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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    June 16, 2009 (Entry version 134)
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].
DOI=10.1073/pnas.80.18.5465; 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]
 PROTEIN SEQUENCE OF 11-24 AND 81-116.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[19]
 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).
[20]
 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).
[21]
 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).
[22]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
 IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[24]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1073/pnas.89.13.6109; 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).
[25]
 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).
[26]
 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).
[27]
 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).
[28]
 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).
[29]
 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).
[30]
 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).
[31]
 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).
[32]
 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).
[33]
 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).
[34]
 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).
[35]
 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).
[36]
 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).
[37]
 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).
[38]
 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.
[39]
 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).
[40]
 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).
[41]
 ERRATUM.
PubMed=8332197 [NCBI, ExPASy, EBI, Israel, Japan]
Rosen D.R.;
Nature 364:362-362(1993).
[42]
 VARIANTS ALS1.
DOI=10.1126/science.8351519; 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).
[43]
 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).
[44]
 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).
[45]
 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).
[46]
 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).
[47]
 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).
[48]
 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).
[49]
 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).
[50]
 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).
[51]
 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).
[52]
 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).
[53]
 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).
[54]
 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).
[55]
 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).
[56]
 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).
[57]
 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).
[58]
 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).
[59]
 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).
[60]
 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).
[61]
 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).
[62]
 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).
[63]
 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).
[64]
 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).
[65]
 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).
[66]
 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).
[67]
 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).
[68]
 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).
[69]
 ERRATUM.
Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M., Bugiani O., Ajmar F., Garre C.;
Neurology 57:1146-1146(2001).
[70]
 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).
[71]
 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).
[72]
 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).
[73]
 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).
[74]
 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).
[75]
 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).
[76]
 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
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L44139; AAB05662.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L44135; AAB05662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L44136; AAB05662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L44137; AAB05662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L44139; AAB05661.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L44135; AAB05661.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L44136; AAB05661.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L44137; AAB05661.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02317; CAA26182.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01780; CAA25915.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01781; CAA25916.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01782; CAA25917.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01783; CAA25918.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01784; CAA25919.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY049787; AAL15444.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY450286; AAR21563.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
