Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Superoxide dismutase 1) (hSod1)

 SODC_HUMAN              Reviewed;         154 AA.
P00441; A6NHJ0; D3DSE4; Q16669; Q16711; Q16838; Q16839; Q16840;
Q6NR85;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 227.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1;
AltName: Full=Superoxide dismutase 1;
Short=hSod1;
Name=SOD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6577438; DOI=10.1073/pnas.80.18.5465;
Sherman L., Dafni N., Lieman-Hurwitz J., Groner Y.;
"Nucleotide sequence and expression of human chromosome 21-encoded
superoxide dismutase mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:5465-5469(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3160582;
Levanon D., Lieman-Hurwitz J., Dafni N., Wigderson M., Sherman L.,
Bernstein Y., Laver-Rudich Z., Danciger E., Stein O., Groner Y.;
"Architecture and anatomy of the chromosomal locus in human chromosome
21 encoding the Cu/Zn superoxide dismutase.";
EMBO J. 4:77-84(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3889846; DOI=10.1093/nar/13.6.2017;
Hallewell R.A., Masiarz F.R., Najarian R.C., Puma J.P., Quiroga M.R.,
Randolph A., Sanchez-Pescador R., Scandella C.J., Smith B.,
Steimer K.S., Mullenbach G.T.;
"Human Cu/Zn superoxide dismutase cDNA: isolation of clones
synthesising high levels of active or inactive enzyme from an
expression library.";
Nucleic Acids Res. 13:2017-2034(1985).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2853161; DOI=10.1093/oxfordjournals.jbchem.a122562;
Kajihara J., Enomoto M., Nishijima K., Yabuuchi M., Katoh K.;
"Comparison of properties between human recombinant and placental
copper-zinc SOD.";
J. Biochem. 104:851-854(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Xu Y., Hu X., Zhou Y., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA].
Lu X., Hui L.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA].
Staege M.S., Bergmann S., Heins S.;
"Direct sequencing and cloning of superoxide dismutase 1 from
peripheral blood.";
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[16]
PROTEIN SEQUENCE OF 2-154.
PubMed=6770891; DOI=10.1021/bi00552a005;
Jabusch J.R., Farb D.L., Kerschensteiner D.A., Deutsch H.F.;
"Some sulfhydryl properties and primary structure of human erythrocyte
superoxide dismutase.";
Biochemistry 19:2310-2316(1980).
[17]
PROTEIN SEQUENCE OF 2-154, CLEAVAGE OF INITIATOR METHIONINE, AND
ACETYLATION AT ALA-2.
PubMed=7002610; DOI=10.1016/0014-5793(80)81044-1;
Barra D., Martini F., Bannister J.V., Schinina M.E., Rotilio G.,
Bannister W.H., Bossa F.;
"The complete amino acid sequence of human Cu/Zn superoxide
dismutase.";
FEBS Lett. 120:53-56(1980).
[18]
PROTEIN SEQUENCE OF 11-24 AND 81-116.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-56 AND 120-154, AND VARIANTS
ALS1 GLN-49; ARG-94; THR-113; THR-114; HIS-126 AND THR-150.
PubMed=8528216; DOI=10.1093/hmg/4.7.1239;
Enayat Z.E., Orrell R.W., Claus A., Ludolph A., Bachus R.,
Brockmueller J., Ray-Chaudhuri K., Radunovic A., Shaw C.,
Wilkinson J., King A., Swash M., Leigh P.N., de Belleroche J.,
Powell J.;
"Two novel mutations in the gene for copper zinc superoxide dismutase
in UK families with amyotrophic lateral sclerosis.";
Hum. Mol. Genet. 4:1239-1240(1995).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-154, AND VARIANT ALS1
THR-152.
PubMed=8682505; DOI=10.1007/s004390050157;
Kostrzewa M., Daamian M., Mueller U.;
"Superoxide dismutase 1: identification of a novel mutation in a case
of familial amyotrophic lateral sclerosis.";
Hum. Genet. 98:48-50(1996).
[21]
SUBUNIT, AND DISULFIDE BOND.
