ID SODC_HUMAN Reviewed; 154 AA. AC P00441; A6NHJ0; D3DSE4; Q16669; Q16711; Q16838; Q16839; Q16840; Q6NR85; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 269. DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000305}; DE EC=1.15.1.1 {ECO:0000269|PubMed:24140062}; DE AltName: Full=Superoxide dismutase 1; DE Short=hSod1; GN Name=SOD1 {ECO:0000312|HGNC:HGNC:11179}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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; DOI=10.1002/j.1460-2075.1985.tb02320.x; 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 21 RT 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., Steimer K.S., RA Mullenbach G.T.; RT "Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising RT high levels of active or inactive enzyme from an 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 copper- RT 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 peripheral RT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA 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 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., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 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 ALS1 RP 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., Brockmueller J., RA Ray-Chaudhuri K., Radunovic A., Shaw C., Wilkinson J., King A., Swash M., RA Leigh P.N., de Belleroche J., Powell J.; RT "Two novel mutations in the gene for copper zinc superoxide dismutase in UK RT 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 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 of RT 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 status."; RL J. Biol. Chem. 279:47998-48003(2004). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY RP 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 MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA 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 dimerization of RT human superoxide dismutase 1 during its bicarbonate-dependent peroxidase RT activity."; RL Free Radic. Biol. Med. 49:1046-1053(2010). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY RP 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT 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., Buerckstuemmer T., RA 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 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., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [29] RP SUCCINYLATION AT LYS-123, DESUCCINYLATION BY SIRT5, MUTAGENESIS OF LYS-123, RP CATALYTIC ACTIVITY, AND FUNCTION. 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 of RT Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT 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 SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA 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 INTERACTION WITH DAOA. RX PubMed=30037290; DOI=10.1080/10715762.2018.1504293; RA Wang M., Saw H.P., Cui F.F., Lin S.Y., Chang H.T., Chiu C.D.; RT "pLG72 induces superoxide radicals via interaction and aggregation with RT SOD1."; RL Free Radic. Res. 52:970-976(2018). RN [34] RP INTERACTION WITH CCS, AND SUBUNIT. RX PubMed=31292775; DOI=10.1007/s10534-019-00206-3; RA Skopp A., Boyd S.D., Ullrich M.S., Liu L., Winkler D.D.; RT "Copper-zinc superoxide dismutase (Sod1) activation terminates interaction RT between its copper chaperone (Ccs) and the cytosolic metal-binding domain RT of the copper importer Ctr1."; RL BioMetals 32:695-705(2019). RN [35] RP INVOLVEMENT IN STAHP. RX PubMed=31332433; DOI=10.1093/brain/awz182; RA Park J.H., Elpers C., Reunert J., McCormick M.L., Mohr J., Biskup S., RA Schwartz O., Rust S., Grueneberg M., Seelhoefer A., Schara U., RA Boltshauser E., Spitz D.R., Marquardt T.; RT "SOD1 deficiency: a novel syndrome distinct from amyotrophic lateral RT sclerosis."; RL Brain 142:2230-2237(2019). RN [36] RP INVOLVEMENT IN STAHP. RX PubMed=31314961; DOI=10.1056/nejmc1905039; RA Andersen P.M., Nordstroem U., Tsiakas K., Johannsen J., Volk A.E., RA Bierhals T., Zetterstroem P., Marklund S.L., Hempel M., Santer R.; RT "Phenotype in an Infant with SOD1 Homozygous Truncating Mutation."; RL N. Engl. J. Med. 381:486-488(2019). RN [37] 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 human RT Cu,Zn superoxide dismutase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6109-6113(1992). RN [38] 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 CuZnSOD RT mutant found in familial amyotrophic lateral sclerosis."; RL Protein Sci. 7:545-555(1998). RN [39] 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 superoxide RT dismutase (SOD). Why is SOD a dimeric enzyme?"; RL Biochemistry 37:11780-11791(1998). RN [40] RP X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF MUTANT GLU-51/GLU-52/GLN-134, RP SUBUNIT, AND MUTAGENESIS OF 51-PHE-GLY-52 AND 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 F50E/G51E/E133Q at RT atomic resolution. The enzyme mechanism revisited."; RL J. Mol. Biol. 288:413-426(1999). RN [41] 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 ions RT in protein folding."; RL Biochemistry 42:9543-9553(2003). RN [42] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS, RP DISULFIDE BOND, SUBUNIT, AND CHARACTERIZATION OF VARIANTS ALS1 VAL-5 AND RP 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., Kassmann C.J., RA Lo T.P., Bruns C.K., Powers E.T., Kelly J.W., 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 [43] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANTS ALS1 ASN-135 AND ARG-47, RP 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., Yeates T.O., RA Hart P.J.; RT "Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant RT proteins linked to familial ALS."; RL Nat. Struct. Biol. 10:461-467(2003). RN [44] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF VARIANTS ALS1 VAL-5 AND THR-114, RP 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., Doucette P.A., RA Rodriguez J.A., Whitson L.J., Hart P.J., Hayward L.J., Valentine J.S., RA 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 [45] 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 of RT copper-depleted, disulfide-reduced form."; RL J. Biol. Chem. 281:2333-2337(2006). RN [46] RP X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEXES WITH COPPER AND ZINC RP 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., Valentine J.S., RA 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 enzymes."; RL J. Mol. Biol. 356:1152-1162(2006). RN [47] 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; CYS-112 AND RP 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 interface RT strength in Cu/Zn superoxide dismutase."; RL J. Mol. Biol. 365:333-342(2007). RN [48] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT SER-81/SER-84 IN COMPLEX RP WITH COPPER IONS, SUBUNIT, MUTAGENESIS OF HIS-81 AND ASP-84, 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 dismutase RT and implications for ALS."; RL J. Mol. Biol. 373:877-890(2007). RN [49] RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC RP IONS, SUBUNIT, AND FORMATION OF FIBRILLAR AGGREGATES BY ZINC-DEPLETED 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 structural RT fluctuations that may lead to polymerization of human Cu-Zn superoxide RT dismutase."