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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: SODC_HUMAN V9HWC9_HUMAN
LinkDB: SODC_HUMAN V9HWC9_HUMAN
Original site: SODC_HUMAN V9HWC9_HUMAN 
ID   SODC_HUMAN              Reviewed;         154 AA.
AC   P00441; A6NHJ0; D3DSE4; Q16669; Q16711; Q16838; Q16839; Q16840;
AC   Q6NR85;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-SEP-2017, entry version 226.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
DE   AltName: Full=Superoxide dismutase 1;
DE            Short=hSod1;
GN   Name=SOD1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6577438; DOI=10.1073/pnas.80.18.5465;
RA   Sherman L., Dafni N., Lieman-Hurwitz J., Groner Y.;
RT   "Nucleotide sequence and expression of human chromosome 21-encoded
RT   superoxide dismutase mRNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:5465-5469(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3160582;
RA   Levanon D., Lieman-Hurwitz J., Dafni N., Wigderson M., Sherman L.,
RA   Bernstein Y., Laver-Rudich Z., Danciger E., Stein O., Groner Y.;
RT   "Architecture and anatomy of the chromosomal locus in human chromosome
RT   21 encoding the Cu/Zn superoxide dismutase.";
RL   EMBO J. 4:77-84(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3889846; DOI=10.1093/nar/13.6.2017;
RA   Hallewell R.A., Masiarz F.R., Najarian R.C., Puma J.P., Quiroga M.R.,
RA   Randolph A., Sanchez-Pescador R., Scandella C.J., Smith B.,
RA   Steimer K.S., Mullenbach G.T.;
RT   "Human Cu/Zn superoxide dismutase cDNA: isolation of clones
RT   synthesising high levels of active or inactive enzyme from an
RT   expression library.";
RL   Nucleic Acids Res. 13:2017-2034(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2853161; DOI=10.1093/oxfordjournals.jbchem.a122562;
RA   Kajihara J., Enomoto M., Nishijima K., Yabuuchi M., Katoh K.;
RT   "Comparison of properties between human recombinant and placental
RT   copper-zinc SOD.";
RL   J. Biochem. 104:851-854(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Xu Y., Hu X., Zhou Y., Peng X., Yuan J., Qiang B.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lu X., Hui L.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Staege M.S., Bergmann S., Heins S.;
RT   "Direct sequencing and cloning of superoxide dismutase 1 from
RT   peripheral blood.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA   Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA   Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA   Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA   Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA   Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA   Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA   Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA   Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA   Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA   Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA   Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [16]
RP   PROTEIN SEQUENCE OF 2-154.
RX   PubMed=6770891; DOI=10.1021/bi00552a005;
RA   Jabusch J.R., Farb D.L., Kerschensteiner D.A., Deutsch H.F.;
RT   "Some sulfhydryl properties and primary structure of human erythrocyte
RT   superoxide dismutase.";
RL   Biochemistry 19:2310-2316(1980).
RN   [17]
RP   PROTEIN SEQUENCE OF 2-154, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   ACETYLATION AT ALA-2.
RX   PubMed=7002610; DOI=10.1016/0014-5793(80)81044-1;
RA   Barra D., Martini F., Bannister J.V., Schinina M.E., Rotilio G.,
RA   Bannister W.H., Bossa F.;
RT   "The complete amino acid sequence of human Cu/Zn superoxide
RT   dismutase.";
RL   FEBS Lett. 120:53-56(1980).
RN   [18]
RP   PROTEIN SEQUENCE OF 11-24 AND 81-116.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [19]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-56 AND 120-154, AND VARIANTS
RP   ALS1 GLN-49; ARG-94; THR-113; THR-114; HIS-126 AND THR-150.
RX   PubMed=8528216; DOI=10.1093/hmg/4.7.1239;
RA   Enayat Z.E., Orrell R.W., Claus A., Ludolph A., Bachus R.,
RA   Brockmueller J., Ray-Chaudhuri K., Radunovic A., Shaw C.,
RA   Wilkinson J., King A., Swash M., Leigh P.N., de Belleroche J.,
RA   Powell J.;
RT   "Two novel mutations in the gene for copper zinc superoxide dismutase
RT   in UK families with amyotrophic lateral sclerosis.";
RL   Hum. Mol. Genet. 4:1239-1240(1995).
RN   [20]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-154, AND VARIANT ALS1
RP   THR-152.
RX   PubMed=8682505; DOI=10.1007/s004390050157;
RA   Kostrzewa M., Daamian M., Mueller U.;
RT   "Superoxide dismutase 1: identification of a novel mutation in a case
RT   of familial amyotrophic lateral sclerosis.";
RL   Hum. Genet. 98:48-50(1996).
RN   [21]
RP   SUBUNIT, AND DISULFIDE BOND.
RX   PubMed=15326189; DOI=10.1074/jbc.M406021200;
RA   Arnesano F., Banci L., Bertini I., Martinelli M., Furukawa Y.,
RA   O'Halloran T.V.;
RT   "The unusually stable quaternary structure of human Cu,Zn-superoxide
RT   dismutase 1 is controlled by both metal occupancy and disulfide
RT   status.";
RL   J. Biol. Chem. 279:47998-48003(2004).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [23]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [24]
RP   SUBUNIT, AND DITRYPTOPHAN CROSS-LINK AT TRP-33.
RX   PubMed=20600836; DOI=10.1016/j.freeradbiomed.2010.06.018;
RA   Medinas D.B., Gozzo F.C., Santos L.F., Iglesias A.H., Augusto O.;
RT   "A ditryptophan cross-link is responsible for the covalent
RT   dimerization of human superoxide dismutase 1 during its bicarbonate-
RT   dependent peroxidase activity.";
RL   Free Radic. Biol. Med. 49:1046-1053(2010).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [26]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [27]
RP   PALMITOYLATION AT CYS-7, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   CYS-7.
RX   PubMed=22496122; DOI=10.1161/CIRCRESAHA.112.269514;
RA   Marin E.P., Derakhshan B., Lam T.T., Davalos A., Sessa W.C.;
RT   "Endothelial cell palmitoylproteomic identifies novel lipid-modified
RT   targets and potential substrates for protein acyl transferases.";
RL   Circ. Res. 110:1336-1344(2012).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22905912; DOI=10.1021/pr300539b;
RA   Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
RA   Fischer-Posovszky P., Mariman E.C., Renes J.;
RT   "Resveratrol-induced changes of the human adipocyte secretion
RT   profile.";
RL   J. Proteome Res. 11:4733-4743(2012).
RN   [29]
RP   SUCCINYLATION AT LYS-123, DESUCCINYLATION BY SIRT5, AND MUTAGENESIS OF
RP   LYS-123.
RX   PubMed=24140062; DOI=10.1016/j.bbrc.2013.10.033;
RA   Lin Z.F., Xu H.B., Wang J.Y., Lin Q., Ruan Z., Liu F.B., Jin W.,
RA   Huang H.H., Chen X.;
RT   "SIRT5 desuccinylates and activates SOD1 to eliminate ROS.";
RL   Biochem. Biophys. Res. Commun. 441:191-195(2013).
RN   [30]
RP   MUTAGENESIS OF CYS-58 AND CYS-147.
RX   PubMed=23625804; DOI=10.1002/cbic.201300042;
RA   Banci L., Cantini F., Kozyreva T., Rubino J.T.;
RT   "Mechanistic aspects of hSOD1 maturation from the solution structure
RT   of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1
RT   mutants.";
RL   ChemBioChem 14:1839-1844(2013).
RN   [31]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-103, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [32]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=1463506; DOI=10.1073/pnas.89.13.6109;
RA   Parge H.E., Hallewell R.A., Tainer J.A.;
RT   "Atomic structures of wild-type and thermostable mutant recombinant
RT   human Cu,Zn superoxide dismutase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6109-6113(1992).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ALS1 ARG-38.
RX   PubMed=9541385; DOI=10.1002/pro.5560070302;
RA   Hart P.J., Liu H., Pellegrini M., Nersissian A.M., Gralla E.B.,
RA   Valentine J.S., Eisenberg D.;
RT   "Subunit asymmetry in the three-dimensional structure of a human
RT   CuZnSOD mutant found in familial amyotrophic lateral sclerosis.";
RL   Protein Sci. 7:545-555(1998).
RN   [35]
RP   STRUCTURE BY NMR.
RX   PubMed=9718300; DOI=10.1021/bi9803473;
RA   Banci L., Benedetto M., Bertini I., del Conte R., Piccioli M.,
RA   Viezzoli M.S.;
RT   "Solution structure of reduced monomeric Q133M2 copper, zinc
RT   superoxide dismutase (SOD). Why is SOD a dimeric enzyme?";
RL   Biochemistry 37:11780-11791(1998).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF MUTANT
RP   GLU-51/GLU-52/GLN-134, SUBUNIT, AND MUTAGENESIS OF 51-PHE-GLY-52 AND
RP   GLU-134.
RX   PubMed=10329151; DOI=10.1006/jmbi.1999.2681;
RA   Ferraroni M., Rypniewski W., Wilson K.S., Viezzoli M.S., Banci L.,
RA   Bertini I., Mangani S.;
RT   "The crystal structure of the monomeric human SOD mutant
RT   F50E/G51E/E133Q at atomic resolution. The enzyme mechanism
RT   revisited.";
RL   J. Mol. Biol. 288:413-426(1999).
RN   [37]
RP   STRUCTURE BY NMR OF MUTANT GLU51/GLU-52/GLN-134, AND SUBUNIT.
RX   PubMed=12911296; DOI=10.1021/bi034324m;
RA   Banci L., Bertini I., Cramaro F., Del Conte R., Viezzoli M.S.;
RT   "Solution structure of Apo Cu,Zn superoxide dismutase: role of metal
RT   ions in protein folding.";
RL   Biochemistry 42:9543-9553(2003).
RN   [38]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC
RP   IONS, DISULFIDE BOND, SUBUNIT, AND CHARACTERIZATION OF VARIANTS ALS1
RP   VAL-5 AND ARG-44.
RX   PubMed=12963370; DOI=10.1016/S0022-2836(03)00889-1;
RA   DiDonato M., Craig L., Huff M.E., Thayer M.M., Cardoso R.M.,
RA   Kassmann C.J., Lo T.P., Bruns C.K., Powers E.T., Kelly J.W.,
RA   Getzoff E.D., Tainer J.A.;
RT   "ALS mutants of human superoxide dismutase form fibrous aggregates via
RT   framework destabilization.";
RL   J. Mol. Biol. 332:601-615(2003).
RN   [39]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANTS ALS1 ASN-135 AND
RP   ARG-47, AND FORMATION OF FIBRILLAR AGGREGATES.
RX   PubMed=12754496; DOI=10.1038/nsb935;
RA   Elam J.S., Taylor A.B., Strange R., Antonyuk S., Doucette P.A.,
RA   Rodriguez J.A., Hasnain S.S., Hayward L.J., Valentine J.S.,
RA   Yeates T.O., Hart P.J.;
RT   "Amyloid-like filaments and water-filled nanotubes formed by SOD1
RT   mutant proteins linked to familial ALS.";
RL   Nat. Struct. Biol. 10:461-467(2003).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF VARIANTS ALS1 VAL-5 AND
RP   THR-114, AND CHARACTERIZATION OF VARIANTS ALS1 VAL-5 AND THR-114.