PubMed=15326189; DOI=10.1074/jbc.M406021200;
Arnesano F., Banci L., Bertini I., Martinelli M., Furukawa Y.,
O'Halloran T.V.;
"The unusually stable quaternary structure of human Cu,Zn-superoxide
dismutase 1 is controlled by both metal occupancy and disulfide
status.";
J. Biol. Chem. 279:47998-48003(2004).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[24]
SUBUNIT, AND DITRYPTOPHAN CROSS-LINK AT TRP-33.
PubMed=20600836; DOI=10.1016/j.freeradbiomed.2010.06.018;
Medinas D.B., Gozzo F.C., Santos L.F., Iglesias A.H., Augusto O.;
"A ditryptophan cross-link is responsible for the covalent
dimerization of human superoxide dismutase 1 during its bicarbonate-
dependent peroxidase activity.";
Free Radic. Biol. Med. 49:1046-1053(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PALMITOYLATION AT CYS-7, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
CYS-7.
PubMed=22496122; DOI=10.1161/CIRCRESAHA.112.269514;
Marin E.P., Derakhshan B., Lam T.T., Davalos A., Sessa W.C.;
"Endothelial cell palmitoylproteomic identifies novel lipid-modified
targets and potential substrates for protein acyl transferases.";
Circ. Res. 110:1336-1344(2012).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[29]
SUCCINYLATION AT LYS-123, DESUCCINYLATION BY SIRT5, AND MUTAGENESIS OF
LYS-123.
PubMed=24140062; DOI=10.1016/j.bbrc.2013.10.033;
Lin Z.F., Xu H.B., Wang J.Y., Lin Q., Ruan Z., Liu F.B., Jin W.,
Huang H.H., Chen X.;
"SIRT5 desuccinylates and activates SOD1 to eliminate ROS.";
Biochem. Biophys. Res. Commun. 441:191-195(2013).
[30]
MUTAGENESIS OF CYS-58 AND CYS-147.
PubMed=23625804; DOI=10.1002/cbic.201300042;
Banci L., Cantini F., Kozyreva T., Rubino J.T.;
"Mechanistic aspects of hSOD1 maturation from the solution structure
of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1
mutants.";
ChemBioChem 14:1839-1844(2013).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-103, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[33]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=1463506; DOI=10.1073/pnas.89.13.6109;
Parge H.E., Hallewell R.A., Tainer J.A.;
"Atomic structures of wild-type and thermostable mutant recombinant
human Cu,Zn superoxide dismutase.";
Proc. Natl. Acad. Sci. U.S.A. 89:6109-6113(1992).
[34]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ALS1 ARG-38.
PubMed=9541385; DOI=10.1002/pro.5560070302;
Hart P.J., Liu H., Pellegrini M., Nersissian A.M., Gralla E.B.,
Valentine J.S., Eisenberg D.;
"Subunit asymmetry in the three-dimensional structure of a human
CuZnSOD mutant found in familial amyotrophic lateral sclerosis.";
Protein Sci. 7:545-555(1998).
[35]
STRUCTURE BY NMR.
PubMed=9718300; DOI=10.1021/bi9803473;
Banci L., Benedetto M., Bertini I., del Conte R., Piccioli M.,
Viezzoli M.S.;
"Solution structure of reduced monomeric Q133M2 copper, zinc
superoxide dismutase (SOD). Why is SOD a dimeric enzyme?";
Biochemistry 37:11780-11791(1998).
[36]
X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF MUTANT
GLU-51/GLU-52/GLN-134, SUBUNIT, AND MUTAGENESIS OF 51-PHE-GLY-52 AND
GLU-134.
PubMed=10329151; DOI=10.1006/jmbi.1999.2681;
Ferraroni M., Rypniewski W., Wilson K.S., Viezzoli M.S., Banci L.,
Bertini I., Mangani S.;
"The crystal structure of the monomeric human SOD mutant
F50E/G51E/E133Q at atomic resolution. The enzyme mechanism
revisited.";
J. Mol. Biol. 288:413-426(1999).
[37]
STRUCTURE BY NMR OF MUTANT GLU51/GLU-52/GLN-134, AND SUBUNIT.