EF151142; ABL96616.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312116; BAG35052.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR450355; CAG29351.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541742; CAG46542.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006676; AAP35322.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY835629; AAV80422.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000253; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471079; EAX09889.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001034; AAH01034.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L46374; AAB59626.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L46375; AAB59627.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L44746; AAC41773.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X95228; CAA64520.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00218733; -.
PIR A22703; DSHUCZ.
RefSeq NP_000445.1; -.
UniGene Hs.443914
3D structure databases
PDB
1AZV; X-ray; 1.90 A; A/B=2-154.[ExPASy / RCSB / EBI]
1BA9; NMR; -; A=2-154.[ExPASy / RCSB / EBI]
1DSW; NMR; -; A=2-154.[ExPASy / RCSB / EBI]
1FUN; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J=2-153.[ExPASy / RCSB / EBI]
1HL4; X-ray; 1.82 A; A/B/C/D=2-154.[ExPASy / RCSB / EBI]
1HL5; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/S=2-154.[ExPASy / RCSB / EBI]
1KMG; NMR; -; A=2-153.[ExPASy / RCSB / EBI]
1L3N; NMR; -; A/B=2-153.[ExPASy / RCSB / EBI]
1MFM; X-ray; 1.02 A; A=2-154.[ExPASy / RCSB / EBI]
1N18; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=1-154.[ExPASy / RCSB / EBI]
1N19; X-ray; 1.86 A; A/B=1-154.[ExPASy / RCSB / EBI]
1OEZ; X-ray; 2.15 A; W/X/Y/Z=2-154.[ExPASy / RCSB / EBI]
1OZT; X-ray; 2.50 A; G/H/I/J/K/L/M/N=2-154.[ExPASy / RCSB / EBI]
1OZU; X-ray; 1.30 A; A/B=2-154.[ExPASy / RCSB / EBI]
1P1V; X-ray; 1.40 A; A/B/C=2-153.[ExPASy / RCSB / EBI]
1PTZ; X-ray; 1.80 A; A/B=2-154.[ExPASy / RCSB / EBI]
1PU0; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-154.[ExPASy / RCSB / EBI]
1RK7; NMR; -; A=2-154.[ExPASy / RCSB / EBI]
1SOS; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=2-154.[ExPASy / RCSB / EBI]
1SPD; X-ray; 2.40 A; A/B=2-154.[ExPASy / RCSB / EBI]
1UXL; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J=2-154.[ExPASy / RCSB / EBI]
1UXM; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154.[ExPASy / RCSB / EBI]
2AF2; NMR; -; A/B=2-154.[ExPASy / RCSB / EBI]
2C9S; X-ray; 1.24 A; A/F=2-154.[ExPASy / RCSB / EBI]
2C9U; X-ray; 1.24 A; A/F=2-154.[ExPASy / RCSB / EBI]
2C9V; X-ray; 1.07 A; A/F=2-154.[ExPASy / RCSB / EBI]
2GBT; X-ray; 1.70 A; A/B/C/D=2-154.[ExPASy / RCSB / EBI]
2GBU; X-ray; 2.00 A; A/B/C/D=2-154.[ExPASy / RCSB / EBI]
2GBV; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=2-154.[ExPASy / RCSB / EBI]
2NNX; X-ray; 2.30 A; A/B/C/D=2-153.[ExPASy / RCSB / EBI]
2R27; X-ray; 2.00 A; A/B=1-154.[ExPASy / RCSB / EBI]
2V0A; X-ray; 1.15 A; A/F=2-154.[ExPASy / RCSB / EBI]
2VR6; X-ray; 1.30 A; A/F=2-154.[ExPASy / RCSB / EBI]
2VR7; X-ray; 1.58 A; A/F=2-154.[ExPASy / RCSB / EBI]
2VR8; X-ray; 1.36 A; A/F=2-154.[ExPASy / RCSB / EBI]
2ZKW; X-ray; 1.90 A; A/B=1-154.[ExPASy / RCSB / EBI]
2ZKX; X-ray; 2.72 A; A/B/C/D=1-154.[ExPASy / RCSB / EBI]
2ZKY; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-154.[ExPASy / RCSB / EBI]
3CQP; X-ray; 1.95 A; A/B/C/D=2-154.[ExPASy / RCSB / EBI]
3CQQ; X-ray; 1.90 A; A/B=2-154.[ExPASy / RCSB / EBI]
3GQF; X-ray; 2.20 A; A/B/C/D/E/F=2-154.[ExPASy / RCSB / EBI]
4SOD; Model; -; A=1-154.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AZV; -.
1BA9; -.
1DSW; -.
1FUN; -.
1HL4; -.
1HL5; -.
1KMG; -.
1L3N; -.
1MFM; -.
1N18; -.
1N19; -.
1OEZ; -.
1OZT; -.
1OZU; -.
1P1V; -.
1PTZ; -.
1PU0; -.
1RK7; -.
1SOS; -.
1SPD; -.
1UXL; -.
1UXM; -.
2AF2; -.
2C9S; -.
2C9U; -.
2C9V; -.
2GBT; -.
2GBU; -.
2GBV; -.
2NNX; -.
2R27; -.
2V0A; -.
2VR6; -.
2VR7; -.
2VR8; -.
2ZKW; -.
2ZKX; -.
2ZKY; -.
3CQP; -.
3CQQ; -.
3GQF; -.
4SOD; -.
ModBase P00441.
Protein-protein interaction databases
IntAct P00441; 3.
PTM databases
PhosphoSite P00441; -.
Enzyme and pathway databases
BRENDA 1.15.1.1; 247.
Pathway_Interaction_DB hnf3apathway; FOXA1 transcription factor network.
Reactome REACT_604; Hemostasis.
2D gel databases
SWISS-2DPAGE P00441; -.
Aarhus/Ghent-2DPAGE 4127; IEF.
