS ALS1 MET-15 AND VAL-85.
DOI=10.1093/hmg/4.6.1113; PubMed=7655471 [NCBI, ExPASy, EBI, Israel, Japan]
Deng H.-X., Tainer J.A., Mitsumoto H., Ohnishi A., He X., Hung W.-Y., Zhao Y., Juneja T., Hentati A., Siddique T.;
"Two novel SOD1 mutations in patients with familial amyotrophic lateral sclerosis.";
Hum. Mol. Genet. 4:1113-1116(1995).
[53]
 VARIANT ALS1 ARG-94.
DOI=10.1038/374504a0; PubMed=7700376 [NCBI, ExPASy, EBI, Israel, Japan]
Orrell R., de Belleroche J., Marklund S., Bowe F., Hallewell R.;
"A novel SOD mutant and ALS.";
Nature 374:504-505(1995).
[54]
 VARIANT ALS1 ALA-91.
DOI=10.1038/ng0595-61; PubMed=7647793 [NCBI, ExPASy, EBI, Israel, Japan]
Andersen P.M., Nilsson P., Ala-Hurula V., Keraenen M.-L., Tarvainen I., Haltia T., Nilsson L., Binzer M., Forsgren L., Marklund S.L.;
"Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase.";
Nat. Genet. 10:61-66(1995).
[55]
 VARIANT ALS1 PHE-105.
PubMed=7501156 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda M., Abe K., Aoki M., Sahara M., Watanabe M., Shoji M., St George-Hyslop P.H., Hirai S., Itoyama Y.;
"Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene.";
Neurology 45:2038-2042(1995).
[56]
 VARIANTS ALS1 SER-145; THR-146 AND PHE-LEU-GLN-119 INS.
DOI=10.1016/0960-8966(95)00007-A; PubMed=7496169 [NCBI, ExPASy, EBI, Israel, Japan]
Sapp P.C., Rosen D.R., Hosler B.A., Esteban J., McKenna-Yasek D., O'Regan J.P., Horvitz H.R., Brown R.H. Jr.;
"Identification of three novel mutations in the gene for Cu/Zn superoxide dismutase in patients with familial amyotrophic lateral sclerosis.";
Neuromuscul. Disord. 5:353-357(1995).
[57]
 VARIANTS ALS1 VAL-94; VAL-125 AND GLU-134 DEL.
DOI=10.1016/0960-8966(96)00353-7; PubMed=8938700 [NCBI, ExPASy, EBI, Israel, Japan]
Hosler B.A., Nicholson G.A., Sapp P.C., Chin W., Orrell R.W., de Belleroche J.S., Esteban J., Hayward L.J., Mckenna-Yasek D., Yeung L., Cherryson A.K., Dench J.E., Wilton S.D., Laing N.G., Horvitz R.H., Brown R.H. Jr.;
"Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral sclerosis.";
Neuromuscul. Disord. 6:361-366(1996).
[58]
 VARIANT ALS1 PHE-7.
DOI=10.1016/0304-3940(96)12378-8; PubMed=8907321 [NCBI, ExPASy, EBI, Israel, Japan]
Morita M., Aoki M., Abe K., Hasegawa T., Sakuma R., Onodera Y., Ichikawa N., Nishizawa M., Itoyama Y.;
"A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan.";
Neurosci. Lett. 205:79-82(1996).
[59]
 VARIANT ALS1 ASN-135.
DOI=10.1002/(SICI)1098-1004(1997)9:1<69::AID-HUMU14>3.3.CO;2-I; PubMed=8990014 [NCBI, ExPASy, EBI, Israel, Japan]
Watanabe M., Aoki M., Abe K., Shoji M., Lizuka T., Ikeda Y., Hirai S., Kurokawa K., Kato T., Sasaki H., Itoyama Y.;
"A novel missense point mutation (S134N) of the Cu/Zn superoxide dismutase gene in a patient with familial motor neuron disease.";
Hum. Mutat. 9:69-71(1997).
[60]
 VARIANT ALS1 SER-17.
DOI=10.1002/(SICI)1098-1004(1997)9:4<356::AID-HUMU9>3.3.CO;2-3; PubMed=9101297 [NCBI, ExPASy, EBI, Israel, Japan]
Kawamata J., Shimohama S., Takano S., Harada K., Ueda K., Kimura J.;
"Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with apparently sporadic young-onset amyotrophic lateral sclerosis.";
Hum. Mutat. 9:356-358(1997).
[61]
 VARIANT ALS1 SER-73.
DOI=10.1016/S0022-510X(97)00181-0; PubMed=9455977 [NCBI, ExPASy, EBI, Israel, Japan]
Orrell R.W., Marklund S.L., deBelleroche J.S.;
"Familial ALS is associated with mutations in all exons of SOD1: a novel mutation in exon 3 (Gly72Ser).";
J. Neurol. Sci. 153:46-49(1997).
[62]
 VARIANT ALS1 THR-114.
DOI=10.1007/s100480050016; PubMed=10732812 [NCBI, ExPASy, EBI, Israel, Japan]
Kikugawa K., Nakano R., Inuzuka T., Kokubo Y., Narita Y., Kuzuhara S., Yoshida S., Tsuji S.;
"A missense mutation in the SOD1 gene in patients with amyotrophic lateral sclerosis from the Kii Peninsula and its vicinity, Japan.";
Neurogenetics 1:113-115(1997).
[63]
 VARIANT ALS1 GLN-9.
DOI=10.1016/S0960-8966(96)00419-1; PubMed=9131652 [NCBI, ExPASy, EBI, Israel, Japan]
Bereznai B., Winkler A., Borasio G.D., Gasser T.;
"A novel SOD1 mutation in an Austrian family with amyotrophic lateral sclerosis.";
Neuromuscul. Disord. 7:113-116(1997).