PubMed=12911296; DOI=10.1021/bi034324m;
Banci L., Bertini I., Cramaro F., Del Conte R., Viezzoli M.S.;
"Solution structure of Apo Cu,Zn superoxide dismutase: role of metal
ions in protein folding.";
Biochemistry 42:9543-9553(2003).
[38]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC
IONS, DISULFIDE BOND, SUBUNIT, AND CHARACTERIZATION OF VARIANTS ALS1
VAL-5 AND ARG-44.
PubMed=12963370; DOI=10.1016/S0022-2836(03)00889-1;
DiDonato M., Craig L., Huff M.E., Thayer M.M., Cardoso R.M.,
Kassmann C.J., Lo T.P., Bruns C.K., Powers E.T., Kelly J.W.,
Getzoff E.D., Tainer J.A.;
"ALS mutants of human superoxide dismutase form fibrous aggregates via
framework destabilization.";
J. Mol. Biol. 332:601-615(2003).
[39]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANTS ALS1 ASN-135 AND
ARG-47, AND FORMATION OF FIBRILLAR AGGREGATES.
PubMed=12754496; DOI=10.1038/nsb935;
Elam J.S., Taylor A.B., Strange R., Antonyuk S., Doucette P.A.,
Rodriguez J.A., Hasnain S.S., Hayward L.J., Valentine J.S.,
Yeates T.O., Hart P.J.;
"Amyloid-like filaments and water-filled nanotubes formed by SOD1
mutant proteins linked to familial ALS.";
Nat. Struct. Biol. 10:461-467(2003).
[40]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF VARIANTS ALS1 VAL-5 AND
THR-114, AND CHARACTERIZATION OF VARIANTS ALS1 VAL-5 AND THR-114.
PubMed=15056757; DOI=10.1073/pnas.0305143101;
Hough M.A., Grossmann J.G., Antonyuk S.V., Strange R.W.,
Doucette P.A., Rodriguez J.A., Whitson L.J., Hart P.J., Hayward L.J.,
Valentine J.S., Hasnain S.S.;
"Dimer destabilization in superoxide dismutase may result in disease-
causing properties: structures of motor neuron disease mutants.";
Proc. Natl. Acad. Sci. U.S.A. 101:5976-5981(2004).
[41]
STRUCTURE BY NMR OF MUTANT ALA-7/SER-112, AND SUBUNIT.
PubMed=16291742; DOI=10.1074/jbc.M506497200;
Banci L., Bertini I., Cantini F., D'Amelio N., Gaggelli E.;
"Human SOD1 before harboring the catalytic metal: solution structure
of copper-depleted, disulfide-reduced form.";
J. Biol. Chem. 281:2333-2337(2006).
[42]
X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEXES WITH COPPER AND
ZINC IONS, DISULFIDE BOND, AND SUBUNIT.
PubMed=16406071; DOI=10.1016/j.jmb.2005.11.081;
Strange R.W., Antonyuk S.V., Hough M.A., Doucette P.A.,
Valentine J.S., Hasnain S.S.;
"Variable metallation of human superoxide dismutase: atomic resolution
crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type
enzymes.";
J. Mol. Biol. 356:1152-1162(2006).
[43]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ALA-7/ALA-112 AND
ALA-7/ALA-58/ALA-112/ALA-147, AND MUTAGENESIS OF CYS-7; CYS-58;
CYS-112 AND CYS-147.
PubMed=17070542; DOI=10.1016/j.jmb.2006.09.048;
Hoernberg A., Logan D.T., Marklund S.L., Oliveberg M.;
"The coupling between disulphide status, metallation and dimer
interface strength in Cu/Zn superoxide dismutase.";
J. Mol. Biol. 365:333-342(2007).
[44]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT SER-81/SER-84 IN
COMPLEX WITH COPPER IONS, SUBUNIT, MUTAGENESIS OF HIS-81 AND ASP-84,
AND COFACTOR.