DOSAC-COBS-2DPAGE P00441; -.
OGP P00441; -.
REPRODUCTION-2DPAGE IPI00783680; -.
Siena-2DPAGE P00441; -.
Organism-specific databases
GeneCards GC21P031953; -.
H-InvDB HIX0016056; -.
HGNC HGNC:11179; SOD1.
GenAtlas SOD1.
HPA CAB008670; -.
HPA001401; -.
MIM 105400; phenotype. [NCBI / EBI]
147450; gene. [NCBI / EBI]
Orphanet 803; Amyotrophic lateral sclerosis.
PharmGKB PA334; -.
Gene expression databases
ArrayExpress P00441; -.
Bgee P00441; -.
CleanEx HS_SOD1; -.
GermOnline ENSG00000142168; Homo sapiens.
Ontologies
GO
GO:0043025; Cellular component: cell soma (inferred from direct assay from UniProtKB).
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from direct assay from UniProtKB).
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0032839; Cellular component: dendrite cytoplasm (inferred from direct assay from UniProtKB).
GO:0031012; Cellular component: extracellular matrix (inferred from direct assay from UniProtKB).
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0005759; Cellular component: mitochondrial matrix (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005777; Cellular component: peroxisome (non-traceable author statement from UniProtKB).
GO:0043234; Cellular component: protein complex (inferred from direct assay from UniProtKB).
GO:0016209; Molecular function: antioxidant activity (inferred from electronic annotation from UniProtKB-KW).
GO:0051087; Molecular function: chaperone binding (inferred from physical interaction from UniProtKB).
GO:0005507; Molecular function: copper ion binding (inferred from direct assay from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (non-traceable author statement from UniProtKB).
GO:0030346; Molecular function: protein phosphatase 2B binding (inferred from direct assay from UniProtKB).
GO:0004784; Molecular function: superoxide dismutase activity (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0000187; Biological process: activation of MAPK activity (inferred from sequence or structural similarity from UniProtKB).
GO:0060088; Biological process: auditory receptor cell stereocilium organization (inferred from sequence or structural similarity from UniProtKB).
GO:0007569; Biological process: cell aging (inferred from mutant phenotype from UniProtKB).
GO:0006879; Biological process: cellular iron ion homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0006309; Biological process: DNA fragmentation involved in apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0006302; Biological process: double-strand break repair (inferred from sequence or structural similarity from UniProtKB).
GO:0007566; Biological process: embryo implantation (non-traceable author statement from UniProtKB).
GO:0006749; Biological process: glutathione metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0060047; Biological process: heart contraction (inferred from direct assay from UniProtKB).
GO:0050665; Biological process: hydrogen peroxide biosynthetic process (inferred from direct assay from UniProtKB).
GO:0007626; Biological process: locomotory behavior (inferred from sequence or structural similarity from UniProtKB).
GO:0046716; Biological process: muscle maintenance (inferred from sequence or structural similarity from UniProtKB).
GO:0032287; Biological process: myelin maintenance in the peripheral nervous system (inferred from sequence or structural similarity from UniProtKB).
GO:0002262; Biological process: myeloid cell homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0045541; Biological process: negative regulation of cholesterol biosynthetic process (inferred from direct assay from UniProtKB).
GO:0043524; Biological process: negative regulation of neuron apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0060052; Biological process: neurofilament cytoskeleton organization (inferred from sequence or structural similarity from UniProtKB).
GO:0001541; Biological process: ovarian follicle development (inferred from sequence or structural similarity from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0001890; Biological process: placenta development (non-traceable author statement from UniProtKB).
GO:0043065; Biological process: positive regulation of apoptosis (inferred by curator from UniProtKB).
GO:0001819; Biological process: positive regulation of cytokine production (inferred from direct assay from UniProtKB).
GO:0008217; Biological process: regulation of blood pressure (inferred from sequence or structural similarity from UniProtKB).
GO:0051881; Biological process: regulation of mitochondrial membrane potential (inferred from mutant phenotype from UniProtKB).
