SODC_HUMAN
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 03-AUG-2022, entry version 260.
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 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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
RP VARIANTS ALS1.
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 [53]
RP ERRATUM OF PUBMED:8446170.
RX PubMed=8332197; DOI=10.1038/364362c0;
RA Rosen D.R.;
RL Nature 364:362-362(1993).
RN [54]
RP VARIANTS ALS1.
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 [55]
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 [56]
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 [57]
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 [58]
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 [59]
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 [60]
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 [61]
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 [62]
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 [63]
RP VARIANTS ALS1.
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 [64]
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 [65]
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 [66]
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 [67]
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 [68]
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 [69]
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 [70]
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 [71]
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 [72]
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 [73]
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 [74]
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 [75]
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 [76]
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 [77]
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 [78]
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 [79]
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 [80]
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 [81]
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 [82]
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 [83]
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 [84]
RP VARIANT ALS1 ALA-81.
RX PubMed=12402272; DOI=10.1002/ana.10369;
RA Alexander M.D., Traynor B.J., Miller N., Corr B., Frost E., 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 [85]
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 [86]
RP VARIANTS ALS1 VAL-9; CYS-21; LEU-23; ARG-49; ARG-55; ALA-88; THR-90;
RP MET-98; LEU-119; GLY-125 AND ARG-148.
RX PubMed=14506936; DOI=10.1080/14660820310011700;
RA Andersen P.M., Sims K.B., Xin W.W., Kiely R., O'Neill G., Ravits J.,
RA Pioro E., Harati Y., Brower R.D., Levine J.S., Heinicke H.U., 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 [87]
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 [88]
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 [89]
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 [90]
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 [91]
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 [92]
RP VARIANTS ALS1 SER-87; ALA-88; ASN-102; GLY-102 AND TYR-112.
RX PubMed=27604643; DOI=10.1038/srep32478;
RA Hou L., Jiao B., Xiao T., Zhou L., Zhou Z., Du J., Yan X., Wang J.,
RA Tang B., Shen L.;
RT "Screening of SOD1, FUS and TARDBP genes in patients with amyotrophic
RT lateral sclerosis in central-southern China.";
RL Sci. Rep. 6:32478-32478(2016).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {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. Homodimerization may take
CC place via the ditryptophan cross-link at Trp-33. The pathogenic
CC variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 interact with RNF19A,
CC whereas wild-type protein does not. The pathogenic variants ALS1 Arg-86
CC and Ala-94 interact with MARCH5, whereas wild-type protein does not.
CC {ECO:0000269|PubMed:10329151, ECO:0000269|PubMed:12911296,
CC ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:15326189,
CC ECO:0000269|PubMed:16291742, ECO:0000269|PubMed:16406071,
CC ECO:0000269|PubMed:17548825, ECO:0000269|PubMed:17888947,
CC ECO:0000269|PubMed:20600836, ECO:0000269|PubMed:20727846}.
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; P00441: SOD1; NbExp=21; 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; Q9GZS3: WDR61; NbExp=3; IntAct=EBI-990792, EBI-358545;
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}.
CC Mitochondrion {ECO:0000269|PubMed:19741096}. Nucleus
CC {ECO:0000269|PubMed:22496122}. Note=Predominantly cytoplasmic; the
CC pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates 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:12402272, ECO:0000269|PubMed:12754496,
CC ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:14506936,
CC ECO:0000269|PubMed:15056757, ECO:0000269|PubMed:18301754,
CC ECO:0000269|PubMed:18378676, ECO:0000269|PubMed:18552350,
CC ECO:0000269|PubMed:19741096, ECO:0000269|PubMed:21220647,
CC ECO:0000269|PubMed:21247266, ECO:0000269|PubMed:27604643,
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:8907321,
CC ECO:0000269|PubMed:8938700, ECO:0000269|PubMed:8990014,
CC ECO:0000269|PubMed:9101297, ECO:0000269|PubMed:9131652,
CC ECO:0000269|PubMed:9455977, ECO:0000269|PubMed:9541385}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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 -!- 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 ---------------------------------------------------------------------------
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DR EMBL; L44139; AAB05662.1; -; Genomic_DNA.
DR EMBL; L44135; AAB05662.1; JOINED; Genomic_DNA.
DR EMBL; L44136; AAB05662.1; JOINED; Genomic_DNA.
DR EMBL; L44137; AAB05662.1; JOINED; Genomic_DNA.
DR EMBL; L44139; AAB05661.1; -; Genomic_DNA.
DR EMBL; L44135; AAB05661.1; JOINED; Genomic_DNA.
DR EMBL; L44136; AAB05661.1; JOINED; Genomic_DNA.
DR EMBL; L44137; AAB05661.1; JOINED; Genomic_DNA.
DR EMBL; X02317; CAA26182.1; -; mRNA.
DR EMBL; X01780; CAA25915.1; -; Genomic_DNA.
DR EMBL; X01781; CAA25916.1; -; Genomic_DNA.
DR EMBL; X01782; CAA25917.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X01783; CAA25918.1; -; Genomic_DNA.
DR EMBL; X01784; CAA25919.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY049787; AAL15444.1; -; mRNA.
DR EMBL; AY450286; AAR21563.1; -; mRNA.
DR EMBL; EF151142; ABL96616.1; -; mRNA.
DR EMBL; AK312116; BAG35052.1; -; mRNA.
DR EMBL; CR450355; CAG29351.1; -; mRNA.
DR EMBL; CR541742; CAG46542.1; -; mRNA.
DR EMBL; BT006676; AAP35322.1; -; mRNA.