RX   PubMed=15056757; DOI=10.1073/pnas.0305143101;
RA   Hough M.A., Grossmann J.G., Antonyuk S.V., Strange R.W.,
RA   Doucette P.A., Rodriguez J.A., Whitson L.J., Hart P.J., Hayward L.J.,
RA   Valentine J.S., Hasnain S.S.;
RT   "Dimer destabilization in superoxide dismutase may result in disease-
RT   causing properties: structures of motor neuron disease mutants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5976-5981(2004).
RN   [41]
RP   STRUCTURE BY NMR OF MUTANT ALA-7/SER-112, AND SUBUNIT.
RX   PubMed=16291742; DOI=10.1074/jbc.M506497200;
RA   Banci L., Bertini I., Cantini F., D'Amelio N., Gaggelli E.;
RT   "Human SOD1 before harboring the catalytic metal: solution structure
RT   of copper-depleted, disulfide-reduced form.";
RL   J. Biol. Chem. 281:2333-2337(2006).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEXES WITH COPPER AND
RP   ZINC IONS, DISULFIDE BOND, AND SUBUNIT.
RX   PubMed=16406071; DOI=10.1016/j.jmb.2005.11.081;
RA   Strange R.W., Antonyuk S.V., Hough M.A., Doucette P.A.,
RA   Valentine J.S., Hasnain S.S.;
RT   "Variable metallation of human superoxide dismutase: atomic resolution
RT   crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type
RT   enzymes.";
RL   J. Mol. Biol. 356:1152-1162(2006).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ALA-7/ALA-112 AND
RP   ALA-7/ALA-58/ALA-112/ALA-147, AND MUTAGENESIS OF CYS-7; CYS-58;
RP   CYS-112 AND CYS-147.
RX   PubMed=17070542; DOI=10.1016/j.jmb.2006.09.048;
RA   Hoernberg A., Logan D.T., Marklund S.L., Oliveberg M.;
RT   "The coupling between disulphide status, metallation and dimer
RT   interface strength in Cu/Zn superoxide dismutase.";
RL   J. Mol. Biol. 365:333-342(2007).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT SER-81/SER-84 IN
RP   COMPLEX WITH COPPER IONS, SUBUNIT, MUTAGENESIS OF HIS-81 AND ASP-84,
RP   AND COFACTOR.
RX   PubMed=17888947; DOI=10.1016/j.jmb.2007.07.043;
RA   Roberts B.R., Tainer J.A., Getzoff E.D., Malencik D.A., Anderson S.R.,
RA   Bomben V.C., Meyers K.R., Karplus P.A., Beckman J.S.;
RT   "Structural characterization of zinc-deficient human superoxide
RT   dismutase and implications for ALS.";
RL   J. Mol. Biol. 373:877-890(2007).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC
RP   IONS, SUBUNIT, AND FORMATION OF FIBRILLAR AGGREGATES BY ZINC-DEPLETED
RP   SOD1.
RX   PubMed=17548825; DOI=10.1073/pnas.0703857104;
RA   Strange R.W., Yong C.W., Smith W., Hasnain S.S.;
RT   "Molecular dynamics using atomic-resolution structure reveal
RT   structural fluctuations that may lead to polymerization of human Cu-Zn
RT   superoxide dismutase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10040-10044(2007).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANT ALS1 ARG-86, AND
RP   CHARACTERIZATION OF VARIANT ALS1 ARG-86.
RX   PubMed=18378676; DOI=10.1074/jbc.M801522200;
RA   Cao X., Antonyuk S.V., Seetharaman S.V., Whitson L.J., Taylor A.B.,
RA   Holloway S.P., Strange R.W., Doucette P.A., Valentine J.S., Tiwari A.,
RA   Hayward L.J., Padua S., Cohlberg J.A., Hasnain S.S., Hart P.J.;
RT   "Structures of the G85R variant of SOD1 in familial amyotrophic
RT   lateral sclerosis.";
RL   J. Biol. Chem. 283:16169-16177(2008).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ALS1 ARG-86.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of human Cu-Zn superoxide dismutase mutant G85R
RT   (P21).";
RL   Submitted (APR-2008) to the PDB data bank.
RN   [48]
RP   REVIEW ON VARIANTS.
RX   PubMed=8592323; DOI=10.1136/jmg.32.11.841;
RA   de Belleroche J., Orrell R., King A.;
RT   "Familial amyotrophic lateral sclerosis/motor neurone disease (FALS):
RT   a review of current developments.";
RL   J. Med. Genet. 32:841-847(1995).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
RX   PubMed=20727846; DOI=10.1016/j.abb.2010.08.014;
RA   Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J.;
RT   "Structures of mouse SOD1 and human/mouse SOD1 chimeras.";
RL   Arch. Biochem. Biophys. 503:183-190(2010).
RN   [50]
RP   VARIANTS ALS1.
RX   PubMed=8446170; DOI=10.1038/362059a0;
RA   Rosen D.R., Siddique T., Patterson D., Figlewicz D.A., Sapp P.,
RA   Hentati A., Donaldson D., Goto J., O'Regan J.P., Deng H.-X.,
RA   Rahmani Z., Krizus A., McKenna-Yasek D., Cayabyab A., Gaston S.M.,
RA   Berger R., Tanzi R.E., Halperin J.J., Herzfeldt B., van den Bergh R.,
RA   Hung W.-Y., Bird T., Deng G., Mulder D.W., Smyth C., Laing N.G.,
RA   Soriano E., Pericak-Vance M.A., Haines J., Rouleau G.A., Gusella J.S.,
RA   Horvitz H.R., Brown R.H. Jr.;
RT   "Mutations in Cu/Zn superoxide dismutase gene are associated with
RT   familial amyotrophic lateral sclerosis.";
RL   Nature 362:59-62(1993).
RN   [51]
RP   ERRATUM.
RX   PubMed=8332197;
RA   Rosen D.R.;
RL   Nature 364:362-362(1993).
RN   [52]
RP   VARIANTS ALS1.
RX   PubMed=8351519; DOI=10.1126/science.8351519;
RA   Deng H.-X., Hentati A., Tainer J.A., Iqbal Z., Cayabyab A.,
RA   Hung W.-Y., Getzoff E.D., Hu P., Herzfeldt B., Roos R.P., Warner C.,
RA   Deng G., Soriano E., Smyth C., Parge H.E., Ahmed A., Roses A.D.,
RA   Hallewell R.A., Pericak-Vance M.A., Siddique T.;
RT   "Amyotrophic lateral sclerosis and structural defects in Cu,Zn
RT   superoxide dismutase.";
RL   Science 261:1047-1051(1993).
RN   [53]
RP   VARIANT ALS1 THR-5.
RX   PubMed=8179602; DOI=10.1006/bbrc.1994.1506;
RA   Nakano R., Sato S., Inuzuka T., Sakimura K., Mishina M., Takahashi H.,
RA   Ikuta F., Honma Y., Fujii J., Taniguchi N., Tsuji S.;
RT   "A novel mutation in Cu/Zn superoxide dismutase gene in Japanese
RT   familial amyotrophic lateral sclerosis.";
RL   Biochem. Biophys. Res. Commun. 200:695-703(1994).
RN   [54]
RP   VARIANT ALS1 GLU-8.
RX   PubMed=7980516; DOI=10.1006/bbrc.1994.2497;
RA   Hirano M., Fujii J., Nagai Y., Sonobe M., Okamoto K., Araki H.,
RA   Taniguchi N., Ueno S.;
RT   "A new variant Cu/Zn superoxide dismutase (Val7-->Glu) deduced from
RT   lymphocyte mRNA sequences from Japanese patients with familial
RT   amyotrophic lateral sclerosis.";
RL   Biochem. Biophys. Res. Commun. 204:572-577(1994).
RN   [55]
RP   VARIANT ALS1 LYS-22.
RX   PubMed=8069312; DOI=10.1093/hmg/3.4.649;
RA   Jones C.T., Swinger R.J., Brock D.J.H.;
RT   "Identification of a novel SOD1 mutation in an apparently sporadic
RT   amyotrophic lateral sclerosis patient and the detection of Ile113Thr
RT   in three others.";
RL   Hum. Mol. Genet. 3:649-650(1994).
RN   [56]
RP   VARIANTS ALS1 ASP-94 AND THR-113.
RX   PubMed=7951252; DOI=10.1093/hmg/3.6.997;
RA   Esteban J., Rosen D.R., Bowling A.C., Sapp P., McKenna-Yasek D.,
RA   O'Regan J.P., Beal M.F., Horvitz H.R., Brown R.H. Jr.;
RT   "Identification of two novel mutations and a new polymorphism in the
RT   gene for Cu/Zn superoxide dismutase in patients with amyotrophic
RT   lateral sclerosis.";
RL   Hum. Mol. Genet. 3:997-998(1994).
RN   [57]
RP   VARIANT ALS1 GLY-116.
RX   PubMed=7881433; DOI=10.1093/hmg/3.12.2261;
RA   Kostrzewa M., Burck-Lehmann U., Mueller U.;
RT   "Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in
RT   the Cu/Zn superoxide dismutase-1 gene.";
RL   Hum. Mol. Genet. 3:2261-2262(1994).
RN   [58]
RP   VARIANT ALS1 ARG-47.
RX   PubMed=7836951; DOI=10.1016/0022-510X(94)90097-3;
RA   Aoki M., Ogasawara M., Matsubara Y., Narisawa K., Nakamura S.,
RA   Itoyama Y., Abe K.;
RT   "Familial amyotrophic lateral sclerosis (ALS) in Japan associated with
RT   H46R mutation in Cu/Zn superoxide dismutase gene: a possible new
RT   subtype of familial ALS.";
RL   J. Neurol. Sci. 126:77-83(1994).
RN   [59]
RP   VARIANT ALS1 THR-114.
RX   PubMed=7997024; DOI=10.1016/S0140-6736(94)92913-0;
RA   Suthers G., Laing N., Wilton S., Dorosz S., Waddy H.;
RT   "'Sporadic' motoneuron disease due to familial SOD1 mutation with low
RT   penetrance.";
RL   Lancet 344:1773-1773(1994).
RN   [60]
RP   VARIANT ALS1 ASN-102.
RX   PubMed=7870076; DOI=10.1006/mcpr.1994.1046;
RA   Jones C.T., Shaw P.J., Chari G., Brock D.J.;
RT   "Identification of a novel exon 4 SOD1 mutation in a sporadic
RT   amyotrophic lateral sclerosis patient.";
RL   Mol. Cell. Probes 8:329-330(1994).
RN   [61]
RP   VARIANTS ALS1.