GO:0040014; Biological process: regulation of multicellular organism growth (inferred from sequence or structural similarity from UniProtKB).
GO:0046620; Biological process: regulation of organ growth (non-traceable author statement from UniProtKB).
GO:0033081; Biological process: regulation of T cell differentiation in the thymus (non-traceable author statement from UniProtKB).
GO:0060087; Biological process: relaxation of vascular smooth muscle (inferred from sequence or structural similarity from UniProtKB).
GO:0019430; Biological process: removal of superoxide radicals (inferred from sequence or structural similarity from UniProtKB).
GO:0048678; Biological process: response to axon injury (inferred from sequence or structural similarity from UniProtKB).
GO:0042493; Biological process: response to drug (inferred from sequence or structural similarity from UniProtKB).
GO:0045471; Biological process: response to ethanol (inferred from sequence or structural similarity from UniProtKB).
GO:0009408; Biological process: response to heat (inferred from sequence or structural similarity from UniProtKB).
GO:0042542; Biological process: response to hydrogen peroxide (inferred from sequence or structural similarity from UniProtKB).
GO:0000303; Biological process: response to superoxide (inferred from direct assay from UniProtKB).
GO:0001895; Biological process: retina homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0007605; Biological process: sensory perception of sound (inferred from sequence or structural similarity from UniProtKB).
GO:0007283; Biological process: spermatogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0048538; Biological process: thymus development (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR018152; SOD_Cu/Zn_BS.
IPR001424; SOD_Cu_Zn.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.200; SOD_Cu_Zn; 1.
PANTHER PTHR10003; SOD_Cu_Zn; 1.
Pfam PF00080; Sod_Cu; 1.
Pfam graphical view of domain structure.
PRINTS PR00068; CUZNDISMTASE.
ProDom PD000469; SOD_CU_ZN; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00087; SOD_CU_ZN_1; 1.
PS00332; SOD_CU_ZN_2; 1.
Proteomic databases
PeptideAtlas P00441; -.
PRIDE P00441; -.
Genome annotation databases
Ensembl ENSG00000142168; Homo sapiens. [Contig view]
GeneID 6647; -.
KEGG hsa:6647; -.
Phylogenomic databases
HOVERGEN P00441; -.
OMA P00441; KAVCVIN.
Other
NextBio 25903; -.
SOURCE SOD1; Homo sapiens.
ProtoNet P00441.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Amyotrophic lateral sclerosis; Antioxidant; Copper; Cytoplasm; Direct protein sequencing; Disease mutation; Disulfide bond; Metal-binding; Neurodegeneration; Oxidoreductase; Phosphoprotein; Ubl conjugation; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   154  153     Superoxide dismutase [Cu-Zn]. PRO_0000164057
METAL   47    47        Copper; catalytic. 
METAL   49    49        Copper; catalytic. 
METAL   64    64        Copper; catalytic. 
METAL   64    64        Zinc; structural. 
METAL   72    72        Zinc; structural. 
METAL   81    81        Zinc; structural. 
METAL   84    84        Zinc; structural. 
METAL   121   121        Copper; catalytic. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   71    71        N6-acetyllysine (By similarity). 
MOD_RES   99    99        Phosphoserine. 