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10040-10044(2007). RN [50] 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 lateral RT sclerosis."; RL J. Biol. Chem. 283:16169-16177(2008). RN [51] 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 (P21)."; RL Submitted (APR-2008) to the PDB data bank. RN [52] 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): a RT review of current developments."; RL J. Med. Genet. 32:841-847(1995). RN [53] 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 [54] RP VARIANTS ALS1 ARG-38; VAL-39; ASP-42; SER-42; ARG-44; ARG-86; ALA-94; RP CYS-94; GLY-101; VAL-107 AND THR-114. RX PubMed=8446170; DOI=10.1038/362059a0; RA Rosen D.R., Siddique T., Patterson D., Figlewicz D.A., Sapp P., Hentati A., RA Donaldson D., Goto J., O'Regan J.P., Deng H.-X., Rahmani Z., Krizus A., RA McKenna-Yasek D., Cayabyab A., Gaston S.M., Berger R., Tanzi R.E., RA Halperin J.J., Herzfeldt B., van den Bergh R., Hung W.-Y., Bird T., RA Deng G., Mulder D.W., Smyth C., Laing N.G., Soriano E., Pericak-Vance M.A., RA Haines J., Rouleau G.A., Gusella J.S., Horvitz H.R., Brown R.H. Jr.; RT "Mutations in Cu/Zn superoxide dismutase gene are associated with familial RT amyotrophic lateral sclerosis."; RL Nature 362:59-62(1993). RN [55] RP ERRATUM OF PUBMED:8446170. RX PubMed=8332197; DOI=10.1038/364362c0; RA Rosen D.R.; RL Nature 364:362-362(1993). RN [56] RP VARIANTS ALS1 VAL-5; ARG-38; VAL-39; ASP-42; SER-42; ARG-44; ARG-86; RP ALA-94; CYS-94; GLY-101; VAL-107; THR-114; PHE-145 AND GLY-149. RX PubMed=8351519; DOI=10.1126/science.8351519; RA Deng H.-X., Hentati A., Tainer J.A., Iqbal Z., Cayabyab A., Hung W.-Y., RA Getzoff E.D., Hu P., Herzfeldt B., Roos R.P., Warner C., Deng G., RA Soriano E., Smyth C., Parge H.E., Ahmed A., Roses A.D., Hallewell R.A., RA Pericak-Vance M.A., Siddique T.; RT "Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide RT dismutase."; RL Science 261:1047-1051(1993). RN [57] 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 familial RT amyotrophic lateral sclerosis."; RL Biochem. Biophys. Res. Commun. 200:695-703(1994). RN [58] 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 amyotrophic RT lateral sclerosis."; RL Biochem. Biophys. Res. Commun. 204:572-577(1994). RN [59] 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 in RT three others."; RL Hum. Mol. Genet. 3:649-650(1994). RN [60] 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 gene RT for Cu/Zn superoxide dismutase in patients with amyotrophic lateral RT sclerosis."; RL Hum. Mol. Genet. 3:997-998(1994). RN [61] 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 the RT Cu/Zn superoxide dismutase-1 gene."; RL Hum. Mol. Genet. 3:2261-2262(1994). RN [62] 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., Itoyama Y., RA Abe K.; RT "Familial amyotrophic lateral sclerosis (ALS) in Japan associated with H46R RT mutation in Cu/Zn superoxide dismutase gene: a possible new subtype of RT familial ALS."; RL J. Neurol. Sci. 126:77-83(1994). RN [63] 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 [64] 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 amyotrophic RT lateral sclerosis patient."; RL Mol. Cell. Probes 8:329-330(1994). RN [65] RP VARIANTS ALS1 VAL-5; ARG-38; THR-114; LYS-140; PHE-145 AND THR-150. RX PubMed=7887412; RA Pramatarova A., Figlewicz D.A., Krizus A., Han F.Y., Ceballos-Picot I., RA Nicole A., Dib M., Meininger V., Brown R.H. Jr., Rouleau G.A.; RT "Identification of new mutations in the Cu/Zn superoxide dismutase gene of RT patients with familial amyotrophic lateral sclerosis."; RL Am. J. Hum. Genet. 56:592-596(1995). RN [66] 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., Shoji M., RA Hirai S., Itoyama Y.; RT "A novel point mutation in the Cu/Zn superoxide dismutase gene in a patient RT with familial amyotrophic lateral sclerosis."; RL Hum. Mol. Genet. 4:491-492(1995). RN [67] 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 new RT mutation in exon 4."; RL Hum. Mol. Genet. 4:1101-1104(1995). RN [68] 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., Siddique T.; RT "The D90A mutation results in a polymorphism of Cu,Zn superoxide dismutase RT that is prevalent in northern Sweden and Finland."; RL Hum. Mol. Genet. 4:1105-1108(1995). RN [69] 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 lateral RT sclerosis."; RL Hum. Mol. Genet. 4:1113-1116(1995). RN [70] 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 [71] 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., Tarvainen I., RA Haltia T., Nilsson L., Binzer M., Forsgren L., Marklund S.L.; RT "Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala RT mutation in CuZn-superoxide dismutase."; RL Nat. Genet. 10:61-66(1995). RN [72] 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 with RT a novel point mutation in the Cu/Zn superoxide dismutase gene."; RL Neurology 45:2038-2042(1995). RN [73] 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 superoxide RT dismutase in patients with familial amyotrophic lateral sclerosis."; RL Neuromuscul. Disord. 5:353-357(1995). RN [74] RP VARIANTS ALS1 LYS-101 AND ARG-147. RX PubMed=8875253; DOI=10.1093/hmg/5.supplement_1.1465; RA Siddique T., Deng H.X.; RT "Genetics of amyotrophic lateral sclerosis."; RL Hum. Mol. Genet. 5:1465-1470(1996). RN [75] 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., Yeung L., RA Cherryson A.K., Dench J.E., Wilton S.D., Laing N.G., Horvitz R.H., RA Brown R.H. Jr.; RT "Three novel mutations and two variants in the gene for Cu/Zn superoxide RT dismutase in familial amyotrophic lateral sclerosis."; RL Neuromuscul. Disord. 6:361-366(1996). RN [76] 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 [77] RP VARIANTS ALS1 VAL-5; GLY-15; TYR-77 AND ALA-91. RX PubMed=9365366; DOI=10.1093/brain/120.10.1723; RA Andersen P.M., Nilsson P., Keraenen M.L., Forsgren L., Haegglund J., RA Karlsborg M., Ronnevi L.O., Gredal O., Marklund S.L.; RT "Phenotypic heterogeneity in motor neuron disease patients with CuZn- RT superoxide dismutase mutations in Scandinavia."; RL Brain 120:1723-1737(1997). RN [78] RP VARIANT ALS1 VAL-109. RX PubMed=24283821; DOI=10.1111/j.1468-1331.1997.tb00298.x; RA Orrell R.W., Habgood J.J., Shepherd D.I., Donnai D., de Belleroche J.; RT "A novel mutation of SOD-1 (Gly 108 Val) in familial amyotrophic lateral RT sclerosis."; RL Eur. J. Neurol. 4:48-51(1997). RN [79] 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 dismutase RT gene in a patient with familial motor neuron disease."; RL Hum. Mutat. 9:69-71(1997). RN [80] 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 [81] 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 novel RT mutation in exon 3 (Gly72Ser)."; RL J. Neurol. Sci. 153:46-49(1997). RN [82] 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 lateral RT sclerosis from the Kii Peninsula and its vicinity, Japan."; RL Neurogenetics 1:113-115(1997). RN [83] 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 [84] RP VARIANTS ALS1 GLY-22; ARG-39; LYS-50; ARG-68 AND PHE-85. RX PubMed=9706719; DOI=10.1017/s0317167100034004; RA Boukaftane Y., Khoris J., Moulard B., Salachas F., Meininger V., RA Malafosse A., Camu W., Rouleau G.A.; RT "Identification of six novel SOD1 gene mutations in familial amyotrophic RT lateral sclerosis."; RL Can. J. Neurol. Sci. 25:192-196(1998). RN [85] RP VARIANT ALS1 VAL-91. RX DOI=10.1046/j.1468-1331.1998.540389.x; RA Morita M., Abe K., Takahashi M., Onodera Y., Okumura H., Niino M., RA Tashiro K., Nakano I., Itoyama Y.; RT "A novel mutation Asp90Val in the SOD1 gene associated with Japanese RT familial ALS."; RL Eur. J. Neurol. 