RX   PubMed=7887412;
RA   Pramatarova A., Figlewicz D.A., Krizus A., Han F.Y.,
RA   Ceballos-Picot I., Nicole A., Dib M., Meininger V., Brown R.H. Jr.,
RA   Rouleau G.A.;
RT   "Identification of new mutations in the Cu/Zn superoxide dismutase
RT   gene of patients with familial amyotrophic lateral sclerosis.";
RL   Am. J. Hum. Genet. 56:592-596(1995).
RN   [62]
RP   VARIANT ALS1 ILE-149.
RX   PubMed=7795609; DOI=10.1093/hmg/4.3.491;
RA   Ikeda M., Abe K., Aoki M., Ogasawara M., Kameya T., Watanabe M.,
RA   Shoji M., Hirai S., Itoyama Y.;
RT   "A novel point mutation in the Cu/Zn superoxide dismutase gene in a
RT   patient with familial amyotrophic lateral sclerosis.";
RL   Hum. Mol. Genet. 4:491-492(1995).
RN   [63]
RP   VARIANT ALS1 GLY-102.
RX   PubMed=7655468; DOI=10.1093/hmg/4.6.1101;
RA   Yulug I.G., Katsanis N., de Belleroche J., Collinge J., Fisher E.M.C.;
RT   "An improved protocol for the analysis of SOD1 gene mutations, and a
RT   new mutation in exon 4.";
RL   Hum. Mol. Genet. 4:1101-1104(1995).
RN   [64]
RP   VARIANT ALS1 ALA-91.
RX   PubMed=7655469; DOI=10.1093/hmg/4.6.1105;
RA   Sjaelander A., Beckman G., Deng H.-X., Iqbal Z., Tainer J.A.,
RA   Siddique T.;
RT   "The D90A mutation results in a polymorphism of Cu,Zn superoxide
RT   dismutase that is prevalent in northern Sweden and Finland.";
RL   Hum. Mol. Genet. 4:1105-1108(1995).
RN   [65]
RP   VARIANTS ALS1 MET-15 AND VAL-85.
RX   PubMed=7655471; DOI=10.1093/hmg/4.6.1113;
RA   Deng H.-X., Tainer J.A., Mitsumoto H., Ohnishi A., He X., Hung W.-Y.,
RA   Zhao Y., Juneja T., Hentati A., Siddique T.;
RT   "Two novel SOD1 mutations in patients with familial amyotrophic
RT   lateral sclerosis.";
RL   Hum. Mol. Genet. 4:1113-1116(1995).
RN   [66]
RP   VARIANT ALS1 ARG-94.
RX   PubMed=7700376; DOI=10.1038/374504a0;
RA   Orrell R., de Belleroche J., Marklund S., Bowe F., Hallewell R.;
RT   "A novel SOD mutant and ALS.";
RL   Nature 374:504-505(1995).
RN   [67]
RP   VARIANT ALS1 ALA-91.
RX   PubMed=7647793; DOI=10.1038/ng0595-61;
RA   Andersen P.M., Nilsson P., Ala-Hurula V., Keraenen M.-L.,
RA   Tarvainen I., Haltia T., Nilsson L., Binzer M., Forsgren L.,
RA   Marklund S.L.;
RT   "Amyotrophic lateral sclerosis associated with homozygosity for an
RT   Asp90Ala mutation in CuZn-superoxide dismutase.";
RL   Nat. Genet. 10:61-66(1995).
RN   [68]
RP   VARIANT ALS1 PHE-105.
RX   PubMed=7501156; DOI=10.1212/WNL.45.11.2038;
RA   Ikeda M., Abe K., Aoki M., Sahara M., Watanabe M., Shoji M.,
RA   St George-Hyslop P.H., Hirai S., Itoyama Y.;
RT   "Variable clinical symptoms in familial amyotrophic lateral sclerosis
RT   with a novel point mutation in the Cu/Zn superoxide dismutase gene.";
RL   Neurology 45:2038-2042(1995).
RN   [69]
RP   VARIANTS ALS1 SER-145; THR-146 AND PHE-LEU-GLN-119 INS.
RX   PubMed=7496169; DOI=10.1016/0960-8966(95)00007-A;
RA   Sapp P.C., Rosen D.R., Hosler B.A., Esteban J., McKenna-Yasek D.,
RA   O'Regan J.P., Horvitz H.R., Brown R.H. Jr.;
RT   "Identification of three novel mutations in the gene for Cu/Zn
RT   superoxide dismutase in patients with familial amyotrophic lateral
RT   sclerosis.";
RL   Neuromuscul. Disord. 5:353-357(1995).
RN   [70]
RP   VARIANTS ALS1 VAL-94; VAL-125 AND GLU-134 DEL.
RX   PubMed=8938700; DOI=10.1016/0960-8966(96)00353-7;
RA   Hosler B.A., Nicholson G.A., Sapp P.C., Chin W., Orrell R.W.,
RA   de Belleroche J.S., Esteban J., Hayward L.J., Mckenna-Yasek D.,
RA   Yeung L., Cherryson A.K., Dench J.E., Wilton S.D., Laing N.G.,
RA   Horvitz R.H., Brown R.H. Jr.;
RT   "Three novel mutations and two variants in the gene for Cu/Zn
RT   superoxide dismutase in familial amyotrophic lateral sclerosis.";
RL   Neuromuscul. Disord. 6:361-366(1996).
RN   [71]
RP   VARIANT ALS1 PHE-7.
RX   PubMed=8907321; DOI=10.1016/0304-3940(96)12378-8;
RA   Morita M., Aoki M., Abe K., Hasegawa T., Sakuma R., Onodera Y.,
RA   Ichikawa N., Nishizawa M., Itoyama Y.;
RT   "A novel two-base mutation in the Cu/Zn superoxide dismutase gene
RT   associated with familial amyotrophic lateral sclerosis in Japan.";
RL   Neurosci. Lett. 205:79-82(1996).
RN   [72]
RP   VARIANT ALS1 ASN-135.
RX   PubMed=8990014;
RX   DOI=10.1002/(SICI)1098-1004(1997)9:1<69::AID-HUMU14>3.0.CO;2-N;
RA   Watanabe M., Aoki M., Abe K., Shoji M., Lizuka T., Ikeda Y., Hirai S.,
RA   Kurokawa K., Kato T., Sasaki H., Itoyama Y.;
RT   "A novel missense point mutation (S134N) of the Cu/Zn superoxide
RT   dismutase gene in a patient with familial motor neuron disease.";
RL   Hum. Mutat. 9:69-71(1997).
RN   [73]
RP   VARIANT ALS1 SER-17.
RX   PubMed=9101297;
RX   DOI=10.1002/(SICI)1098-1004(1997)9:4<356::AID-HUMU9>3.0.CO;2-3;
RA   Kawamata J., Shimohama S., Takano S., Harada K., Ueda K., Kimura J.;
RT   "Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with
RT   apparently sporadic young-onset amyotrophic lateral sclerosis.";
RL   Hum. Mutat. 9:356-358(1997).
RN   [74]
RP   VARIANT ALS1 SER-73.
RX   PubMed=9455977; DOI=10.1016/S0022-510X(97)00181-0;
RA   Orrell R.W., Marklund S.L., deBelleroche J.S.;
RT   "Familial ALS is associated with mutations in all exons of SOD1: a
RT   novel mutation in exon 3 (Gly72Ser).";
RL   J. Neurol. Sci. 153:46-49(1997).
RN   [75]
RP   VARIANT ALS1 THR-114.
RX   PubMed=10732812; DOI=10.1007/s100480050016;
RA   Kikugawa K., Nakano R., Inuzuka T., Kokubo Y., Narita Y., Kuzuhara S.,
RA   Yoshida S., Tsuji S.;
RT   "A missense mutation in the SOD1 gene in patients with amyotrophic
RT   lateral sclerosis from the Kii Peninsula and its vicinity, Japan.";
RL   Neurogenetics 1:113-115(1997).
RN   [76]
RP   VARIANT ALS1 GLN-9.
RX   PubMed=9131652; DOI=10.1016/S0960-8966(96)00419-1;
RA   Bereznai B., Winkler A., Borasio G.D., Gasser T.;
RT   "A novel SOD1 mutation in an Austrian family with amyotrophic lateral
RT   sclerosis.";
RL   Neuromuscul. Disord. 7:113-116(1997).
RN   [77]
RP   CHARACTERIZATION OF VARIANTS ALS1 VAL-5; ARG-38; ARG-47; GLN-49;
RP   ARG-86 AND THR-114.
RX   PubMed=10400992; DOI=10.1093/hmg/8.8.1451;
RA   Ratovitski T., Corson L.B., Strain J., Wong P., Cleveland D.W.,
RA   Culotta V.C., Borchelt D.R.;
RT   "Variation in the biochemical/biophysical properties of mutant
RT   superoxide dismutase 1 enzymes and the rate of disease progression in
RT   familial amyotrophic lateral sclerosis kindreds.";
RL   Hum. Mol. Genet. 8:1451-1460(1999).
RN   [78]
RP   VARIANT ALS1 ARG-13.
RX   PubMed=10430435; DOI=10.1212/WNL.53.2.404;
RA   Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M.,
RA   Bugiani O., Ajmar F., Garre C.;
RT   "A SOD1 gene mutation in a patient with slowly progressing familial
RT   ALS.";
RL   Neurology 53:404-406(1999).
RN   [79]
RP   ERRATUM.
RA   Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M.,
RA   Bugiani O., Ajmar F., Garre C.;
RL   Neurology 57:1146-1146(2001).
RN   [80]
RP   VARIANT ALS1 SER-127.
RX   PubMed=11535232; DOI=10.1016/S0022-510X(01)00558-5;
RA   Murakami T., Warita H., Hayashi T., Sato K., Manabe Y., Mizuno S.,
RA   Yamane K., Abe K.;
RT   "A novel SOD1 gene mutation in familial ALS with low penetrance in
RT   females.";
RL   J. Neurol. Sci. 189:45-47(2001).
RN   [81]
RP   VARIANT ALS1 CYS-46.
RX   PubMed=11369193; DOI=10.1016/S0960-8966(00)00215-7;
RA   Gellera C., Castellotti B., Riggio M.C., Silani V., Morandi L.,
RA   Testa D., Casali C., Taroni F., Di Donato S., Zeviani M., Mariotti C.;
RT   "Superoxide dismutase gene mutations in Italian patients with familial
RT   and sporadic amyotrophic lateral sclerosis: identification of three
RT   novel missense mutations.";
RL   Neuromuscul. Disord. 11:404-410(2001).
RN   [82]
RP   VARIANT ALS1 ALA-81.
RX   PubMed=12402272; DOI=10.1002/ana.10369;
RA   Alexander M.D., Traynor B.J., Miller N., Corr B., Frost E.,
RA   McQuaid S., Brett F.M., Green A., Hardiman O.;
RT   "'True' sporadic ALS associated with a novel SOD-1 mutation.";
RL   Ann. Neurol. 52:680-683(2002).
RN   [83]
RP   CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-47; ARG-86 AND ALA-94,
RP   INTERACTION WITH RNF19A, AND UBIQUITINATION.