DISULFID   58   147         
VARIANT   5     5  1     A -> S (in ALS1). VAR_013518 [3D]
VARIANT   5     5  1     A -> T (in ALS1). VAR_007130 [3D]
VARIANT   5     5  1     A -> V (in ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggegates). VAR_007131 [3D]
VARIANT   7     7  1     C -> F (in ALS1). VAR_008717 [3D]
VARIANT   8     8  1     V -> E (in ALS1). VAR_007132 [3D]
VARIANT   9     9  1     L -> Q (in ALS1). VAR_013519 [3D]
VARIANT   9     9  1     L -> V (in ALS1). VAR_013520 [3D]
VARIANT   13    13  1     G -> R (in ALS1). VAR_013521 [3D]
VARIANT   15    15  1     V -> G (in ALS1). VAR_013522 [3D]
VARIANT   15    15  1     V -> M (in ALS1). VAR_007133 [3D]
VARIANT   17    17  1     G -> S (in ALS1; sporadic young onset). VAR_007134 [3D]
VARIANT   21    21  1     F -> C (in ALS1). VAR_045876 [3D]
VARIANT   22    22  1     E -> G (in ALS1). VAR_013523 [3D]
VARIANT   22    22  1     E -> K (in ALS1). VAR_007135 [3D]
VARIANT   23    23  1     Q -> L (in ALS1). VAR_045877 [3D]
VARIANT   38    38  1     G -> R (in ALS1; mild form; ubiquitinated by RNF19A). VAR_007136 [3D]
VARIANT   39    39  1     L -> R (in ALS1). VAR_013524 [3D]
VARIANT   39    39  1     L -> V (in ALS1). VAR_007137 [3D]
VARIANT   42    42  1     G -> D (in ALS1). VAR_007139 [3D]
VARIANT   42    42  1     G -> S (in ALS1). VAR_007138 [3D]
VARIANT   44    44  1     H -> R (in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggegates). VAR_007140 [3D]
VARIANT   46    46  1     F -> C (in ALS1; slow progression). VAR_013525 [3D]
VARIANT   47    47  1     H -> R (in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A). VAR_007141 [3D]
VARIANT   49    49  1     H -> Q (in ALS1). VAR_007142 [3D]
VARIANT   49    49  1     H -> R (in ALS1). VAR_045878 [3D]
VARIANT   50    50  1     E -> K (in ALS1). VAR_013526 [3D]
VARIANT   55    55  1     T -> R (in ALS1; reduces tendency to form fibrillar aggregates). VAR_045879 [3D]
VARIANT   66    66  1     N -> S (in ALS1). VAR_013527 [3D]
VARIANT   68    68  1     L -> R (in ALS1). VAR_013528 [3D]
VARIANT   73    73  1     G -> S (in ALS1). VAR_008718 [3D]
VARIANT   77    77  1     D -> Y (in ALS1). VAR_013529 [3D]
VARIANT   81    81  1     H -> A (in ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions). VAR_016874 [3D]
VARIANT   85    85  1     L -> F (in ALS1). VAR_013530 [3D]
VARIANT   85    85  1     L -> V (in ALS1). VAR_007143 [3D]
VARIANT   86    86  1     G -> R (in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding). VAR_007144 [3D]
VARIANT   87    87  1     N -> S (in ALS1). VAR_013531 [3D]
VARIANT   88    88  1     V -> A (in ALS1). VAR_045880 [3D]
VARIANT   90    90  1     A -> T (in ALS1). VAR_045881 [3D]
VARIANT   90    90  1     A -> V (in ALS1). VAR_013532 [3D]
VARIANT   91    91  1     D -> A (in ALS1; does not seem to be linked with a decrease in activity). VAR_007145 [3D]
VARIANT   91    91  1     D -> V (in ALS1). VAR_013533 [3D]
VARIANT   94    94  1     G -> A (in ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A). VAR_007146 [3D]
VARIANT   94    94  1     G -> C (in ALS1). VAR_007147 [3D]
VARIANT   94    94  1     G -> D (in ALS1). VAR_007148 [3D]
VARIANT   94    94  1     G -> R (in ALS1; 30% of wild-type activity). VAR_007149 [3D]
VARIANT   94    94  1     G -> V (in ALS1). VAR_008719 [3D]
VARIANT   98    98  1     V -> M (in ALS1; increases tendency to form fibrillar aggregates). VAR_045882 [3D]
VARIANT   101   101  1     E -> G (in ALS1). VAR_007150 [3D]
VARIANT   101   101  1     E -> K (in ALS1). VAR_013534 [3D]
VARIANT   102   102  1     D -> G (in ALS1). VAR_007151 [3D]
VARIANT   102   102  1     D -> N (in ALS1). VAR_007152 [3D]
VARIANT   105   105  1     I -> F (in ALS1). VAR_008720 [3D]