5:389-392(1998). RN [86] RP VARIANT ALS1 SER-5. RX PubMed=9696308; DOI=10.1016/s0165-0270(98)00012-0; RA Nakanishi T., Kishikawa M., Miyazaki A., Shimizu A., Ogawa Y., Sakoda S., RA Ohi T., Shoji H.; RT "Simple and defined method to detect the SOD-1 mutants from patients with RT familial amyotrophic lateral sclerosis by mass spectrometry."; RL J. Neurosci. Methods 81:41-44(1998). RN [87] RP CHARACTERIZATION OF VARIANTS ALS1 VAL-5; ARG-38; ARG-47; GLN-49; ARG-86 AND RP 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 superoxide RT dismutase 1 enzymes and the rate of disease progression in familial RT amyotrophic lateral sclerosis kindreds."; RL Hum. Mol. Genet. 8:1451-1460(1999). RN [88] 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., Bugiani O., RA Ajmar F., Garre C.; RT "A SOD1 gene mutation in a patient with slowly progressing familial ALS."; RL Neurology 53:404-406(1999). RN [89] RP ERRATUM OF PUBMED:10430435. RA Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M., Bugiani O., RA Ajmar F., Garre C.; RL Neurology 57:1146-1146(2001). RN [90] 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 [91] 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., Testa D., RA Casali C., Taroni F., Di Donato S., Zeviani M., Mariotti C.; RT "Superoxide dismutase gene mutations in Italian patients with familial and RT sporadic amyotrophic lateral sclerosis: identification of three novel RT missense mutations."; RL Neuromuscul. Disord. 11:404-410(2001). RN [92] RP VARIANT ALS1 ARG-81. RX PubMed=12402272; DOI=10.1002/ana.10369; RA Alexander M.D., Traynor B.J., Miller N., Corr B., Frost E., McQuaid S., RA 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 [93] 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 [94] RP VARIANTS ALS1 ARG-38; SER-66 AND MET-113. RX PubMed=12210393; DOI=10.1002/mus.10193; RA Garcia-Redondo A., Bustos F., Juan Y Seva B., Del Hoyo P., Jimenez S., RA Campos Y., Martin M.A., Rubio J.C., Canadillas F., Arenas J., Esteban J.; RT "Molecular analysis of the superoxide dismutase 1 gene in Spanish patients RT with sporadic or familial amyotrophic lateral sclerosis."; RL Muscle Nerve 26:274-278(2002). RN [95] RP VARIANTS ALS1 VAL-9; CYS-21; LEU-23; ARG-49; ARG-55; ALA-88; THR-90; RP MET-98; LEU-106; ALA-115; 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., Seltzer W., RA 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 [96] RP CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-86 AND ARG-94, MUTAGENESIS OF RP CYS-7; 51-PHE-GLY-52; CYS-58; HIS-81; ASP-84; CYS-112 AND CYS-147, AND RP 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 [97] RP CHARACTERIZATION OF VARIANTS ALS1 ARG-55; ALA-91; ALA-94; ASP-94; MET-98 RP AND PHE-145. RX PubMed=18301754; DOI=10.1371/journal.pone.0001677; RA Banci L., Bertini I., Boca M., Girotto S., Martinelli M., Valentine J.S., RA Vieru M.; RT "SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization."; RL PLoS ONE 3:E1677-E1677(2008). RN [98] 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., Inatome R., RA 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 [99] RP VARIANTS ALS1 ALA-91 AND LYS-101. RX PubMed=20460594; DOI=10.1136/jnnp.2009.192310; RA Felbecker A., Camu W., Valdmanis P.N., Sperfeld A.D., Waibel S., RA Steinbach P., Rouleau G.A., Ludolph A.C., Andersen P.M.; RT "Four familial ALS pedigrees discordant for two SOD1 mutations: are all RT SOD1 mutations pathogenic?"; RL J. Neurol. Neurosurg. Psych. 81:572-577(2010). RN [100] 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., Marangi G., RA 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 [101] 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., Floris G., RA Cannas A., Parish L.D., Cossu P., Abramzon Y., Johnson J.O., Nalls M.A., RA Arepalli S., Chong S., Hernandez D.G., Traynor B.J., Restagno G.; RT "Large proportion of amyotrophic lateral sclerosis cases in Sardinia due to RT a single founder mutation of the TARDBP gene."; RL Arch. Neurol. 68:594-598(2011). RN [102] 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). RN [103] RP VARIANT ALS1 VAL-90. RX PubMed=31086828; DOI=10.1212/nxg.0000000000000335; RA Kuuluvainen L., Kaivola K., Moenkaere S., Laaksovirta H., Jokela M., RA Udd B., Valori M., Pasanen P., Paetau A., Traynor B.J., Stone D.J., RA Schleutker J., Poeyhoenen M., Tienari P.J., Myllykangas L.; RT "Oligogenic basis of sporadic ALS: The example of SOD1 p.Ala90Val RT mutation."; RL Neurol. Genet. 5:e335-e335(2019). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC {ECO:0000269|PubMed:24140062}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:18421; EC=1.15.1.1; CC Evidence={ECO:0000269|PubMed:24140062}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000269|PubMed:17888947}; CC Note=Binds 1 copper ion per subunit. {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 (By similarity). CC Homodimerization may take place via the ditryptophan cross-link at Trp- CC 33. Heterodimer with SOD1 (PubMed:31292775). The heterodimer CCS:SOD1 CC interacts with SLC31A1; this heterotrimer is Cu(1+)-mediated and its CC maintenance is regulated through SOD1 activation (PubMed:31292775). CC Interacts with DAOA; the interaction is direct (PubMed:30037290). CC {ECO:0000250|UniProtKB:P08228, 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, ECO:0000269|PubMed:30037290, CC ECO:0000269|PubMed:31292775}. CC -!- INTERACTION: CC P00441; P13928: ANXA8; NbExp=3; IntAct=EBI-990792, EBI-2556915; CC P00441; P63010-2: AP2B1; NbExp=3; IntAct=EBI-990792, EBI-11529439; CC P00441; Q0P5N6: ARL16; NbExp=3; IntAct=EBI-990792, EBI-10186132; CC P00441; Q16611: BAK1; NbExp=3; IntAct=EBI-990792, EBI-519866; CC P00441; P10415: BCL2; NbExp=3; IntAct=EBI-990792, EBI-77694; CC P00441; Q5SZD1: C6orf141; NbExp=3; IntAct=EBI-990792, EBI-10697767; CC P00441; P02748: C9; NbExp=3; IntAct=EBI-990792, EBI-6677628; CC P00441; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-990792, EBI-25850646; CC P00441; Q13191: CBLB; NbExp=3; IntAct=EBI-990792, EBI-744027; CC P00441; O14618: CCS; NbExp=4; IntAct=EBI-990792, EBI-11668690; CC P00441; P53672: CRYBA2; NbExp=3; IntAct=EBI-990792, EBI-750444; CC P00441; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-990792, EBI-9087876; CC P00441; P98082: DAB2; NbExp=3; IntAct=EBI-990792, EBI-1171238; CC P00441; Q8TCX1: DYNC2LI1; NbExp=3; IntAct=EBI-990792, EBI-8568003; CC P00441; P29692: EEF1D; NbExp=3; IntAct=EBI-990792, EBI-358607; CC P00441; Q8TC29: ENKUR; NbExp=3; IntAct=EBI-990792, EBI-9246952; CC P00441; P02671-2: FGA; NbExp=3; IntAct=EBI-990792, EBI-9640259; CC P00441; Q8WW76: FGA; NbExp=3; IntAct=EBI-990792, EBI-16467458; CC P00441; F2Z2M7: GALNT10; NbExp=3; IntAct=EBI-990792, EBI-23893155; CC P00441; P04406: GAPDH; NbExp=3; IntAct=EBI-990792, EBI-354056; CC P00441; P62879: GNB2; NbExp=3; IntAct=EBI-990792, EBI-356942; CC P00441; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-990792, EBI-347538; CC