RX   PubMed=12145308; DOI=10.1074/jbc.M206559200;
RA   Niwa J., Ishigaki S., Hishikawa N., Yamamoto M., Doyu M., Murata S.,
RA   Tanaka K., Taniguchi N., Sobue G.;
RT   "Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated
RT   neurotoxicity.";
RL   J. Biol. Chem. 277:36793-36798(2002).
RN   [84]
RP   VARIANTS ALS1 VAL-9; CYS-21; LEU-23; ARG-49; ARG-55; ALA-88; THR-90;
RP   MET-98; LEU-119; GLY-125 AND ARG-148.
RX   PubMed=14506936; DOI=10.1080/14660820310011700;
RA   Andersen P.M., Sims K.B., Xin W.W., Kiely R., O'Neill G., Ravits J.,
RA   Pioro E., Harati Y., Brower R.D., Levine J.S., Heinicke H.U.,
RA   Seltzer W., Boss M., Brown R.H. Jr.;
RT   "Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in
RT   amyotrophic lateral sclerosis: a decade of discoveries, defects and
RT   disputes.";
RL   Amyotroph. Lateral Scler. 4:62-73(2003).
RN   [85]
RP   CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-86 AND ARG-94,
RP   MUTAGENESIS OF CYS-7; 51-PHE-GLY-52; CYS-58; HIS-81; ASP-84; CYS-112
RP   AND CYS-147, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18552350; DOI=10.1074/jbc.M802083200;
RA   Furukawa Y., Kaneko K., Yamanaka K., O'Halloran T.V., Nukina N.;
RT   "Complete loss of post-translational modifications triggers fibrillar
RT   aggregation of SOD1 in the familial form of amyotrophic lateral
RT   sclerosis.";
RL   J. Biol. Chem. 283:24167-24176(2008).
RN   [86]
RP   CHARACTERIZATION OF VARIANTS ALS1 ARG-55; ALA-91; ALA-94; ASP-94;
RP   MET-98 AND PHE-145.
RX   PubMed=18301754; DOI=10.1371/journal.pone.0001677;
RA   Banci L., Bertini I., Boca M., Girotto S., Martinelli M.,
RA   Valentine J.S., Vieru M.;
RT   "SOD1 and amyotrophic lateral sclerosis: mutations and
RT   oligomerization.";
RL   PLoS ONE 3:E1677-E1677(2008).
RN   [87]
RP   CHARACTERIZATION OF VARIANTS ALS1 ARG-86 AND ALA-94, UBIQUITINATION BY
RP   MARCH5, AND SUBCELLULAR LOCATION.
RX   PubMed=19741096; DOI=10.1091/mbc.E09-02-0112;
RA   Yonashiro R., Sugiura A., Miyachi M., Fukuda T., Matsushita N.,
RA   Inatome R., Ogata Y., Suzuki T., Dohmae N., Yanagi S.;
RT   "Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and
RT   attenuates mutant SOD1-induced reactive oxygen species generation.";
RL   Mol. Biol. Cell 20:4524-4530(2009).
RN   [88]
RP   VARIANT ALS1 PRO-68.
RX   PubMed=21247266; DOI=10.3109/17482968.2011.551939;
RA   del Grande A., Luigetti M., Conte A., Mancuso I., Lattante S.,
RA   Marangi G., Stipa G., Zollino M., Sabatelli M.;
RT   "A novel L67P SOD1 mutation in an Italian ALS patient.";
RL   Amyotroph. Lateral Scler. 12:150-152(2011).
RN   [89]
RP   VARIANT ALS1 GLY-96.
RX   PubMed=21220647; DOI=10.1001/archneurol.2010.352;
RA   Chio A., Borghero G., Pugliatti M., Ticca A., Calvo A., Moglia C.,
RA   Mutani R., Brunetti M., Ossola I., Marrosu M.G., Murru M.R.,
RA   Floris G., Cannas A., Parish L.D., Cossu P., Abramzon Y.,
RA   Johnson J.O., Nalls M.A., Arepalli S., Chong S., Hernandez D.G.,
RA   Traynor B.J., Restagno G.;
RT   "Large proportion of amyotrophic lateral sclerosis cases in Sardinia
RT   due to a single founder mutation of the TARDBP gene.";
RL   Arch. Neurol. 68:594-598(2011).
RN   [90]
RP   VARIANTS ALS1 SER-87; ALA-88; ASN-102; GLY-102 AND TYR-112.
RX   PubMed=27604643; DOI=10.1038/srep32478;
RA   Hou L., Jiao B., Xiao T., Zhou L., Zhou Z., Du J., Yan X., Wang J.,
RA   Tang B., Shen L.;
RT   "Screening of SOD1, FUS and TARDBP genes in patients with amyotrophic
RT   lateral sclerosis in central-southern China.";
RL   Sci. Rep. 6:32478-32478(2016).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000269|PubMed:17888947};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000269|PubMed:17888947};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:17888947};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17888947};
CC   -!- SUBUNIT: Homodimer; non-disulfide linked. Homodimerization may
CC       take place via the ditryptophan cross-link at Trp-33. The
CC       pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94
CC       interact with RNF19A, whereas wild-type protein does not. The
CC       pathogenic variants ALS1 Arg-86 and Ala-94 interact with MARCH5,
CC       whereas wild-type protein does not. {ECO:0000269|PubMed:10329151,
CC       ECO:0000269|PubMed:12911296, ECO:0000269|PubMed:12963370,
CC       ECO:0000269|PubMed:15326189, ECO:0000269|PubMed:16291742,
CC       ECO:0000269|PubMed:16406071, ECO:0000269|PubMed:17548825,
CC       ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:20600836,
CC       ECO:0000269|PubMed:20727846}.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-990792, EBI-990792;
CC       P26339:Chga (xeno); NbExp=5; IntAct=EBI-990792, EBI-990900;
CC       P16014:Chgb (xeno); NbExp=6; IntAct=EBI-990792, EBI-990820;
CC       Q8TCX1:DYNC2LI1; NbExp=3; IntAct=EBI-990792, EBI-8568003;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19741096}.
CC       Mitochondrion {ECO:0000269|PubMed:19741096}. Nucleus
CC       {ECO:0000269|PubMed:22496122}. Note=Predominantly cytoplasmic; the
CC       pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates
CC       and accumulates in mitochondria. {ECO:0000269|PubMed:19741096}.
CC   -!- PTM: Unlike wild-type protein, the pathogenic variants ALS1 Arg-
CC       38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A
CC       leading to their proteasomal degradation. The pathogenic variants
CC       ALS1 Arg-86 and Ala-94 are ubiquitinated by MARCH5 leading to
CC       their proteasomal degradation. {ECO:0000269|PubMed:12145308,
CC       ECO:0000269|PubMed:19741096}.
CC   -!- PTM: The ditryptophan cross-link at Trp-33 is responsible for the
CC       non-disulfide-linked homodimerization. Such modification might
CC       only occur in extreme conditions and additional experimental
CC       evidence is required. {ECO:0000269|PubMed:20600836}.
CC   -!- PTM: Palmitoylation helps nuclear targeting and decreases
CC       catalytic activity. {ECO:0000269|PubMed:22496122}.
CC   -!- PTM: Succinylation, adjacent to copper catalytic site, probably
CC       inhibits activity. Desuccinylation by SIRT5 enhances activity.
CC       {ECO:0000269|PubMed:24140062}.
CC   -!- DISEASE: Amyotrophic lateral sclerosis 1 (ALS1) [MIM:105400]: A
CC       neurodegenerative disorder affecting upper motor neurons in the
CC       brain and lower motor neurons in the brain stem and spinal cord,
CC       resulting in fatal paralysis. Sensory abnormalities are absent.
CC       The pathologic hallmarks of the disease include pallor of the
CC       corticospinal tract due to loss of motor neurons, presence of
CC       ubiquitin-positive inclusions within surviving motor neurons, and
CC       deposition of pathologic aggregates. The etiology of amyotrophic
CC       lateral sclerosis is likely to be multifactorial, involving both
CC       genetic and environmental factors. The disease is inherited in 5-
CC       10% of the cases. {ECO:0000269|PubMed:10400992,
CC       ECO:0000269|PubMed:10430435, ECO:0000269|PubMed:10732812,
CC       ECO:0000269|PubMed:11369193, ECO:0000269|PubMed:11535232,
CC       ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12402272,
CC       ECO:0000269|PubMed:12754496, ECO:0000269|PubMed:12963370,
CC       ECO:0000269|PubMed:14506936, ECO:0000269|PubMed:15056757,
CC       ECO:0000269|PubMed:18301754, ECO:0000269|PubMed:18378676,
CC       ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:19741096,
CC       ECO:0000269|PubMed:21220647, ECO:0000269|PubMed:21247266,
CC       ECO:0000269|PubMed:27604643, ECO:0000269|PubMed:7496169,
CC       ECO:0000269|PubMed:7501156, ECO:0000269|PubMed:7647793,
CC       ECO:0000269|PubMed:7655468, ECO:0000269|PubMed:7655469,
CC       ECO:0000269|PubMed:7655471, ECO:0000269|PubMed:7700376,
CC       ECO:0000269|PubMed:7795609, ECO:0000269|PubMed:7836951,
CC       ECO:0000269|PubMed:7870076, ECO:0000269|PubMed:7881433,
CC       ECO:0000269|PubMed:7887412, ECO:0000269|PubMed:7951252,
CC       ECO:0000269|PubMed:7980516, ECO:0000269|PubMed:7997024,
CC       ECO:0000269|PubMed:8069312, ECO:0000269|PubMed:8179602,
CC       ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170,
CC       ECO:0000269|PubMed:8528216, ECO:0000269|PubMed:8682505,
CC       ECO:0000269|PubMed:8907321, ECO:0000269|PubMed:8938700,
CC       ECO:0000269|PubMed:8990014, ECO:0000269|PubMed:9101297,
CC       ECO:0000269|PubMed:9131652, ECO:0000269|PubMed:9455977,
CC       ECO:0000269|PubMed:9541385}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: The protein (both wild-type and ALS1 variants) has
CC       a tendency to form fibrillar aggregates in the absence of the
CC       intramolecular disulfide bond or of bound zinc ions. These
CC       aggregates may have cytotoxic effects. Zinc binding promotes
CC       dimerization and stabilizes the native form.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Alsod; Note=ALS genetic mutations db;
CC       URL="http://alsod.iop.kcl.ac.uk/Als/";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/sod1/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Superoxide dismutase entry;
CC       URL="https://en.wikipedia.org/wiki/Superoxide_dismutase";
DR   EMBL; L44139; AAB05662.1; -; Genomic_DNA.
DR   EMBL; L44135; AAB05662.1; JOINED; Genomic_DNA.
DR   EMBL; L44136; AAB05662.1; JOINED; Genomic_DNA.
DR   EMBL; L44137; AAB05662.1; JOINED; Genomic_DNA.
DR   EMBL; L44139; AAB05661.1; -; Genomic_DNA.
DR   EMBL; L44135; AAB05661.1; JOINED; Genomic_DNA.
DR   EMBL; L44136; AAB05661.1; JOINED; Genomic_DNA.