VARIANT   106   106  1     S -> L (in ALS1). VAR_013535 [3D]
VARIANT   107   107  1     L -> V (in ALS1). VAR_007153 [3D]
VARIANT   109   109  1     G -> V (in ALS1). VAR_013536 [3D]
VARIANT   113   113  1     I -> M (in ALS1). VAR_013537 [3D]
VARIANT   113   113  1     I -> T (in ALS1). VAR_007154 [3D]
VARIANT   114   114  1     I -> T (in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates). VAR_007155 [3D]
VARIANT   115   115  1     G -> A (in ALS1). VAR_013538 [3D]
VARIANT   116   116  1     R -> G (in ALS1). VAR_007156 [3D]
VARIANT   119   119  1     V -> L (in ALS1). VAR_045883 [3D]
VARIANT   119   119  1     V -> VFLQ (in ALS1). VAR_008721
VARIANT   125   125  1     D -> G (in ALS1). VAR_045884 [3D]
VARIANT   125   125  1     D -> V (in ALS1). VAR_008722 [3D]
VARIANT   126   126  1     D -> H (in ALS1). VAR_007157 [3D]
VARIANT   127   127  1     L -> S (in ALS1). VAR_013539 [3D]
VARIANT   134   134  1     Missing (in ALS). VAR_008723
VARIANT   135   135  1     S -> N (in ALS1; reduced metal binding; increases tendency to form fibrillar aggegates). VAR_007158 [3D]
VARIANT   140   140  1     N -> K (in ALS1). VAR_007159 [3D]
VARIANT   145   145  1     L -> F (in ALS1). VAR_007160 [3D]
VARIANT   145   145  1     L -> S (in ALS1). VAR_008724 [3D]
VARIANT   146   146  1     A -> T (in ALS1). VAR_008725 [3D]
VARIANT   147   147  1     C -> R (in ALS1). VAR_013540 [3D]
VARIANT   148   148  1     G -> R (in ALS1). VAR_045885 [3D]
VARIANT   149   149  1     V -> G (in ALS1). VAR_007161 [3D]
VARIANT   149   149  1     V -> I (in ALS1). VAR_007162 [3D]
VARIANT   150   150  1     I -> T (in ALS1). VAR_007163 [3D]
VARIANT   152   152  1     I -> T (in ALS1; seems to affect formation of homodimer). VAR_007164 [3D]
MUTAGEN   7     7        C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147. 
MUTAGEN   51    52        FG->EE: Abolishes dimerization; when associated with Q-134. 
MUTAGEN   58    58        C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147. 
MUTAGEN   81    81        H->A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84. 
MUTAGEN   81    81        H->S: Destabilization of dimer and loss of zinc binding; when associated with S-84. 
MUTAGEN   84    84        D->A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81. 
MUTAGEN   84    84        D->S: Destabilization of dimer and loss of zinc binding; when associated with S-81. 
MUTAGEN   112   112        C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147. 
MUTAGEN   134   134        E->Q: Abolishes dimerization; when associated with E-50 and E-51. 
MUTAGEN   147   147        C->S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112. 
CONFLICT   18    18        I -> S (in Ref. 3). 
CONFLICT   99    99        S -> V (in Ref. 3). 
STRAND   3    10  8      
STRAND   12    14  3      
STRAND   16    25  10      
STRAND   30    38  9      
STRAND   41    50  10      
HELIX   57    59  3      
STRAND   77    79  3      
STRAND   84    90  7      
STRAND   96   104  9      
STRAND   107   109  3      
STRAND   116   123  8      
STRAND   130   132  3      
HELIX   135   138  4      
STRAND   143   149  7      
Sequence information
Length: 154 AA [This is the length of the unprocessed precursor] Molecular weight: 15936 Da [This is the MW of the unprocessed precursor] CRC64: 25CA38DA8D564483 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS 

        70         80         90        100        110        120 
AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV 

       130        140        150 
HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ
P00441 in FASTA format

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