P00441; Q8WVV9-3: HNRNPLL; NbExp=3; IntAct=EBI-990792, EBI-25845242; CC P00441; P09017: HOXC4; NbExp=3; IntAct=EBI-990792, EBI-3923226; CC P00441; P80217-2: IFI35; NbExp=3; IntAct=EBI-990792, EBI-12823003; CC P00441; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-990792, EBI-21911304; CC P00441; O14713: ITGB1BP1; NbExp=3; IntAct=EBI-990792, EBI-2127319; CC P00441; Q15046: KARS1; NbExp=3; IntAct=EBI-990792, EBI-356367; CC P00441; Q9NVX7-2: KBTBD4; NbExp=3; IntAct=EBI-990792, EBI-25871195; CC P00441; Q8N4N3-2: KLHL36; NbExp=3; IntAct=EBI-990792, EBI-10973851; CC P00441; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-990792, EBI-11985629; CC P00441; Q9BYZ2: LDHAL6B; NbExp=3; IntAct=EBI-990792, EBI-1108377; CC P00441; Q8N448: LNX2; NbExp=3; IntAct=EBI-990792, EBI-2340947; CC P00441; O95777: LSM8; NbExp=3; IntAct=EBI-990792, EBI-347779; CC P00441; Q8TDB4: MGARP; NbExp=3; IntAct=EBI-990792, EBI-4397720; CC P00441; A4FUJ8: MKL1; NbExp=3; IntAct=EBI-990792, EBI-21250407; CC P00441; Q8N594: MPND; NbExp=3; IntAct=EBI-990792, EBI-2512452; CC P00441; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-990792, EBI-1058491; CC P00441; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-990792, EBI-25830200; CC P00441; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-990792, EBI-10302990; CC P00441; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-990792, EBI-716063; CC P00441; Q08209-2: PPP3CA; NbExp=3; IntAct=EBI-990792, EBI-11959013; CC P00441; P30044: PRDX5; NbExp=10; IntAct=EBI-990792, EBI-722161; CC P00441; P28062-2: PSMB8; NbExp=3; IntAct=EBI-990792, EBI-372312; CC P00441; P62191: PSMC1; NbExp=5; IntAct=EBI-990792, EBI-357598; CC P00441; P17980: PSMC3; NbExp=3; IntAct=EBI-990792, EBI-359720; CC P00441; P43686-2: PSMC4; NbExp=3; IntAct=EBI-990792, EBI-21522939; CC P00441; Q09028: RBBP4; NbExp=3; IntAct=EBI-990792, EBI-620823; CC P00441; Q6ZNA4-2: RNF111; NbExp=3; IntAct=EBI-990792, EBI-21535400; CC P00441; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-990792, EBI-25829984; CC P00441; Q9NV58: RNF19A; NbExp=3; IntAct=EBI-990792, EBI-1390270; CC P00441; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-990792, EBI-366570; CC P00441; P08865: RPSA; NbExp=3; IntAct=EBI-990792, EBI-354112; CC P00441; Q8N488: RYBP; NbExp=3; IntAct=EBI-990792, EBI-752324; CC P00441; P60896: SEM1; NbExp=3; IntAct=EBI-990792, EBI-79819; CC P00441; Q15393: SF3B3; NbExp=3; IntAct=EBI-990792, EBI-346977; CC P00441; Q2NKQ1-4: SGSM1; NbExp=3; IntAct=EBI-990792, EBI-10182463; CC P00441; Q9GZS3: SKIC8; NbExp=3; IntAct=EBI-990792, EBI-358545; CC P00441; P37840: SNCA; NbExp=9; IntAct=EBI-990792, EBI-985879; CC P00441; P00441: SOD1; NbExp=22; IntAct=EBI-990792, EBI-990792; CC P00441; Q3SY56: SP6; NbExp=3; IntAct=EBI-990792, EBI-11175533; CC P00441; Q8NHS9: SPATA22; NbExp=3; IntAct=EBI-990792, EBI-7067260; CC P00441; Q96MF2: STAC3; NbExp=3; IntAct=EBI-990792, EBI-745680; CC P00441; Q92797-2: SYMPK; NbExp=3; IntAct=EBI-990792, EBI-21560407; CC P00441; Q9BZK7: TBL1XR1; NbExp=3; IntAct=EBI-990792, EBI-765729; CC P00441; Q15554-4: TERF2; NbExp=3; IntAct=EBI-990792, EBI-25840535; CC P00441; Q9H3N1: TMX1; NbExp=3; IntAct=EBI-990792, EBI-1051115; CC P00441; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-990792, EBI-2505861; CC P00441; P07951-2: TPM2; NbExp=3; IntAct=EBI-990792, EBI-10977815; CC P00441; P07437: TUBB; NbExp=3; IntAct=EBI-990792, EBI-350864; CC P00441; P0CG47: UBB; NbExp=3; IntAct=EBI-990792, EBI-413034; CC P00441; O75604-3: USP2; NbExp=3; IntAct=EBI-990792, EBI-10696113; CC P00441; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-990792, EBI-2682299; CC P00441; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-990792, EBI-12949277; CC P00441; Q8NBB4-2: ZSCAN1; NbExp=3; IntAct=EBI-990792, EBI-12021938; CC P00441; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-990792, EBI-1538838; CC P00441; P26339: Chga; Xeno; NbExp=5; IntAct=EBI-990792, EBI-990900; CC P00441; P16014: Chgb; Xeno; NbExp=6; IntAct=EBI-990792, EBI-990820; CC P00441; P01041: Cstb; Xeno; NbExp=3; IntAct=EBI-990792, EBI-26602017; CC P00441; P20029: Hspa5; Xeno; NbExp=7; IntAct=EBI-990792, EBI-772325; CC -!- SUBCELLULAR LOCATION: Cytoplasm {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 and CC accumulates in mitochondria. {ECO:0000269|PubMed:19741096}. CC -!- PTM: Unlike wild-type protein, the pathogenic variants ALS1 Arg-38, CC Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A leading to CC their proteasomal degradation. The pathogenic variants ALS1 Arg-86 and CC Ala-94 are ubiquitinated by MARCH5 leading to their proteasomal CC degradation. {ECO:0000269|PubMed:12145308, CC ECO:0000269|PubMed:19741096}. CC -!- PTM: The ditryptophan cross-link at Trp-33 is responsible for the non- CC disulfide-linked homodimerization. Such modification might only occur CC in extreme conditions and additional experimental evidence is required. CC {ECO:0000269|PubMed:20600836}. CC -!- PTM: Palmitoylation helps nuclear targeting and decreases catalytic CC 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 brain CC and lower motor neurons in the brain stem and spinal cord, resulting in CC fatal paralysis. Sensory abnormalities are absent. The pathologic CC hallmarks of the disease include pallor of the corticospinal tract due CC to loss of motor neurons, presence of ubiquitin-positive inclusions CC within surviving motor neurons, and deposition of pathologic CC aggregates. The etiology of amyotrophic lateral sclerosis is likely to CC be multifactorial, involving both genetic and environmental factors. CC The disease is inherited in 5-10% of the cases. CC {ECO:0000269|PubMed:10400992, ECO:0000269|PubMed:10430435, CC ECO:0000269|PubMed:10732812, ECO:0000269|PubMed:11369193, CC ECO:0000269|PubMed:11535232, ECO:0000269|PubMed:12145308, CC ECO:0000269|PubMed:12210393, 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:20460594, ECO:0000269|PubMed:21220647, CC ECO:0000269|PubMed:21247266, ECO:0000269|PubMed:24283821, CC ECO:0000269|PubMed:27604643, ECO:0000269|PubMed:31086828, CC ECO:0000269|PubMed:7496169, ECO:0000269|PubMed:7501156, CC ECO:0000269|PubMed:7647793, ECO:0000269|PubMed:7655468, CC ECO:0000269|PubMed:7655469, ECO:0000269|PubMed:7655471, CC ECO:0000269|PubMed:7700376, ECO:0000269|PubMed:7795609, CC ECO:0000269|PubMed:7836951, ECO:0000269|PubMed:7870076, CC ECO:0000269|PubMed:7881433, ECO:0000269|PubMed:7887412, CC ECO:0000269|PubMed:7951252, ECO:0000269|PubMed:7980516, CC ECO:0000269|PubMed:7997024, ECO:0000269|PubMed:8069312, CC ECO:0000269|PubMed:8179602, ECO:0000269|PubMed:8351519, CC ECO:0000269|PubMed:8446170, ECO:0000269|PubMed:8528216, CC ECO:0000269|PubMed:8682505, ECO:0000269|PubMed:8875253, 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:9365366, CC ECO:0000269|PubMed:9455977, ECO:0000269|PubMed:9541385, CC ECO:0000269|PubMed:9696308, ECO:0000269|PubMed:9706719, CC ECO:0000269|Ref.85}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- DISEASE: Spastic tetraplegia and axial hypotonia, progressive (STAHP) CC [MIM:618598]: An autosomal recessive, neurologic disorder characterized CC by loss of motor abilities in the first year of life, after which CC severe, progressive spastic tetraparesis develops. Affected individuals CC have severe axial hypotonia, hyperekplexia, hypertonia, and myokymia, CC reflecting upper motor neuron involvement. Cognitive development may be CC affected. {ECO:0000269|PubMed:31314961, ECO:0000269|PubMed:31332433}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- MISCELLANEOUS: The protein (both wild-type and ALS1 variants) has a CC tendency to form fibrillar aggregates in the absence of the CC intramolecular disulfide bond or of bound zinc ions. These aggregates CC may have cytotoxic effects. Zinc binding promotes dimerization and CC stabilizes the native form. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC41773.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAA25917.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Alsod; Note=ALS genetic mutations db; CC URL="https://alsod.ac.uk"; 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; -; 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 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; 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; 5IIW; X-ray; 2.00 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; 5O3Y; X-ray; 1.30 A; A/F=2-154. DR PDB; 5O40; X-ray; 1.50 A; A/F=2-154. DR PDB; 5U9M; X-ray; 2.35 A; A/C=2-154. DR PDB; 5WMJ; X-ray; 1.40 A; A/B=31-36. DR PDB; 5WOR; X-ray; 2.77 A; A/B/C/D/E/F/G/H/I/J=29-39. DR PDB; 5YTO; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=1-154. DR PDB; 5YTU; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=1-154. DR PDB; 5YUL; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=1-154. DR PDB; 6A9O; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=1-154. DR PDB; 6B79; X-ray; 1.80 A; A/B=29-39. DR PDB; 6DTK; X-ray; 2.00 A; A/C/E/G/I=1-154. DR PDB; 6FFK; X-ray; 1.94 A; A/B/D/F=2-154. DR PDB; 6FLH; X-ray; 1.79 A; A=2-154. DR PDB; 6FOI; X-ray; 2.00 A; A/D/F/G/I/K/M/O/Q/S/U/W=2-154. DR PDB; 6FOL; X-ray; 2.55 A; B/C/F/G=2-154. DR PDB; 6FON; X-ray; 3.05 A; B/D=2-154. DR PDB; 6FP6; X-ray; 3.00 A; A/C/E/G/I/K/M/O/Q/S/U/W=2-154. DR PDB; 6SPA; X-ray; 1.65 A; A/C/E/G/J/L=2-154. DR PDB; 6SPH; X-ray; 2.25 A; A/C/E/G/J/L=2-154. DR PDB; 6SPI; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-154. DR PDB; 6SPJ; X-ray; 1.97 A; A/B/E/F/I/J=2-154. DR PDB; 6SPK; X-ray; 2.77 A; A/B/E/F/I/J=2-154. DR PDB; 6Z3V; X-ray; 1.25 A; AAA/BBB=2-154. DR PDB; 6Z4G; X-ray; 1.45 A; AAA/BBB=2-154. DR PDB; 6Z4H; X-ray; 1.95 A; AAA/BBB=2-154. DR PDB; 6Z4I; X-ray; 1.60 A; AAA/FFF=2-154. DR PDB; 6Z4J; X-ray; 1.55 A; AAA/BBB=2-154. DR PDB; 6Z4K; X-ray; 1.45 A; AAA/BBB=2-154. DR PDB; 6Z4L; X-ray; 1.60 A; AAA/BBB=2-154. DR PDB; 6Z4M; X-ray; 1.55 A; AAA/BBB=2-154. DR PDB; 6Z4O; X-ray; 1.40 A; AAA/BBB=2-154. DR PDB; 7CJV; NMR; -; A=2-154. DR PDB; 7CJW; NMR; -; A=2-154. DR PDB; 7FB6; X-ray; 1.80 A; A/B=1-154. DR PDB; 7FB9; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-154. DR PDB; 7NXX; X-ray; 2.19 A; A=2-154. DR PDB; 7T8E; X-ray; 1.40 A; A/F=2-154. DR PDB; 7T8F; X-ray; 1.40 A; A/F=2-154. DR PDB; 7T8G; X-ray; 1.35 A; A/F=2-154. DR PDB; 7T8H; X-ray; 1.50 A; A/F=2-154. DR PDB; 7VZF; EM; 2.95 A; A/B/C=1-154. DR PDB; 8GSQ; X-ray; 2.10 A; A/B/C/D/F/I/J=1-154. 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; 4XCR; -. DR PDBsum; 5DLI; -. DR PDBsum; 5IIW; -. DR PDBsum; 5J07; -. DR PDBsum; 5J0C; -. DR PDBsum; 5J0F; -. DR PDBsum; 5J0G; -. DR PDBsum; 5K02; -. DR PDBsum; 5O3Y; -. DR PDBsum; 5O40; -. DR PDBsum; 5U9M; -. DR PDBsum; 5WMJ; -. DR PDBsum; 5WOR; -. DR PDBsum; 5YTO; -. DR PDBsum; 5YTU; -. DR PDBsum; 5YUL; -. DR PDBsum; 6A9O; -. DR PDBsum; 6B79; -. DR PDBsum; 6DTK; -. DR PDBsum; 6FFK; -. DR PDBsum; 6FLH; -. DR PDBsum; 6FOI; -. DR PDBsum; 6FOL; -. DR PDBsum; 6FON; -. DR PDBsum; 6FP6; -. DR PDBsum; 6SPA; -. DR PDBsum; 6SPH; -. DR PDBsum; 6SPI; -. DR PDBsum; 6SPJ; -. DR PDBsum; 6SPK; -. DR PDBsum; 6Z3V; -. DR PDBsum; 6Z4G; -. DR PDBsum; 6Z4H; -. DR PDBsum; 6Z4I; -. DR PDBsum; 6Z4J; -. DR PDBsum; 6Z4K; -. DR PDBsum; 6Z4L; -. DR PDBsum; 6Z4M; -. DR PDBsum; 6Z4O; -. DR PDBsum; 7CJV; -. DR PDBsum; 7CJW; -. DR PDBsum; 7FB6; -. DR PDBsum; 7FB9; -. DR PDBsum; 7NXX; -. DR PDBsum; 7T8E; -. DR PDBsum; 7T8F; -. DR PDBsum; 7T8G; -. DR PDBsum; 7T8H; -. DR PDBsum; 7VZF; -. DR PDBsum; 8GSQ; -. DR AlphaFoldDB; P00441; -. DR BMRB; P00441; -. DR EMDB; EMD-32227; -. DR SMR; P00441; -. DR BioGRID; 112530; 419. DR ComplexPortal; CPX-2897; [Cu-Zn] Superoxide dismutase complex. DR DIP; DIP-44941N; -. DR IntAct; P00441; 337. DR MINT; P00441; -. DR STRING; 9606.ENSP00000270142; -. DR BindingDB; P00441; -. DR ChEMBL; CHEMBL2354; -. DR DrugBank; DB01629; 5-fluorouridine. DR DrugBank; DB14001; alpha-Tocopherol succinate. DR DrugBank; DB05025; Arimoclomol. DR DrugBank; DB09096; Benzoyl peroxide. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB00958; Carboplatin. DR DrugBank; DB00515; Cisplatin. DR DrugBank; DB09130; Copper. DR DrugBank; DB14002; D-alpha-Tocopherol acetate. DR DrugBank; DB00988; Dopamine. DR DrugBank; DB01064; Isoprenaline. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB14011; Nabiximols. DR DrugBank; DB00526; Oxaliplatin. DR DrugBank; DB09221; Polaprezinc. DR DrugBank; DB03382; S-oxy-L-cysteine. DR DrugBank; DB00163; Vitamin E. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR CarbonylDB; P00441; -. DR GlyConnect; 1778; 2 N-Linked glycans (1 site). DR GlyCosmos; P00441; 1 site, 2 glycans. DR GlyGen; P00441; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site). 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 EPD; P00441; -. DR jPOST; P00441; -. DR MassIVE; P00441; -. DR PaxDb; 9606-ENSP00000270142; -. DR PeptideAtlas; P00441; -. DR ProteomicsDB; 51250; -. DR Pumba; P00441; -. DR TopDownProteomics; P00441; -. DR ABCD; P00441; 17 sequenced antibodies. DR Antibodypedia; 786; 1768 antibodies from 50 providers. DR DNASU; 6647; -. DR Ensembl; ENST00000270142.11; ENSP00000270142.7; ENSG00000142168.15. DR GeneID; 6647; -. DR KEGG; hsa:6647; -. DR MANE-Select; ENST00000270142.11; ENSP00000270142.7; NM_000454.5; NP_000445.1. DR AGR; HGNC:11179; -. DR DisGeNET; 6647; -. DR GeneCards; SOD1; -. DR HGNC; HGNC:11179; SOD1. DR HPA; ENSG00000142168; Tissue enhanced (liver). DR MalaCards; SOD1; -. DR MIM; 105400; phenotype. DR MIM; 147450; gene. DR MIM; 618598; phenotype. DR neXtProt; NX_P00441; -. DR OpenTargets; ENSG00000142168; -. DR Orphanet; 803; Amyotrophic lateral sclerosis. DR PharmGKB; PA334; -. DR VEuPathDB; HostDB:ENSG00000142168; -. DR eggNOG; KOG0441; Eukaryota. DR GeneTree; ENSGT00940000155551; -. DR HOGENOM; CLU_056632_4_1_1; -. DR InParanoid; P00441; -. DR OMA; AQRGFHI; -. DR OrthoDB; 3470597at2759; -. DR PhylomeDB; P00441; -. DR TreeFam; TF105131; -. DR BioCyc; MetaCyc:HS06899-MONOMER; -. DR BRENDA; 1.15.1.1; 2681. DR PathwayCommons; P00441; -. 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 SignaLink; P00441; -. DR SIGNOR; P00441; -. DR BioGRID-ORCS; 6647; 803 hits in 1146 CRISPR screens. DR ChiTaRS; SOD1; human. DR EvolutionaryTrace; P00441; -. DR GeneWiki; SOD1; -. DR GenomeRNAi; 6647; -. DR Pharos; P00441; Tchem. DR PRO; PR:P00441; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P00441; Protein. DR Bgee; ENSG00000142168; Expressed in pons and 213 other cell types or tissues. DR ExpressionAtlas; P00441; baseline and differential. 