DR   EMBL; L44137; AAB05661.1; JOINED; Genomic_DNA.
DR   EMBL; X02317; CAA26182.1; -; mRNA.
DR   EMBL; X01780; CAA25915.1; -; Genomic_DNA.
DR   EMBL; X01781; CAA25916.1; -; Genomic_DNA.
DR   EMBL; X01782; CAA25917.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X01783; CAA25918.1; -; Genomic_DNA.
DR   EMBL; X01784; CAA25919.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY049787; AAL15444.1; -; mRNA.
DR   EMBL; AY450286; AAR21563.1; -; mRNA.
DR   EMBL; EF151142; ABL96616.1; -; mRNA.
DR   EMBL; AK312116; BAG35052.1; -; mRNA.
DR   EMBL; CR450355; CAG29351.1; -; mRNA.
DR   EMBL; CR541742; CAG46542.1; -; mRNA.
DR   EMBL; BT006676; AAP35322.1; -; mRNA.
DR   EMBL; AY835629; AAV80422.1; -; Genomic_DNA.
DR   EMBL; AP000253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471079; EAX09889.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09890.1; -; Genomic_DNA.
DR   EMBL; BC001034; AAH01034.1; -; mRNA.
DR   EMBL; L46374; AAB59626.1; -; Genomic_DNA.
DR   EMBL; L46375; AAB59627.1; -; Genomic_DNA.
DR   EMBL; L44746; AAC41773.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X95228; CAA64520.1; -; Genomic_DNA.
DR   CCDS; CCDS33536.1; -.
DR   PIR; A22703; DSHUCZ.
DR   RefSeq; NP_000445.1; NM_000454.4.
DR   UniGene; Hs.443914; -.
DR   PDB; 1AZV; X-ray; 1.90 A; A/B=2-154.
DR   PDB; 1BA9; NMR; -; A=2-154.
DR   PDB; 1DSW; NMR; -; A=2-154.
DR   PDB; 1FUN; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J=2-154.
DR   PDB; 1HL4; X-ray; 1.82 A; A/B/C/D=2-154.
DR   PDB; 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.
DR   PDB; 1KMG; NMR; -; A=2-154.
DR   PDB; 1L3N; NMR; -; A/B=2-154.
DR   PDB; 1MFM; X-ray; 1.02 A; A=2-154.
DR   PDB; 1N18; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=1-154.
DR   PDB; 1N19; X-ray; 1.86 A; A/B=1-154.
DR   PDB; 1OEZ; X-ray; 2.15 A; W/X/Y/Z=2-154.
DR   PDB; 1OZT; X-ray; 2.50 A; G/H/I/J/K/L/M/N=2-154.
DR   PDB; 1OZU; X-ray; 1.30 A; A/B=2-154.
DR   PDB; 1P1V; X-ray; 1.40 A; A/B/C=2-154.
DR   PDB; 1PTZ; X-ray; 1.80 A; A/B=2-154.
DR   PDB; 1PU0; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-154.
DR   PDB; 1RK7; NMR; -; A=2-154.
DR   PDB; 1SOS; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=2-154.
DR   PDB; 1SPD; X-ray; 2.40 A; A/B=2-154.
DR   PDB; 1UXL; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J=2-154.
DR   PDB; 1UXM; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154.
DR   PDB; 2AF2; NMR; -; A/B=2-154.
DR   PDB; 2C9S; X-ray; 1.24 A; A/F=2-154.
DR   PDB; 2C9U; X-ray; 1.24 A; A/F=2-154.
DR   PDB; 2C9V; X-ray; 1.07 A; A/F=2-154.
DR   PDB; 2GBT; X-ray; 1.70 A; A/B/C/D=2-154.
DR   PDB; 2GBU; X-ray; 2.00 A; A/B/C/D=2-154.
DR   PDB; 2GBV; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=2-154.
DR   PDB; 2LU5; NMR; -; A=2-154.
DR   PDB; 2MP3; NMR; -; A=2-126.
DR   PDB; 2NAM; NMR; -; A=2-154.
DR   PDB; 2NNX; X-ray; 2.30 A; A/B/C/D=2-154.
DR   PDB; 2R27; X-ray; 2.00 A; A/B=1-154.
DR   PDB; 2V0A; X-ray; 1.15 A; A/F=2-154.
DR   PDB; 2VR6; X-ray; 1.30 A; A/F=2-154.
DR   PDB; 2VR7; X-ray; 1.58 A; A/F=2-154.
DR   PDB; 2VR8; X-ray; 1.36 A; A/F=2-154.
DR   PDB; 2WKO; X-ray; 1.97 A; A/F=2-154.
DR   PDB; 2WYT; X-ray; 1.00 A; A/F=2-154.
DR   PDB; 2WYZ; X-ray; 1.70 A; A/F=2-154.
DR   PDB; 2WZ0; X-ray; 1.72 A; A/F=2-154.
DR   PDB; 2WZ5; X-ray; 1.50 A; A/F=2-154.
DR   PDB; 2WZ6; X-ray; 1.55 A; A/F=2-154.
DR   PDB; 2XJK; X-ray; 1.45 A; A=2-154.
DR   PDB; 2XJL; X-ray; 1.55 A; A=2-154.
DR   PDB; 2ZKW; X-ray; 1.90 A; A/B=1-154.
DR   PDB; 2ZKX; X-ray; 2.72 A; A/B/C/D=1-154.
DR   PDB; 2ZKY; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-154.
DR   PDB; 3CQP; X-ray; 1.95 A; A/B/C/D=2-154.
DR   PDB; 3CQQ; X-ray; 1.90 A; A/B=2-154.
DR   PDB; 3ECU; X-ray; 1.90 A; A/B/C/D=2-154.
DR   PDB; 3ECV; X-ray; 1.90 A; A/B/C/D=2-154.
DR   PDB; 3ECW; X-ray; 2.15 A; A/B/C/D=2-154.
DR   PDB; 3GQF; X-ray; 2.20 A; A/B/C/D/E/F=2-154.
DR   PDB; 3GTV; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-81.
DR   PDB; 3GZO; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=2-154.
DR   PDB; 3GZP; X-ray; 3.10 A; A/B/C/D=2-154.
DR   PDB; 3GZQ; X-ray; 1.40 A; A/B=2-154.
DR   PDB; 3H2P; X-ray; 1.55 A; A/B=2-154.
DR   PDB; 3H2Q; X-ray; 1.85 A; A/B/C/D=2-154.
DR   PDB; 3HFF; X-ray; 2.20 A; A=2-154.
DR   PDB; 3K91; X-ray; 1.75 A; A/B=2-154.
DR   PDB; 3KH3; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154.
DR   PDB; 3KH4; X-ray; 3.50 A; A/B/C/D/E/F=2-154.
DR   PDB; 3LTV; X-ray; 2.45 A; A/B/C/D/E/F=82-154.
DR   PDB; 3QQD; X-ray; 1.65 A; A/B=2-154.
DR   PDB; 3RE0; X-ray; 2.28 A; A/B/C/D=2-154.
DR   PDB; 3T5W; X-ray; 1.80 A; A/B/D/E/F/G/H/I/J/K/L/M=2-154.
DR   PDB; 4A7G; X-ray; 1.24 A; A/F=2-154.
DR   PDB; 4A7Q; X-ray; 1.22 A; A/F=2-154.
DR   PDB; 4A7S; X-ray; 1.06 A; A/F=2-154.
DR   PDB; 4A7T; X-ray; 1.45 A; A/F=2-154.
DR   PDB; 4A7U; X-ray; 0.98 A; A/F=2-154.
DR   PDB; 4A7V; X-ray; 1.00 A; A/F=2-154.
DR   PDB; 4B3E; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J=1-154.
DR   PDB; 4BCY; X-ray; 1.27 A; A=2-154.
DR   PDB; 4BCZ; X-ray; 1.93 A; A/B=2-49, A/B=83-124, A/B=141-154.
DR   PDB; 4BD4; X-ray; 2.78 A; A/B/C/D/E/F/G/H/I=2-49, A/B/C/D/E/F/G/H/I=83-124, A/B/C/D/E/F/G/H/I=141-154.
DR   PDB; 4FF9; X-ray; 2.50 A; A/B=2-154.
DR   PDB; 4MCM; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154.
DR   PDB; 4MCN; X-ray; 2.60 A; A/B=2-154.
DR   PDB; 4NIN; X-ray; 1.40 A; A=102-108.
DR   PDB; 4NIO; X-ray; 1.30 A; A=148-154.
DR   PDB; 4NIP; X-ray; 1.90 A; A=148-154.
DR   PDB; 4OH2; X-ray; 2.38 A; A/B/C/D/E/F/G/H/I/J=2-154.
DR   PDB; 4SOD; Model; -; A=1-154.
DR   PDB; 4XCR; X-ray; 3.60 A; A/B=2-154.
DR   PDB; 5DLI; X-ray; 2.10 A; A/B/C/D/E/F/G/H=29-39.
DR   PDB; 5J07; X-ray; 2.00 A; A/B=14-49, A/B=84-124, A/B=141-154.
DR   PDB; 5J0C; X-ray; 1.60 A; A/B=29-49, A/B=84-124.
DR   PDB; 5J0F; X-ray; 1.25 A; A/B=83-124.
DR   PDB; 5J0G; X-ray; 2.50 A; A/B=2-124.
DR   PDB; 5K02; X-ray; 1.99 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-154.
DR   PDB; 5U9M; X-ray; 2.35 A; A/C=2-154.
DR   PDBsum; 1AZV; -.
DR   PDBsum; 1BA9; -.
DR   PDBsum; 1DSW; -.
DR   PDBsum; 1FUN; -.
DR   PDBsum; 1HL4; -.
DR   PDBsum; 1HL5; -.
DR   PDBsum; 1KMG; -.
DR   PDBsum; 1L3N; -.
DR   PDBsum; 1MFM; -.
DR   PDBsum; 1N18; -.
DR   PDBsum; 1N19; -.
DR   PDBsum; 1OEZ; -.
DR   PDBsum; 1OZT; -.
DR   PDBsum; 1OZU; -.
DR   PDBsum; 1P1V; -.
DR   PDBsum; 1PTZ; -.
DR   PDBsum; 1PU0; -.
DR   PDBsum; 1RK7; -.
DR   PDBsum; 1SOS; -.
DR   PDBsum; 1SPD; -.
DR   PDBsum; 1UXL; -.
DR   PDBsum; 1UXM; -.
DR   PDBsum; 2AF2; -.
DR   PDBsum; 2C9S; -.
DR   PDBsum; 2C9U; -.
DR   PDBsum; 2C9V; -.
DR   PDBsum; 2GBT; -.
DR   PDBsum; 2GBU; -.
DR   PDBsum; 2GBV; -.
DR   PDBsum; 2LU5; -.
DR   PDBsum; 2MP3; -.
DR   PDBsum; 2NAM; -.
DR   PDBsum; 2NNX; -.
DR   PDBsum; 2R27; -.
DR   PDBsum; 2V0A; -.
DR   PDBsum; 2VR6; -.
DR   PDBsum; 2VR7; -.