DR EMBL; AY835629; AAV80422.1; -; Genomic_DNA.
DR EMBL; AP000253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09889.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09890.1; -; Genomic_DNA.
DR EMBL; BC001034; AAH01034.1; -; mRNA.
DR EMBL; L46374; AAB59626.1; -; Genomic_DNA.
DR EMBL; L46375; AAB59627.1; -; Genomic_DNA.
DR EMBL; L44746; AAC41773.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X95228; CAA64520.1; -; Genomic_DNA.
DR CCDS; CCDS33536.1; -.
DR PIR; A22703; DSHUCZ.
DR RefSeq; NP_000445.1; NM_000454.4.
DR 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 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 AlphaFoldDB; P00441; -.
DR BMRB; P00441; -.
DR SMR; P00441; -.
DR BioGRID; 112530; 401.
DR ComplexPortal; CPX-2897; [Cu-Zn] Superoxide dismutase complex.
DR DIP; DIP-44941N; -.
DR IntAct; P00441; 332.
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 GlyGen; P00441; 1 site, 2 N-linked glycans (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 SWISS-2DPAGE; P00441; -.
DR UCD-2DPAGE; P00441; -.
DR EPD; P00441; -.
DR jPOST; P00441; -.
DR MassIVE; P00441; -.
DR PaxDb; P00441; -.
DR PeptideAtlas; P00441; -.
DR PRIDE; P00441; -.
DR ProteomicsDB; 51250; -.
DR TopDownProteomics; P00441; -.
DR ABCD; P00441; 17 sequenced antibodies.
DR Antibodypedia; 786; 1525 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 CTD; 6647; -.
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; 1574423at2759; -.
DR PhylomeDB; P00441; -.
DR TreeFam; TF105131; -.
DR BioCyc; MetaCyc:HS06899-MON; -.
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; 765 hits in 1065 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 211 other tissues.
DR ExpressionAtlas; P00441; baseline and differential.
DR Genevisible; P00441; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB.
DR GO; GO:0031045; C:dense core granule; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO: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:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030346; F:protein phosphatase 2B binding; IDA: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:0007568; P:aging; 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:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0035865; P:cellular response to potassium ion; 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: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: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: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:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl.
DR GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
DR GO; GO:0000303; P:response to superoxide; IDA:UniProtKB.
DR GO; GO: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; -; 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; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amyotrophic lateral sclerosis; Antioxidant;
KW Copper; Cytoplasm; Direct protein sequencing; Disease variant;
KW Disulfide bond; Lipoprotein; Metal-binding; Mitochondrion;
KW Neurodegeneration; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
KW Reference proteome; 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 /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 /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 /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 /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 MARCH5; leading to the degradation of
FT mitochondrial SOD1; dbSNP:rs121912431)"
FT /evidence="ECO:0000269|PubMed:10400992,
FT ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:18552350,
FT ECO:0000269|PubMed:9541385"
FT /id="VAR_007136"
FT VARIANT 39
FT /note="L -> R (in ALS1; dbSNP:rs1555836520)"
FT /id="VAR_013524"
FT VARIANT 39
FT /note="L -> V (in ALS1; dbSNP:rs121912432)"
FT /id="VAR_007137"
FT VARIANT 42
FT /note="G -> D (in ALS1; dbSNP:rs121912434)"
FT /id="VAR_007139"
FT VARIANT 42
FT /note="G -> S (in ALS1; dbSNP:rs121912433)"
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 /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; 'benign' form; 80% of wild-type
FT activity; 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 /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 /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 /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 /id="VAR_013529"
FT VARIANT 81
FT /note="H -> A (in ALS1; sporadic form; interferes with zinc
FT binding; requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:12402272"
FT /id="VAR_016874"
FT VARIANT 85
FT /note="L -> F (in ALS1; dbSNP:rs1315541036)"
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 MARCH5; 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|Ref.49"
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 /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:7647793, ECO:0000269|PubMed:7655469"
FT /id="VAR_007145"
FT VARIANT 91
FT /note="D -> V (in ALS1; dbSNP:rs80265967)"
FT /id="VAR_013533"
FT VARIANT 94
FT /note="G -> A (in ALS1; increases tendency to form
FT fibrillar aggregates; ubiquitinated by RNF19A;
FT dbSNP:rs121912438)"
FT /evidence="ECO:0000269|PubMed:12145308,
FT ECO:0000269|PubMed:18301754, ECO:0000269|PubMed:19741096"
FT /id="VAR_007146"
FT VARIANT 94
FT /note="G -> C (in ALS1; dbSNP:rs121912437)"
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 /id="VAR_007150"
FT VARIANT 101
FT /note="E -> K (in ALS1; dbSNP:rs76731700)"
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 /id="VAR_013535"
FT VARIANT 107
FT /note="L -> V (in ALS1; dbSNP:rs121912440)"
FT /id="VAR_007153"
FT VARIANT 109
FT /note="G -> V (in ALS1; dbSNP:rs1359299834)"
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 /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:7997024, ECO:0000269|PubMed:8528216"
FT /id="VAR_007155"
FT VARIANT 115
FT /note="G -> A (in ALS1; dbSNP:rs1568810789)"
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 /id="VAR_007159"
FT VARIANT 145
FT /note="L -> F (in ALS1; dbSNP:rs1482760341)"
FT /evidence="ECO:0000269|PubMed:18301754"
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 /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 /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: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 TURN 55..57
FT /evidence="ECO:0007829|PDB:5U9M"
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 112..115
FT /evidence="ECO:0007829|PDB:2AF2"
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