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:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. 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: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:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030346; F:protein phosphatase 2B binding; IDA:UniProtKB. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:UniProtKB. DR GO; GO:0031267; F:small 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:0099610; P:action potential initiation; IEA:Ensembl. DR GO; GO:0008089; P:anterograde axonal transport; ISS:BHF-UCL. DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB. DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl. DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl. DR GO; GO:0007566; P:embryo implantation; ISS:UniProtKB. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. 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:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB. 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:0051093; P:negative regulation of developmental process; IEA:Ensembl. DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl. DR GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl. 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: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:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB. DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL. DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl. 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 associated smooth muscle; ISS:UniProtKB. DR GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB. DR GO; GO:0048678; P:response to axon injury; 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:0010033; P:response to organic substance; IDA:UniProtKB. DR GO; GO:0000303; P:response to superoxide; IDA:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. 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 DisProt; DP00652; -. DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1. DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf. DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone. DR InterPro; IPR018152; SOD_Cu/Zn_BS. DR InterPro; IPR001424; SOD_Cu_Zn_dom. DR PANTHER; PTHR10003:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1. DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. DR SWISS-2DPAGE; P00441; -. DR UCD-2DPAGE; P00441; -. DR Genevisible; P00441; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Amyotrophic lateral sclerosis; Antioxidant; KW Copper; Cytoplasm; Direct protein sequencing; Disease variant; KW Disulfide bond; Lipoprotein; Metal-binding; Neurodegeneration; Nucleus; KW Oxidoreductase; Palmitate; Phosphoprotein; Reference proteome; KW Ubl conjugation; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:6770891, FT ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712" FT CHAIN 2..154 FT /note="Superoxide dismutase [Cu-Zn]" FT /id="PRO_0000164057" FT BINDING 47 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12963370, FT ECO:0000269|PubMed:17548825" FT BINDING 49 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12963370, FT ECO:0000269|PubMed:17548825" FT BINDING 64 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12963370, FT ECO:0000269|PubMed:17548825" FT BINDING 64 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:20727846" FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:20727846" FT BINDING 81 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:20727846" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:20727846" FT BINDING 121 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:12963370, FT ECO:0000269|PubMed:17548825" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:1463506, FT ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712" FT MOD_RES 4 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 10 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 92 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07632" FT MOD_RES 108 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 123 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:24140062" FT MOD_RES 137 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 137 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08228" FT LIPID 7 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:22496122" FT DISULFID 58..147 FT /evidence="ECO:0000269|PubMed:12963370, FT ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:15326189, FT ECO:0000269|PubMed:16406071" FT CROSSLNK 33 FT /note="1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain FT with W-33)" FT /evidence="ECO:0000269|PubMed:20600836" FT VARIANT 5 FT /note="A -> S (in ALS1; dbSNP:rs121912444)" FT /evidence="ECO:0000269|PubMed:9696308" FT /id="VAR_013518" FT VARIANT 5 FT /note="A -> T (in ALS1; dbSNP:rs121912444)" FT /evidence="ECO:0000269|PubMed:8179602" FT /id="VAR_007130" FT VARIANT 5 FT /note="A -> V (in ALS1; severe form; reduces structural FT stability and enzyme activity; increases tendency to form FT fibrillar aggregates; dbSNP:rs121912442)" FT /evidence="ECO:0000269|PubMed:10400992, FT ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:15056757, FT ECO:0000269|PubMed:7887412, ECO:0000269|PubMed:8351519, FT ECO:0000269|PubMed:9365366" FT /id="VAR_007131" FT VARIANT 7 FT /note="C -> F (in ALS1; dbSNP:rs121912448)" FT /evidence="ECO:0000269|PubMed:8907321" FT /id="VAR_008717" FT VARIANT 8 FT /note="V -> E (in ALS1; dbSNP:rs1568807330)" FT /evidence="ECO:0000269|PubMed:7980516" FT /id="VAR_007132" FT VARIANT 9 FT /note="L -> Q (in ALS1; dbSNP:rs1568807342)" FT /evidence="ECO:0000269|PubMed:9131652" FT /id="VAR_013519" FT VARIANT 9 FT /note="L -> V (in ALS1; dbSNP:rs1568807333)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_013520" FT VARIANT 13 FT /note="G -> R (in ALS1; dbSNP:rs121912456)" FT /evidence="ECO:0000269|PubMed:10430435" FT /id="VAR_013521" FT VARIANT 15 FT /note="V -> G (in ALS1; dbSNP:rs1202989817)" FT /evidence="ECO:0000269|PubMed:9365366" FT /id="VAR_013522" FT VARIANT 15 FT /note="V -> M (in ALS1; dbSNP:rs1568807400)" FT /evidence="ECO:0000269|PubMed:7655471" FT /id="VAR_007133" FT VARIANT 17 FT /note="G -> S (in ALS1; sporadic young onset; FT dbSNP:rs121912453)" FT /evidence="ECO:0000269|PubMed:9101297" FT /id="VAR_007134" FT VARIANT 21 FT /note="F -> C (in ALS1; dbSNP:rs1555836169)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_045876" FT VARIANT 22 FT /note="E -> G (in ALS1; dbSNP:rs1568807435)" FT /evidence="ECO:0000269|PubMed:9706719" FT /id="VAR_013523" FT VARIANT 22 FT /note="E -> K (in ALS1; dbSNP:rs121912450)" FT /evidence="ECO:0000269|PubMed:8069312" FT /id="VAR_007135" FT VARIANT 23 FT /note="Q -> L (in ALS1; dbSNP:rs1169198442)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_045877" FT VARIANT 38 FT /note="G -> R (in ALS1; mild form; ubiquitinated by RNF19A. FT Ubiquitinated by MARCHF5; leading to the degradation of FT mitochondrial SOD1; dbSNP:rs121912431)" FT /evidence="ECO:0000269|PubMed:10400992, FT ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12210393, FT ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:7887412, FT ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170, FT ECO:0000269|PubMed:9541385" FT /id="VAR_007136" FT VARIANT 39 FT /note="L -> R (in ALS1; dbSNP:rs1555836520)" FT /evidence="ECO:0000269|PubMed:9706719" FT /id="VAR_013524" FT VARIANT 39 FT /note="L -> V (in ALS1; dbSNP:rs121912432)" FT /evidence="ECO:0000269|PubMed:8351519, FT ECO:0000269|PubMed:8446170" FT /id="VAR_007137" FT VARIANT 42 FT /note="G -> D (in ALS1; dbSNP:rs121912434)" FT /evidence="ECO:0000269|PubMed:8351519, FT ECO:0000269|PubMed:8446170" FT /id="VAR_007139" FT VARIANT 42 FT /note="G -> S (in ALS1; dbSNP:rs121912433)" FT /evidence="ECO:0000269|PubMed:8351519, FT ECO:0000269|PubMed:8446170" FT /id="VAR_007138" FT VARIANT 44 FT /note="H -> R (in ALS1; reduces structural stability and FT enzyme activity; increases tendency to form fibrillar FT aggregates; dbSNP:rs121912435)" FT /evidence="ECO:0000269|PubMed:12963370, FT ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170" FT /id="VAR_007140" FT VARIANT 46 FT /note="F -> C (in ALS1; slow progression; FT dbSNP:rs121912457)" FT /evidence="ECO:0000269|PubMed:11369193" FT /id="VAR_013525" FT VARIANT 47 FT /note="H -> R (in ALS1; 80% of wild-type activity; FT ubiquitinated by RNF19A; dbSNP:rs121912443)" FT /evidence="ECO:0000269|PubMed:10400992, FT ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12754496, FT ECO:0000269|PubMed:7836951" FT /id="VAR_007141" FT VARIANT 49 FT /note="H -> Q (in ALS1; dbSNP:rs1568809175)" FT /evidence="ECO:0000269|PubMed:10400992, FT ECO:0000269|PubMed:8528216" FT /id="VAR_007142" FT VARIANT 49 FT /note="H -> R (in ALS1; dbSNP:rs1568809172)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_045878" FT VARIANT 50 FT /note="E -> K (in ALS1; dbSNP:rs1568809178)" FT /evidence="ECO:0000269|PubMed:9706719" FT /id="VAR_013526" FT VARIANT 55 FT /note="T -> R (in ALS1; reduces tendency to form fibrillar FT aggregates; dbSNP:rs986277034)" FT /evidence="ECO:0000269|PubMed:14506936, FT ECO:0000269|PubMed:18301754" FT /id="VAR_045879" FT VARIANT 66 FT /note="N -> S (in ALS1; dbSNP:rs1568810275)" FT /evidence="ECO:0000269|PubMed:12210393" FT /id="VAR_013527" FT VARIANT 68 FT /note="L -> P (in ALS1; dbSNP:rs1568810289)" FT /evidence="ECO:0000269|PubMed:21247266" FT /id="VAR_065560" FT VARIANT 68 FT /note="L -> R (in ALS1; dbSNP:rs1568810289)" FT /evidence="ECO:0000269|PubMed:9706719" FT /id="VAR_013528" FT VARIANT 73 FT /note="G -> S (in ALS1; dbSNP:rs121912455)" FT /evidence="ECO:0000269|PubMed:9455977" FT /id="VAR_008718" FT VARIANT 77 FT /note="D -> Y (in ALS1; dbSNP:rs1601157750)" FT /evidence="ECO:0000269|PubMed:9365366" FT /id="VAR_013529" FT VARIANT 81 FT /note="H -> R (in ALS1; sporadic form; interferes with zinc FT binding)" FT /evidence="ECO:0000269|PubMed:12402272" FT /id="VAR_016874" FT VARIANT 85 FT /note="L -> F (in ALS1; dbSNP:rs1315541036)" FT /evidence="ECO:0000269|PubMed:9706719" FT /id="VAR_013530" FT VARIANT 85 FT /note="L -> V (in ALS1; dbSNP:rs121912452)" FT /evidence="ECO:0000269|PubMed:7655471" FT /id="VAR_007143" FT VARIANT 86 FT /note="G -> R (in ALS1; ubiquitinated by RNF19A; interferes FT with zinc-binding; ubiquitinated by MARCHF5; leading to the FT degradation of mitochondrial SOD1; dbSNP:rs121912436)" FT /evidence="ECO:0000269|PubMed:10400992, FT ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:18378676, FT ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:19741096, FT ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170, FT ECO:0000269|Ref.51" FT /id="VAR_007144" FT VARIANT 87 FT /note="N -> S (in ALS1; dbSNP:rs11556620)" FT /evidence="ECO:0000269|PubMed:27604643" FT /id="VAR_013531" FT VARIANT 88 FT /note="V -> A (in ALS1; dbSNP:rs1339283341)" FT /evidence="ECO:0000269|PubMed:14506936, FT ECO:0000269|PubMed:27604643" FT /id="VAR_045880" FT VARIANT 90 FT /note="A -> T (in ALS1; dbSNP:rs1568810660)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_045881" FT VARIANT 90 FT /note="A -> V (in ALS1; dbSNP:rs1280042397)" FT /evidence="ECO:0000269|PubMed:31086828" FT /id="VAR_013532" FT VARIANT 91 FT /note="D -> A (in ALS1; does not seem to be linked with a FT decrease in activity; dbSNP:rs80265967)" FT /evidence="ECO:0000269|PubMed:18301754, FT ECO:0000269|PubMed:20460594, ECO:0000269|PubMed:7647793, FT ECO:0000269|PubMed:7655469, ECO:0000269|PubMed:9365366" FT /id="VAR_007145" FT VARIANT 91 FT /note="D -> V (in ALS1; dbSNP:rs80265967)" FT /evidence="ECO:0000269|Ref.85" FT /id="VAR_013533" FT VARIANT 94 FT /note="G -> A (in ALS1; increases tendency to form FT fibrillar aggregates; ubiquitinated by RNF19A; FT ubiquitinated by MARCHF5; dbSNP:rs121912438)" FT /evidence="ECO:0000269|PubMed:12145308, FT ECO:0000269|PubMed:18301754, ECO:0000269|PubMed:19741096, FT ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170" FT /id="VAR_007146" FT VARIANT 94 FT /note="G -> C (in ALS1; dbSNP:rs121912437)" FT /evidence="ECO:0000269|PubMed:8351519, FT ECO:0000269|PubMed:8446170" FT /id="VAR_007147" FT VARIANT 94 FT /note="G -> D (in ALS1; dbSNP:rs121912438)" FT /evidence="ECO:0000269|PubMed:18301754, FT ECO:0000269|PubMed:7951252" FT /id="VAR_007148" FT VARIANT 94 FT /note="G -> R (in ALS1; 30% of wild-type activity; FT dbSNP:rs121912437)" FT /evidence="ECO:0000269|PubMed:18552350, FT ECO:0000269|PubMed:7700376, ECO:0000269|PubMed:8528216" FT /id="VAR_007149" FT VARIANT 94 FT /note="G -> V (in ALS1; dbSNP:rs121912438)" FT /evidence="ECO:0000269|PubMed:8938700" FT /id="VAR_008719" FT VARIANT 96 FT /note="A -> G (in ALS1; dbSNP:rs1568810690)" FT /evidence="ECO:0000269|PubMed:21220647" FT /id="VAR_065194" FT VARIANT 98 FT /note="V -> M (in ALS1; increases tendency to form FT fibrillar aggregates; dbSNP:rs1555836806)" FT /evidence="ECO:0000269|PubMed:14506936, FT ECO:0000269|PubMed:18301754" FT /id="VAR_045882" FT VARIANT 101 FT /note="E -> G (in ALS1; dbSNP:rs121912439)" FT /evidence="ECO:0000269|PubMed:8351519, FT ECO:0000269|PubMed:8446170" FT /id="VAR_007150" FT VARIANT 101 FT /note="E -> K (in ALS1; dbSNP:rs76731700)" FT /evidence="ECO:0000269|PubMed:20460594, FT ECO:0000269|PubMed:8875253" FT /id="VAR_013534" FT VARIANT 102 FT /note="D -> G (in ALS1; dbSNP:rs1568810721)" FT /evidence="ECO:0000269|PubMed:27604643, FT ECO:0000269|PubMed:7655468" FT /id="VAR_007151" FT VARIANT 102 FT /note="D -> N (in ALS1; dbSNP:rs1568810715)" FT /evidence="ECO:0000269|PubMed:27604643, FT ECO:0000269|PubMed:7870076" FT /id="VAR_007152" FT VARIANT 105 FT /note="I -> F (in ALS1; dbSNP:rs121912445)" FT /evidence="ECO:0000269|PubMed:7501156" FT /id="VAR_008720" FT VARIANT 106 FT /note="S -> L (in ALS1; dbSNP:rs1378590183)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_013535" FT VARIANT 107 FT /note="L -> V (in ALS1; dbSNP:rs121912440)" FT /evidence="ECO:0000269|PubMed:8351519, FT ECO:0000269|PubMed:8446170" FT /id="VAR_007153" FT VARIANT 109 FT /note="G -> V (in ALS1; dbSNP:rs1359299834)" FT /evidence="ECO:0000269|PubMed:24283821" FT /id="VAR_013536" FT VARIANT 112 FT /note="C -> Y (in ALS1; dbSNP:rs1601158483)" FT /evidence="ECO:0000269|PubMed:27604643" FT /id="VAR_077327" FT VARIANT 113 FT /note="I -> M (in ALS1; dbSNP:rs1299542356)" FT /evidence="ECO:0000269|PubMed:12210393" FT /id="VAR_013537" FT VARIANT 113 FT /note="I -> T (in ALS1; dbSNP:rs74315452)" FT /evidence="ECO:0000269|PubMed:7951252, FT ECO:0000269|PubMed:8528216" FT /id="VAR_007154" FT VARIANT 114 FT /note="I -> T (in