DR   PDBsum; 2VR8; -.
DR   PDBsum; 2WKO; -.
DR   PDBsum; 2WYT; -.
DR   PDBsum; 2WYZ; -.
DR   PDBsum; 2WZ0; -.
DR   PDBsum; 2WZ5; -.
DR   PDBsum; 2WZ6; -.
DR   PDBsum; 2XJK; -.
DR   PDBsum; 2XJL; -.
DR   PDBsum; 2ZKW; -.
DR   PDBsum; 2ZKX; -.
DR   PDBsum; 2ZKY; -.
DR   PDBsum; 3CQP; -.
DR   PDBsum; 3CQQ; -.
DR   PDBsum; 3ECU; -.
DR   PDBsum; 3ECV; -.
DR   PDBsum; 3ECW; -.
DR   PDBsum; 3GQF; -.
DR   PDBsum; 3GTV; -.
DR   PDBsum; 3GZO; -.
DR   PDBsum; 3GZP; -.
DR   PDBsum; 3GZQ; -.
DR   PDBsum; 3H2P; -.
DR   PDBsum; 3H2Q; -.
DR   PDBsum; 3HFF; -.
DR   PDBsum; 3K91; -.
DR   PDBsum; 3KH3; -.
DR   PDBsum; 3KH4; -.
DR   PDBsum; 3LTV; -.
DR   PDBsum; 3QQD; -.
DR   PDBsum; 3RE0; -.
DR   PDBsum; 3T5W; -.
DR   PDBsum; 4A7G; -.
DR   PDBsum; 4A7Q; -.
DR   PDBsum; 4A7S; -.
DR   PDBsum; 4A7T; -.
DR   PDBsum; 4A7U; -.
DR   PDBsum; 4A7V; -.
DR   PDBsum; 4B3E; -.
DR   PDBsum; 4BCY; -.
DR   PDBsum; 4BCZ; -.
DR   PDBsum; 4BD4; -.
DR   PDBsum; 4FF9; -.
DR   PDBsum; 4MCM; -.
DR   PDBsum; 4MCN; -.
DR   PDBsum; 4NIN; -.
DR   PDBsum; 4NIO; -.
DR   PDBsum; 4NIP; -.
DR   PDBsum; 4OH2; -.
DR   PDBsum; 4SOD; -.
DR   PDBsum; 4XCR; -.
DR   PDBsum; 5DLI; -.
DR   PDBsum; 5J07; -.
DR   PDBsum; 5J0C; -.
DR   PDBsum; 5J0F; -.
DR   PDBsum; 5J0G; -.
DR   PDBsum; 5K02; -.
DR   PDBsum; 5U9M; -.
DR   DisProt; DP00652; -.
DR   ProteinModelPortal; P00441; -.
DR   SMR; P00441; -.
DR   BioGrid; 112530; 163.
DR   DIP; DIP-44941N; -.
DR   IntAct; P00441; 29.
DR   MINT; MINT-204523; -.
DR   STRING; 9606.ENSP00000270142; -.
DR   BindingDB; P00441; -.
DR   ChEMBL; CHEMBL2354; -.
DR   DrugBank; DB05025; Arimoclomol.
DR   DrugBank; DB00958; Carboplatin.
DR   DrugBank; DB00515; Cisplatin.
DR   DrugBank; DB00526; Oxaliplatin.
DR   DrugBank; DB03382; S-Oxy Cysteine.
DR   DrugBank; DB00163; Vitamin E.
DR   iPTMnet; P00441; -.
DR   PhosphoSitePlus; P00441; -.
DR   SwissPalm; P00441; -.
DR   BioMuta; SOD1; -.
DR   DOSAC-COBS-2DPAGE; P00441; -.
DR   OGP; P00441; -.
DR   REPRODUCTION-2DPAGE; IPI00783680; -.
DR   SWISS-2DPAGE; P00441; -.
DR   UCD-2DPAGE; P00441; -.
DR   EPD; P00441; -.
DR   PaxDb; P00441; -.
DR   PeptideAtlas; P00441; -.
DR   PRIDE; P00441; -.
DR   TopDownProteomics; P00441; -.
DR   DNASU; 6647; -.
DR   Ensembl; ENST00000270142; ENSP00000270142; ENSG00000142168.
DR   GeneID; 6647; -.
DR   KEGG; hsa:6647; -.
DR   CTD; 6647; -.
DR   DisGeNET; 6647; -.
DR   EuPathDB; HostDB:ENSG00000142168.14; -.
DR   GeneCards; SOD1; -.
DR   GeneReviews; SOD1; -.
DR   HGNC; HGNC:11179; SOD1.
DR   HPA; CAB008670; -.
DR   HPA; HPA001401; -.
DR   MalaCards; SOD1; -.
DR   MIM; 105400; phenotype.
DR   MIM; 147450; gene.
DR   neXtProt; NX_P00441; -.
DR   OpenTargets; ENSG00000142168; -.
DR   Orphanet; 803; Amyotrophic lateral sclerosis.
DR   PharmGKB; PA334; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00530000063226; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; P00441; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   PhylomeDB; P00441; -.
DR   TreeFam; TF105131; -.
DR   BioCyc; MetaCyc:HS06899-MONOMER; -.
DR   BRENDA; 1.15.1.1; 2681.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR   ChiTaRS; SOD1; human.
DR   EvolutionaryTrace; P00441; -.
DR   GeneWiki; SOD1; -.
DR   GenomeRNAi; 6647; -.
DR   PRO; PR:P00441; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   Bgee; ENSG00000142168; -.
DR   CleanEx; HS_SOD1; -.
DR   ExpressionAtlas; P00441; baseline and differential.
DR   Genevisible; P00441; HS.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031045; C:dense core granule; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR   GO; GO:0005759; C:mitochondrial matrix; NAS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IDA:UniProtKB.
DR   GO; GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; ISS:BHF-UCL.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
DR   GO; GO:0007569; P:cell aging; IMP:UniProtKB.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
DR   GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0060047; P:heart contraction; IDA:UniProtKB.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB.
DR   GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB.
DR   GO; GO:0001890; P:placenta development; NAS:UniProtKB.
DR   GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IC:UniProtKB.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:UniProtKB.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
DR   GO; GO:0046620; P:regulation of organ growth; NAS:UniProtKB.
DR   GO; GO:0045859; P:regulation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0033081; P:regulation of T cell differentiation in thymus; NAS:UniProtKB.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; ISS:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl.
DR   GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR   GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
DR   GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; ISS:UniProtKB.
DR   GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
DR   GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
DR   GO; GO:0000303; P:response to superoxide; IDA:UniProtKB.
DR   GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR   GO; GO:0008090; P:retrograde axonal transport; ISS:BHF-UCL.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0006801; P:superoxide metabolic process; IDA:BHF-UCL.
DR   GO; GO:0048538; P:thymus development; NAS:UniProtKB.
DR   GO; GO:0019226; P:transmission of nerve impulse; ISS:UniProtKB.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Amyotrophic lateral sclerosis; Antioxidant;
KW   Complete proteome; Copper; Cytoplasm; Direct protein sequencing;
KW   Disease mutation; Disulfide bond; Lipoprotein; Metal-binding;
KW   Mitochondrion; Neurodegeneration; Nucleus; Oxidoreductase; Palmitate;
KW   Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:25944712,
FT                                ECO:0000269|PubMed:6770891,
FT                                ECO:0000269|PubMed:7002610}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164057.
FT   METAL        47     47       Copper; catalytic.
FT                                {ECO:0000269|PubMed:12963370,
FT                                ECO:0000269|PubMed:17548825}.
FT   METAL        49     49       Copper; catalytic.
FT                                {ECO:0000269|PubMed:12963370,
FT                                ECO:0000269|PubMed:17548825}.
FT   METAL        64     64       Copper; catalytic.
FT                                {ECO:0000269|PubMed:12963370,
FT                                ECO:0000269|PubMed:17548825}.
FT   METAL        64     64       Zinc; via pros nitrogen.
FT                                {ECO:0000269|PubMed:20727846}.
FT   METAL        72     72       Zinc; via pros nitrogen.
FT                                {ECO:0000269|PubMed:20727846}.
FT   METAL        81     81       Zinc; via pros nitrogen.
FT                                {ECO:0000269|PubMed:20727846}.
FT   METAL        84     84       Zinc; structural.
FT                                {ECO:0000269|PubMed:20727846}.
FT   METAL       121    121       Copper; catalytic.
FT                                {ECO:0000269|PubMed:12963370,
FT                                ECO:0000269|PubMed:17548825}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:25944712,
FT                                ECO:0000269|PubMed:1463506,
FT                                ECO:0000269|PubMed:7002610}.
FT   MOD_RES       4      4       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      10     10       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      92     92       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES      99     99       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     103    103       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     106    106       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07632}.
FT   MOD_RES     108    108       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     123    123       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     123    123       N6-succinyllysine; alternate.
FT                                {ECO:0000269|PubMed:24140062}.
FT   MOD_RES     137    137       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   MOD_RES     137    137       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P08228}.
FT   LIPID         7      7       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:22496122}.
FT   DISULFID     58    147       {ECO:0000269|PubMed:12963370,
FT                                ECO:0000269|PubMed:1463506,
FT                                ECO:0000269|PubMed:15326189,
FT                                ECO:0000269|PubMed:16406071}.
FT   CROSSLNK     33     33       1-(tryptophan-3-yl)-tryptophan (Trp-Trp)
FT                                (interchain with W-33).
FT                                {ECO:0000269|PubMed:20600836}.
FT   VARIANT       5      5       A -> S (in ALS1).
FT                                /FTId=VAR_013518.
FT   VARIANT       5      5       A -> T (in ALS1; dbSNP:rs121912444).
FT                                {ECO:0000269|PubMed:8179602}.
FT                                /FTId=VAR_007130.
FT   VARIANT       5      5       A -> V (in ALS1; severe form; reduces
FT                                structural stability and enzyme activity;
FT                                increases tendency to form fibrillar
FT                                aggregates; dbSNP:rs121912442).
FT                                {ECO:0000269|PubMed:10400992,
FT                                ECO:0000269|PubMed:12963370,
FT                                ECO:0000269|PubMed:15056757}.
FT                                /FTId=VAR_007131.
FT   VARIANT       7      7       C -> F (in ALS1; dbSNP:rs121912448).
FT                                {ECO:0000269|PubMed:8907321}.
FT                                /FTId=VAR_008717.
FT   VARIANT       8      8       V -> E (in ALS1).
FT                                {ECO:0000269|PubMed:7980516}.
FT                                /FTId=VAR_007132.
FT   VARIANT       9      9       L -> Q (in ALS1).
FT                                {ECO:0000269|PubMed:9131652}.
FT                                /FTId=VAR_013519.
FT   VARIANT       9      9       L -> V (in ALS1).
FT                                {ECO:0000269|PubMed:14506936}.
FT                                /FTId=VAR_013520.
FT   VARIANT      13     13       G -> R (in ALS1; dbSNP:rs121912456).
FT                                {ECO:0000269|PubMed:10430435}.