[64]
 CHARACTERIZATION OF VARIANTS ALS1 VAL-5; ARG-38; ARG-47; GLN-49; ARG-86 AND THR-114.
DOI=10.1093/hmg/8.8.1451; PubMed=10400992 [NCBI, ExPASy, EBI, Israel, Japan]
Ratovitski T., Corson L.B., Strain J., Wong P., Cleveland D.W., Culotta V.C., Borchelt D.R.;
"Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds.";
Hum. Mol. Genet. 8:1451-1460(1999).
[65]
 VARIANT ALS1 ARG-13.
PubMed=10430435 [NCBI, ExPASy, EBI, Israel, Japan]
Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M., Bugiani O., Ajmar F., Garre C.;
"A SOD1 gene mutation in a patient with slowly progressing familial ALS.";
Neurology 53:404-406(1999).
[66]
 ERRATUM.
Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M., Bugiani O., Ajmar F., Garre C.;
Neurology 57:1146-1146(2001).
[67]
 VARIANT ALS1 SER-127.
DOI=10.1016/S0022-510X(01)00558-5; PubMed=11535232 [NCBI, ExPASy, EBI, Israel, Japan]
Murakami T., Warita H., Hayashi T., Sato K., Manabe Y., Mizuno S., Yamane K., Abe K.;
"A novel SOD1 gene mutation in familial ALS with low penetrance in females.";
J. Neurol. Sci. 189:45-47(2001).
[68]
 VARIANT ALS1 CYS-46.
DOI=10.1016/S0960-8966(00)00215-7; PubMed=11369193 [NCBI, ExPASy, EBI, Israel, Japan]
Gellera C., Castellotti B., Riggio M.C., Silani V., Morandi L., Testa D., Casali C., Taroni F., Di Donato S., Zeviani M., Mariotti C.;
"Superoxide dismutase gene mutations in Italian patients with familial and sporadic amyotrophic lateral sclerosis: identification of three novel missense mutations.";
Neuromuscul. Disord. 11:404-410(2001).
[69]
 VARIANT ALS1 ALA-81.
DOI=10.1002/ana.10369; PubMed=12402272 [NCBI, ExPASy, EBI, Israel, Japan]
Alexander M.D., Traynor B.J., Miller N., Corr B., Frost E., McQuaid S., Brett F.M., Green A., Hardiman O.;
"'True' sporadic ALS associated with a novel SOD-1 mutation.";
Ann. Neurol. 52:680-683(2002).
[70]
 CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-47; ARG-86 AND ALA-94, INTERACTION WITH RNF19A, AND UBIQUITINATION.
DOI=10.1074/jbc.M206559200; PubMed=12145308 [NCBI, ExPASy, EBI, Israel, Japan]
Niwa J., Ishigaki S., Hishikawa N., Yamamoto M., Doyu M., Murata S., Tanaka K., Taniguchi N., Sobue G.;
"Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity.";
J. Biol. Chem. 277:36793-36798(2002).
[71]
 VARIANTS ALS1 VAL-9; CYS-21; LEU-23; ARG-49; ARG-55; ALA-88; THR-90; MET-98; LEU-119; GLY-125 AND ARG-148.
PubMed=14506936 [NCBI, ExPASy, EBI, Israel, Japan]
Andersen P.M., Sims K.B., Xin W.W., Kiely R., O'Neill G., Ravits J., Pioro E., Harati Y., Brower R.D., Levine J.S., Heinicke H.U., Seltzer W., Boss M., Brown R.H. Jr.;
"Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes.";
Amyotroph. Lateral Scler. 4:62-73(2003).
[72]
 CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-86 AND ARG-94, MUTAGENESIS OF CYS-7; 51-PHE-GLY-52; CYS-58; HIS-81; ASP-84; CYS-112 AND CYS-147, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.M802083200; PubMed=18552350 [NCBI, ExPASy, EBI, Israel, Japan]
Furukawa Y., Kaneko K., Yamanaka K., O'Halloran T.V., Nukina N.;
"Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis.";
J. Biol. Chem. 283:24167-24176(2008).
[73]
 CHARACTERIZATION OF VARIANTS ALS1 ARG-55; ALA-91; ALA-94; ASP-94; MET-98 AND PHE-145.
DOI=10.1371/journal.pone.0001677; PubMed=18301754 [NCBI, ExPASy, EBI, Israel, Japan]
Banci L., Bertini I., Boca M., Girotto S., Martinelli M., Valentine J.S., Vieru M.;
"SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization.";
PLoS ONE 3:E1677-E1677(2008).
Comments
  • FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
  • CATALYTIC ACTIVITY: 2 superoxide + 2 H+ = O2 + H2O2.
  • COFACTOR: Binds 1 copper ion per subunit.
  • COFACTOR: Binds 1 zinc ion per subunit.
  • SUBUNIT: Homodimer. The pathogenics variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 interact with RNF19A, whereas wild-type protein does not.
  • INTERACTION:
    P26339:Chga (xeno); NbExp=2; IntAct=EBI-990792, EBI-990900;
    P16014:Chgb (xeno); NbExp=2; IntAct=EBI-990792, EBI-990820;
    Q62313:Tgoln1 (xeno); NbExp=1; IntAct=EBI-990792, EBI-991369;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • PTM: Unlike wild-type protein, the pathogenics variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A; which leads to their proteasomal degradation.
  • DISEASE: Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:105400]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.
  • MISCELLANEOUS: The protein (both wild-type and ALS1 variants) has a tendency to form fibrillar aggregates in the absence of the intramolecular disulfide bond or of bound zinc ions. These aggregates may have cytotoxic effects. Zinc binding promotes dimerization and stabilizes the native form.