ALS1; destabilizes dimeric protein FT structure and increases tendency to form fibrillar FT aggregates; dbSNP:rs121912441)" FT /evidence="ECO:0000269|PubMed:10400992, FT ECO:0000269|PubMed:10732812, ECO:0000269|PubMed:15056757, FT ECO:0000269|PubMed:7887412, ECO:0000269|PubMed:7997024, FT ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170, FT ECO:0000269|PubMed:8528216" FT /id="VAR_007155" FT VARIANT 115 FT /note="G -> A (in ALS1; dbSNP:rs1568810789)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_013538" FT VARIANT 116 FT /note="R -> G (in ALS1; dbSNP:rs1301635320)" FT /evidence="ECO:0000269|PubMed:7881433" FT /id="VAR_007156" FT VARIANT 119 FT /note="V -> L (in ALS1; dbSNP:rs1235629842)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_045883" FT VARIANT 119 FT /note="V -> VFLQ (in ALS1)" FT /id="VAR_008721" FT VARIANT 125 FT /note="D -> G (in ALS1; dbSNP:rs1568811366)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_045884" FT VARIANT 125 FT /note="D -> V (in ALS1; dbSNP:rs1568811366)" FT /evidence="ECO:0000269|PubMed:8938700" FT /id="VAR_008722" FT VARIANT 126 FT /note="D -> H (in ALS1; dbSNP:rs1568811372)" FT /evidence="ECO:0000269|PubMed:8528216" FT /id="VAR_007157" FT VARIANT 127 FT /note="L -> S (in ALS1; dbSNP:rs121912454)" FT /evidence="ECO:0000269|PubMed:11535232" FT /id="VAR_013539" FT VARIANT 134 FT /note="Missing (in ALS; dbSNP:rs1568811423)" FT /evidence="ECO:0000269|PubMed:8938700" FT /id="VAR_008723" FT VARIANT 135 FT /note="S -> N (in ALS1; reduced metal binding; increases FT tendency to form fibrillar aggregates; dbSNP:rs121912451)" FT /evidence="ECO:0000269|PubMed:12754496, FT ECO:0000269|PubMed:8990014" FT /id="VAR_007158" FT VARIANT 140 FT /note="N -> K (in ALS1; dbSNP:rs1804449)" FT /evidence="ECO:0000269|PubMed:7887412" FT /id="VAR_007159" FT VARIANT 145 FT /note="L -> F (in ALS1; dbSNP:rs1482760341)" FT /evidence="ECO:0000269|PubMed:18301754, FT ECO:0000269|PubMed:7887412, ECO:0000269|PubMed:8351519" FT /id="VAR_007160" FT VARIANT 145 FT /note="L -> S (in ALS1; dbSNP:rs121912446)" FT /evidence="ECO:0000269|PubMed:7496169" FT /id="VAR_008724" FT VARIANT 146 FT /note="A -> T (in ALS1; dbSNP:rs121912447)" FT /evidence="ECO:0000269|PubMed:7496169" FT /id="VAR_008725" FT VARIANT 147 FT /note="C -> R (in ALS1; dbSNP:rs1568811515)" FT /evidence="ECO:0000269|PubMed:8875253" FT /id="VAR_013540" FT VARIANT 148 FT /note="G -> R (in ALS1; dbSNP:rs1568811520)" FT /evidence="ECO:0000269|PubMed:14506936" FT /id="VAR_045885" FT VARIANT 149 FT /note="V -> G (in ALS1; dbSNP:rs1476760624)" FT /evidence="ECO:0000269|PubMed:8351519" FT /id="VAR_007161" FT VARIANT 149 FT /note="V -> I (in ALS1; dbSNP:rs567511139)" FT /evidence="ECO:0000269|PubMed:7795609" FT /id="VAR_007162" FT VARIANT 150 FT /note="I -> T (in ALS1; dbSNP:rs1424014997)" FT /evidence="ECO:0000269|PubMed:7887412, FT ECO:0000269|PubMed:8528216" FT /id="VAR_007163" FT VARIANT 152 FT /note="I -> T (in ALS1; dbSNP:rs121912449)" FT /evidence="ECO:0000269|PubMed:8682505" FT /id="VAR_007164" FT MUTAGEN 7 FT /note="C->S: Enhances formation of fibrillar aggregates in FT the absence of bound zinc; when associated with S-58; S-112 FT and S-147." FT /evidence="ECO:0000269|PubMed:17070542, FT ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:22496122" FT MUTAGEN 7 FT /note="C->S: No palmitoylation, reduced nuclear targeting." FT /evidence="ECO:0000269|PubMed:17070542, FT ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:22496122" FT MUTAGEN 51..52 FT /note="FG->EE: Abolishes dimerization; when associated with FT Q-134." FT /evidence="ECO:0000269|PubMed:10329151, FT ECO:0000269|PubMed:18552350" FT MUTAGEN 58 FT /note="C->A: Exhibits very slow copper acquisition." FT /evidence="ECO:0000269|PubMed:17070542, FT ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804" FT MUTAGEN 58 FT /note="C->S: Enhances formation of fibrillar aggregates in FT the absence of bound zinc; when associated with S-7; S-112 FT and S-147." FT /evidence="ECO:0000269|PubMed:17070542, FT ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804" FT MUTAGEN 81 FT /note="H->A: Loss of zinc binding and enhanced tendency to FT form aggregates; when associated with A-84." FT /evidence="ECO:0000269|PubMed:17888947, FT ECO:0000269|PubMed:18552350" FT MUTAGEN 81 FT /note="H->S: Destabilization of dimer and loss of zinc FT binding; when associated with S-84." FT /evidence="ECO:0000269|PubMed:17888947, FT ECO:0000269|PubMed:18552350" FT MUTAGEN 84 FT /note="D->A: Loss of zinc binding and enhanced tendency to FT form aggregates; when associated with A-81." FT /evidence="ECO:0000269|PubMed:17888947, FT ECO:0000269|PubMed:18552350" FT MUTAGEN 84 FT /note="D->S: Destabilization of dimer and loss of zinc FT binding; when associated with S-81." FT /evidence="ECO:0000269|PubMed:17888947, FT ECO:0000269|PubMed:18552350" FT MUTAGEN 112 FT /note="C->S: Enhances formation of fibrillar aggregates in FT the absence of bound zinc; when associated with S-7; S-58 FT and S-147." FT /evidence="ECO:0000269|PubMed:17070542, FT ECO:0000269|PubMed:18552350" FT MUTAGEN 123 FT /note="K->A: Decreased succinylation." FT /evidence="ECO:0000269|PubMed:24140062" FT MUTAGEN 123 FT /note="K->E: Mimicks constitutive succinylation state; FT decreased activity." FT /evidence="ECO:0000269|PubMed:24140062" FT MUTAGEN 134 FT /note="E->Q: Abolishes dimerization; when associated with FT E-50 and E-51." FT /evidence="ECO:0000269|PubMed:10329151" FT MUTAGEN 147 FT /note="C->A: Exhibits very slow copper acquisition." FT /evidence="ECO:0000269|PubMed:17070542, FT ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804" FT MUTAGEN 147 FT /note="C->S: Enhances formation of fibrillar aggregates in FT the absence of bound zinc; when associated with S-7; S-58 FT and S-112." FT /evidence="ECO:0000269|PubMed:17070542, FT ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:23625804" FT CONFLICT 18 FT /note="I -> S (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 99 FT /note="S -> V (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT STRAND 3..10 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 16..25 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:1RK7" FT STRAND 30..38 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 41..50 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:2NAM" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:7FB6" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:1KMG" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:1KMG" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:1RK7" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:1MFM" FT TURN 80..82 FT /evidence="ECO:0007829|PDB:2MP3" FT STRAND 84..90 FT /evidence="ECO:0007829|PDB:4A7U" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:1SPD" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:4A7U" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:7VZF" FT STRAND 116..123 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:2LU5" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:4A7U" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:6FLH" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:4A7U" FT STRAND 151..153 FT /evidence="ECO:0007829|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 //