FT                                /FTId=VAR_013521.
FT   VARIANT      15     15       V -> G (in ALS1).
FT                                /FTId=VAR_013522.
FT   VARIANT      15     15       V -> M (in ALS1).
FT                                {ECO:0000269|PubMed:7655471}.
FT                                /FTId=VAR_007133.
FT   VARIANT      17     17       G -> S (in ALS1; sporadic young onset;
FT                                dbSNP:rs121912453).
FT                                {ECO:0000269|PubMed:9101297}.
FT                                /FTId=VAR_007134.
FT   VARIANT      21     21       F -> C (in ALS1).
FT                                {ECO:0000269|PubMed:14506936}.
FT                                /FTId=VAR_045876.
FT   VARIANT      22     22       E -> G (in ALS1).
FT                                /FTId=VAR_013523.
FT   VARIANT      22     22       E -> K (in ALS1; dbSNP:rs121912450).
FT                                {ECO:0000269|PubMed:8069312}.
FT                                /FTId=VAR_007135.
FT   VARIANT      23     23       Q -> L (in ALS1).
FT                                {ECO:0000269|PubMed:14506936}.
FT                                /FTId=VAR_045877.
FT   VARIANT      38     38       G -> R (in ALS1; mild form; ubiquitinated
FT                                by RNF19A. Ubiquitinated by MARCH5;
FT                                leading to the degradation of
FT                                mitochondrial SOD1; dbSNP:rs121912431).
FT                                {ECO:0000269|PubMed:10400992,
FT                                ECO:0000269|PubMed:12145308,
FT                                ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:9541385}.
FT                                /FTId=VAR_007136.
FT   VARIANT      39     39       L -> R (in ALS1).
FT                                /FTId=VAR_013524.
FT   VARIANT      39     39       L -> V (in ALS1; dbSNP:rs121912432).
FT                                /FTId=VAR_007137.
FT   VARIANT      42     42       G -> D (in ALS1; dbSNP:rs121912434).
FT                                /FTId=VAR_007139.
FT   VARIANT      42     42       G -> S (in ALS1; dbSNP:rs121912433).
FT                                /FTId=VAR_007138.
FT   VARIANT      44     44       H -> R (in ALS1; reduces structural
FT                                stability and enzyme activity; increases
FT                                tendency to form fibrillar aggregates;
FT                                dbSNP:rs121912435).
FT                                {ECO:0000269|PubMed:12963370}.
FT                                /FTId=VAR_007140.
FT   VARIANT      46     46       F -> C (in ALS1; slow progression;
FT                                dbSNP:rs121912457).
FT                                {ECO:0000269|PubMed:11369193}.
FT                                /FTId=VAR_013525.
FT   VARIANT      47     47       H -> R (in ALS1; "benign" form; 80% of
FT                                wild-type activity; ubiquitinated by
FT                                RNF19A; dbSNP:rs121912443).
FT                                {ECO:0000269|PubMed:10400992,
FT                                ECO:0000269|PubMed:12145308,
FT                                ECO:0000269|PubMed:12754496,
FT                                ECO:0000269|PubMed:7836951}.
FT                                /FTId=VAR_007141.
FT   VARIANT      49     49       H -> Q (in ALS1).
FT                                {ECO:0000269|PubMed:10400992,
FT                                ECO:0000269|PubMed:8528216}.
FT                                /FTId=VAR_007142.
FT   VARIANT      49     49       H -> R (in ALS1).
FT                                {ECO:0000269|PubMed:14506936}.
FT                                /FTId=VAR_045878.
FT   VARIANT      50     50       E -> K (in ALS1).
FT                                /FTId=VAR_013526.
FT   VARIANT      55     55       T -> R (in ALS1; reduces tendency to form
FT                                fibrillar aggregates).
FT                                {ECO:0000269|PubMed:14506936,
FT                                ECO:0000269|PubMed:18301754}.
FT                                /FTId=VAR_045879.
FT   VARIANT      66     66       N -> S (in ALS1).
FT                                /FTId=VAR_013527.
FT   VARIANT      68     68       L -> P (in ALS1).
FT                                {ECO:0000269|PubMed:21247266}.
FT                                /FTId=VAR_065560.
FT   VARIANT      68     68       L -> R (in ALS1).
FT                                /FTId=VAR_013528.
FT   VARIANT      73     73       G -> S (in ALS1; dbSNP:rs121912455).
FT                                {ECO:0000269|PubMed:9455977}.
FT                                /FTId=VAR_008718.
FT   VARIANT      77     77       D -> Y (in ALS1).
FT                                /FTId=VAR_013529.
FT   VARIANT      81     81       H -> A (in ALS1; sporadic form;
FT                                interferes with zinc binding; requires 2
FT                                nucleotide substitutions).
FT                                {ECO:0000269|PubMed:12402272}.
FT                                /FTId=VAR_016874.
FT   VARIANT      85     85       L -> F (in ALS1).
FT                                /FTId=VAR_013530.
FT   VARIANT      85     85       L -> V (in ALS1; dbSNP:rs121912452).
FT                                {ECO:0000269|PubMed:7655471}.
FT                                /FTId=VAR_007143.
FT   VARIANT      86     86       G -> R (in ALS1; ubiquitinated by RNF19A;
FT                                interferes with zinc-binding;
FT                                ubiquitinated by MARCH5; leading to the
FT                                degradation of mitochondrial SOD1;
FT                                dbSNP:rs121912436).
FT                                {ECO:0000269|PubMed:10400992,
FT                                ECO:0000269|PubMed:12145308,
FT                                ECO:0000269|PubMed:18378676,
FT                                ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:19741096,
FT                                ECO:0000269|Ref.47}.
FT                                /FTId=VAR_007144.
FT   VARIANT      87     87       N -> S (in ALS1; dbSNP:rs11556620).
FT                                {ECO:0000269|PubMed:27604643}.
FT                                /FTId=VAR_013531.
FT   VARIANT      88     88       V -> A (in ALS1).
FT                                {ECO:0000269|PubMed:14506936,
FT                                ECO:0000269|PubMed:27604643}.
FT                                /FTId=VAR_045880.
FT   VARIANT      90     90       A -> T (in ALS1).
FT                                {ECO:0000269|PubMed:14506936}.
FT                                /FTId=VAR_045881.
FT   VARIANT      90     90       A -> V (in ALS1).
FT                                /FTId=VAR_013532.
FT   VARIANT      91     91       D -> A (in ALS1; does not seem to be
FT                                linked with a decrease in activity;
FT                                dbSNP:rs80265967).
FT                                {ECO:0000269|PubMed:18301754,
FT                                ECO:0000269|PubMed:7647793,
FT                                ECO:0000269|PubMed:7655469}.
FT                                /FTId=VAR_007145.
FT   VARIANT      91     91       D -> V (in ALS1).
FT                                /FTId=VAR_013533.
FT   VARIANT      94     94       G -> A (in ALS1; increases tendency to
FT                                form fibrillar aggregates; ubiquitinated
FT                                by RNF19A; dbSNP:rs121912438).
FT                                {ECO:0000269|PubMed:12145308,
FT                                ECO:0000269|PubMed:18301754,
FT                                ECO:0000269|PubMed:19741096}.
FT                                /FTId=VAR_007146.
FT   VARIANT      94     94       G -> C (in ALS1; dbSNP:rs121912437).
FT                                /FTId=VAR_007147.
FT   VARIANT      94     94       G -> D (in ALS1).
FT                                {ECO:0000269|PubMed:18301754,
FT                                ECO:0000269|PubMed:7951252}.
FT                                /FTId=VAR_007148.
FT   VARIANT      94     94       G -> R (in ALS1; 30% of wild-type
FT                                activity; dbSNP:rs121912437).
FT                                {ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:7700376,
FT                                ECO:0000269|PubMed:8528216}.
FT                                /FTId=VAR_007149.
FT   VARIANT      94     94       G -> V (in ALS1).
FT                                {ECO:0000269|PubMed:8938700}.
FT                                /FTId=VAR_008719.
FT   VARIANT      96     96       A -> G (in ALS1).
FT                                {ECO:0000269|PubMed:21220647}.
FT                                /FTId=VAR_065194.
FT   VARIANT      98     98       V -> M (in ALS1; increases tendency to
FT                                form fibrillar aggregates).
FT                                {ECO:0000269|PubMed:14506936,
FT                                ECO:0000269|PubMed:18301754}.
FT                                /FTId=VAR_045882.
FT   VARIANT     101    101       E -> G (in ALS1; dbSNP:rs121912439).
FT                                /FTId=VAR_007150.
FT   VARIANT     101    101       E -> K (in ALS1).
FT                                /FTId=VAR_013534.
FT   VARIANT     102    102       D -> G (in ALS1).
FT                                {ECO:0000269|PubMed:27604643,
FT                                ECO:0000269|PubMed:7655468}.
FT                                /FTId=VAR_007151.
FT   VARIANT     102    102       D -> N (in ALS1).
FT                                {ECO:0000269|PubMed:27604643,
FT                                ECO:0000269|PubMed:7870076}.
FT                                /FTId=VAR_007152.
FT   VARIANT     105    105       I -> F (in ALS1; dbSNP:rs121912445).
FT                                {ECO:0000269|PubMed:7501156}.
FT                                /FTId=VAR_008720.
FT   VARIANT     106    106       S -> L (in ALS1).
FT                                /FTId=VAR_013535.
FT   VARIANT     107    107       L -> V (in ALS1; dbSNP:rs121912440).
FT                                /FTId=VAR_007153.
FT   VARIANT     109    109       G -> V (in ALS1).
FT                                /FTId=VAR_013536.
FT   VARIANT     112    112       C -> Y (in ALS1).
FT                                {ECO:0000269|PubMed:27604643}.
FT                                /FTId=VAR_077327.
FT   VARIANT     113    113       I -> M (in ALS1).
FT                                /FTId=VAR_013537.
FT   VARIANT     113    113       I -> T (in ALS1; dbSNP:rs74315452).
FT                                {ECO:0000269|PubMed:7951252,
FT                                ECO:0000269|PubMed:8528216}.
FT                                /FTId=VAR_007154.
FT   VARIANT     114    114       I -> T (in ALS1; destabilizes dimeric
FT                                protein structure and increases tendency
FT                                to form fibrillar aggregates;
FT                                dbSNP:rs121912441).
FT                                {ECO:0000269|PubMed:10400992,
FT                                ECO:0000269|PubMed:10732812,
FT                                ECO:0000269|PubMed:15056757,
FT                                ECO:0000269|PubMed:7997024,
FT                                ECO:0000269|PubMed:8528216}.
FT                                /FTId=VAR_007155.
FT   VARIANT     115    115       G -> A (in ALS1).
FT                                /FTId=VAR_013538.
FT   VARIANT     116    116       R -> G (in ALS1).
FT                                {ECO:0000269|PubMed:7881433}.
FT                                /FTId=VAR_007156.
FT   VARIANT     119    119       V -> L (in ALS1).
FT                                {ECO:0000269|PubMed:14506936}.
FT                                /FTId=VAR_045883.
FT   VARIANT     119    119       V -> VFLQ (in ALS1).
FT                                /FTId=VAR_008721.
FT   VARIANT     125    125       D -> G (in ALS1).
FT                                {ECO:0000269|PubMed:14506936}.
FT                                /FTId=VAR_045884.
FT   VARIANT     125    125       D -> V (in ALS1).
FT                                {ECO:0000269|PubMed:8938700}.
FT                                /FTId=VAR_008722.
FT   VARIANT     126    126       D -> H (in ALS1).
FT                                {ECO:0000269|PubMed:8528216}.
FT                                /FTId=VAR_007157.
FT   VARIANT     127    127       L -> S (in ALS1).
FT                                {ECO:0000269|PubMed:11535232}.
FT                                /FTId=VAR_013539.
FT   VARIANT     134    134       Missing (in ALS).
FT                                {ECO:0000269|PubMed:8938700}.
FT                                /FTId=VAR_008723.
FT   VARIANT     135    135       S -> N (in ALS1; reduced metal binding;
FT                                increases tendency to form fibrillar
FT                                aggregates; dbSNP:rs121912451).
FT                                {ECO:0000269|PubMed:12754496,
FT                                ECO:0000269|PubMed:8990014}.
FT                                /FTId=VAR_007158.
FT   VARIANT     140    140       N -> K (in ALS1).
FT                                /FTId=VAR_007159.
FT   VARIANT     145    145       L -> F (in ALS1).
FT                                {ECO:0000269|PubMed:18301754}.
FT                                /FTId=VAR_007160.
FT   VARIANT     145    145       L -> S (in ALS1; dbSNP:rs121912446).
FT                                {ECO:0000269|PubMed:7496169}.
FT                                /FTId=VAR_008724.
FT   VARIANT     146    146       A -> T (in ALS1; dbSNP:rs121912447).
FT                                {ECO:0000269|PubMed:7496169}.
FT                                /FTId=VAR_008725.
FT   VARIANT     147    147       C -> R (in ALS1).
FT                                /FTId=VAR_013540.
FT   VARIANT     148    148       G -> R (in ALS1).
FT                                {ECO:0000269|PubMed:14506936}.
FT                                /FTId=VAR_045885.
FT   VARIANT     149    149       V -> G (in ALS1).
FT                                /FTId=VAR_007161.
FT   VARIANT     149    149       V -> I (in ALS1; dbSNP:rs567511139).
FT                                {ECO:0000269|PubMed:7795609}.
FT                                /FTId=VAR_007162.
FT   VARIANT     150    150       I -> T (in ALS1).
FT                                {ECO:0000269|PubMed:8528216}.
FT                                /FTId=VAR_007163.
FT   VARIANT     152    152       I -> T (in ALS1; dbSNP:rs121912449).
FT                                {ECO:0000269|PubMed:8682505}.
FT                                /FTId=VAR_007164.
FT   MUTAGEN       7      7       C->S: Enhances formation of fibrillar
FT                                aggregates in the absence of bound zinc;
FT                                when associated with S-58; S-112 and S-
FT                                147. {ECO:0000269|PubMed:17070542,
FT                                ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:22496122}.
FT   MUTAGEN       7      7       C->S: No palmitoylation, reduced nuclear
FT                                targeting. {ECO:0000269|PubMed:17070542,
FT                                ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:22496122}.
FT   MUTAGEN      51     52       FG->EE: Abolishes dimerization; when
FT                                associated with Q-134.
FT                                {ECO:0000269|PubMed:10329151,
FT                                ECO:0000269|PubMed:18552350}.
FT   MUTAGEN      58     58       C->A: Exhibits very slow copper
FT                                acquisition.
FT                                {ECO:0000269|PubMed:17070542,
FT                                ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:23625804}.
FT   MUTAGEN      58     58       C->S: Enhances formation of fibrillar
FT                                aggregates in the absence of bound zinc;
FT                                when associated with S-7; S-112 and S-
FT                                147. {ECO:0000269|PubMed:17070542,
FT                                ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:23625804}.
FT   MUTAGEN      81     81       H->A: Loss of zinc binding and enhanced
FT                                tendency to form aggregates; when
FT                                associated with A-84.
FT                                {ECO:0000269|PubMed:17888947,
FT                                ECO:0000269|PubMed:18552350}.
FT   MUTAGEN      81     81       H->S: Destabilization of dimer and loss
FT                                of zinc binding; when associated with S-
FT                                84. {ECO:0000269|PubMed:17888947,
FT                                ECO:0000269|PubMed:18552350}.
FT   MUTAGEN      84     84       D->A: Loss of zinc binding and enhanced
FT                                tendency to form aggregates; when
FT                                associated with A-81.
FT                                {ECO:0000269|PubMed:17888947,
FT                                ECO:0000269|PubMed:18552350}.
FT   MUTAGEN      84     84       D->S: Destabilization of dimer and loss
FT                                of zinc binding; when associated with S-
FT                                81. {ECO:0000269|PubMed:17888947,
FT                                ECO:0000269|PubMed:18552350}.
FT   MUTAGEN     112    112       C->S: Enhances formation of fibrillar
FT                                aggregates in the absence of bound zinc;
FT                                when associated with S-7; S-58 and S-147.
FT                                {ECO:0000269|PubMed:17070542,
FT                                ECO:0000269|PubMed:18552350}.
FT   MUTAGEN     123    123       K->A: Deacreased succinylation.
FT                                {ECO:0000269|PubMed:24140062}.
FT   MUTAGEN     123    123       K->E: Mimicks constitutive succinylation
FT                                state; decreased activity.
FT                                {ECO:0000269|PubMed:24140062}.
FT   MUTAGEN     134    134       E->Q: Abolishes dimerization; when
FT                                associated with E-50 and E-51.
FT                                {ECO:0000269|PubMed:10329151}.
FT   MUTAGEN     147    147       C->A: Exhibits very slow copper
FT                                acquisition.
FT                                {ECO:0000269|PubMed:17070542,
FT                                ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:23625804}.
FT   MUTAGEN     147    147       C->S: Enhances formation of fibrillar
FT                                aggregates in the absence of bound zinc;
FT                                when associated with S-7; S-58 and S-112.
FT                                {ECO:0000269|PubMed:17070542,
FT                                ECO:0000269|PubMed:18552350,
FT                                ECO:0000269|PubMed:23625804}.
FT   CONFLICT     18     18       I -> S (in Ref. 3; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT     99     99       S -> V (in Ref. 3; no nucleotide entry).
FT                                {ECO:0000305}.
FT   STRAND        3     10       {ECO:0000244|PDB:4A7U}.
FT   STRAND       12     14       {ECO:0000244|PDB:4A7U}.
FT   STRAND       16     25       {ECO:0000244|PDB:4A7U}.
FT   STRAND       26     28       {ECO:0000244|PDB:1RK7}.
FT   STRAND       30     38       {ECO:0000244|PDB:4A7U}.
FT   STRAND       41     50       {ECO:0000244|PDB:4A7U}.
FT   STRAND       51     53       {ECO:0000244|PDB:2NAM}.
FT   HELIX        54     56       {ECO:0000244|PDB:1BA9}.
FT   HELIX        58     61       {ECO:0000244|PDB:4A7U}.
FT   STRAND       63     65       {ECO:0000244|PDB:1KMG}.
FT   STRAND       67     69       {ECO:0000244|PDB:1KMG}.
FT   STRAND       74     76       {ECO:0000244|PDB:1RK7}.
FT   STRAND       77     79       {ECO:0000244|PDB:1MFM}.
FT   TURN         80     82       {ECO:0000244|PDB:2MP3}.
FT   STRAND       84     90       {ECO:0000244|PDB:4A7U}.
FT   HELIX        92     94       {ECO:0000244|PDB:1SPD}.
FT   STRAND       96    104       {ECO:0000244|PDB:4A7U}.
FT   STRAND      106    108       {ECO:0000244|PDB:4A7U}.
FT   HELIX       109    111       {ECO:0000244|PDB:4A7U}.
FT   STRAND      112    115       {ECO:0000244|PDB:2AF2}.
FT   STRAND      116    123       {ECO:0000244|PDB:4A7U}.
FT   STRAND      127    129       {ECO:0000244|PDB:2LU5}.
FT   STRAND      130    132       {ECO:0000244|PDB:4A7U}.
FT   HELIX       133    136       {ECO:0000244|PDB:4A7U}.
FT   TURN        138    140       {ECO:0000244|PDB:1AZV}.
FT   STRAND      143    149       {ECO:0000244|PDB:4A7U}.
FT   STRAND      151    153       {ECO:0000244|PDB:2C9S}.
SQ   SEQUENCE   154 AA;  15936 MW;  25CA38DA8D564483 CRC64;
     MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS
     AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV
     HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ
//
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Ontology (88)   
   GO (88)   
Disease (2)   
   OMIM (2)   
Drug (7)   
   DrugBank (6)   
   CHEMBL-UP (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (8)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   HGNC (1)   
   ENSEMBL-UP (3)   
Protein sequence (167)   
   RefSeq(pep) (1)   
   PMD (166)   
DNA sequence (25)   
   EMBL (25)   
3D Structure (96)   
   PDB (96)   
Protein domain (5)   
   InterPro (2)   
   Pfam (1)   
   PROSITE (2)   
DNA domain (1)   
   EPD (1)   
Literature (79)   
   PubMed (79)   
Enzyme (1)   
   BRENDA (1)   
All databases (480)   

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ID   V9HWC9_HUMAN            Unreviewed;       154 AA.
AC   V9HWC9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-SEP-2017, entry version 28.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=HEL-S-44 {ECO:0000313|EMBL:ACJ13715.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:ACJ13715.1};
RN   [1] {ECO:0000313|EMBL:ACJ13715.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Li J.Y., Wang H.Y., Liu F.J., Liu J.;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; EU794661; ACJ13715.1; -; mRNA.
DR   RefSeq; NP_000445.1; NM_000454.4.
DR   UniGene; Hs.443914; -.
DR   ProteinModelPortal; V9HWC9; -.
DR   SMR; V9HWC9; -.
DR   MaxQB; V9HWC9; -.
DR   PaxDb; V9HWC9; -.
DR   GeneID; 6647; -.
DR   KEGG; hsa:6647; -.
DR   UCSC; uc002ypa.4; human.
DR   CTD; 6647; -.
DR   EuPathDB; HostDB:ENSG00000142168.14; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   PhylomeDB; V9HWC9; -.
DR   ChiTaRS; SOD1; human.
DR   GenomeRNAi; 6647; -.
DR   Bgee; ENSG00000142168; -.
DR   ExpressionAtlas; V9HWC9; baseline and differential.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0031045; C:dense core granule; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR   GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; IEA:Ensembl.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl.
DR   GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR   GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
DR   GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
DR   GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15936 MW;  25CA38DA8D564483 CRC64;
     MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS
     AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV
     HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ
//
  All links  
Ontology (52)   
   GO (52)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (2)   
   Pfam (1)   
   PROSITE (2)   
All databases (64)   

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