PubMed=17888947; DOI=10.1016/j.jmb.2007.07.043;
Roberts B.R., Tainer J.A., Getzoff E.D., Malencik D.A., Anderson S.R.,
Bomben V.C., Meyers K.R., Karplus P.A., Beckman J.S.;
"Structural characterization of zinc-deficient human superoxide
dismutase and implications for ALS.";
J. Mol. Biol. 373:877-890(2007).
[45]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC
IONS, SUBUNIT, AND FORMATION OF FIBRILLAR AGGREGATES BY ZINC-DEPLETED
SOD1.
PubMed=17548825; DOI=10.1073/pnas.0703857104;
Strange R.W., Yong C.W., Smith W., Hasnain S.S.;
"Molecular dynamics using atomic-resolution structure reveal
structural fluctuations that may lead to polymerization of human Cu-Zn
superoxide dismutase.";
Proc. Natl. Acad. Sci. U.S.A. 104:10040-10044(2007).
[46]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANT ALS1 ARG-86, AND
CHARACTERIZATION OF VARIANT ALS1 ARG-86.
PubMed=18378676; DOI=10.1074/jbc.M801522200;
Cao X., Antonyuk S.V., Seetharaman S.V., Whitson L.J., Taylor A.B.,
Holloway S.P., Strange R.W., Doucette P.A., Valentine J.S., Tiwari A.,
Hayward L.J., Padua S., Cohlberg J.A., Hasnain S.S., Hart P.J.;
"Structures of the G85R variant of SOD1 in familial amyotrophic
lateral sclerosis.";
J. Biol. Chem. 283:16169-16177(2008).
[47]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ALS1 ARG-86.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of human Cu-Zn superoxide dismutase mutant G85R
(P21).";
Submitted (APR-2008) to the PDB data bank.
[48]
REVIEW ON VARIANTS.
PubMed=8592323; DOI=10.1136/jmg.32.11.841;
de Belleroche J., Orrell R., King A.;
"Familial amyotrophic lateral sclerosis/motor neurone disease (FALS):
a review of current developments.";
J. Med. Genet. 32:841-847(1995).
[49]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
PubMed=20727846; DOI=10.1016/j.abb.2010.08.014;
Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J.;
"Structures of mouse SOD1 and human/mouse SOD1 chimeras.";
Arch. Biochem. Biophys. 503:183-190(2010).
[50]
VARIANTS ALS1.
PubMed=8446170; DOI=10.1038/362059a0;
Rosen D.R., Siddique T., Patterson D., Figlewicz D.A., Sapp P.,
Hentati A., Donaldson D., Goto J., O'Regan J.P., Deng H.-X.,
Rahmani Z., Krizus A., McKenna-Yasek D., Cayabyab A., Gaston S.M.,
Berger R., Tanzi R.E., Halperin J.J., Herzfeldt B., van den Bergh R.,
Hung W.-Y., Bird T., Deng G., Mulder D.W., Smyth C., Laing N.G.,
Soriano E., Pericak-Vance M.A., Haines J., Rouleau G.A., Gusella J.S.,
Horvitz H.R., Brown R.H. Jr.;
"Mutations in Cu/Zn superoxide dismutase gene are associated with
familial amyotrophic lateral sclerosis.";
Nature 362:59-62(1993).
[51]
ERRATUM.
PubMed=8332197;
Rosen D.R.;
Nature 364:362-362(1993).
[52]
VARIANTS ALS1.
PubMed=8351519; DOI=10.1126/science.8351519;
Deng H.-X., Hentati A., Tainer J.A., Iqbal Z., Cayabyab A.,
Hung W.-Y., Getzoff E.D., Hu P., Herzfeldt B., Roos R.P., Warner C.,
Deng G., Soriano E., Smyth C., Parge H.E., Ahmed A., Roses A.D.,
Hallewell R.A., Pericak-Vance M.A., Siddique T.;
"Amyotrophic lateral sclerosis and structural defects in Cu,Zn
superoxide dismutase.";
Science 261:1047-1051(1993).
[53]
VARIANT ALS1 THR-5.
PubMed=8179602; DOI=10.1006/bbrc.1994.1506;
Nakano R., Sato S., Inuzuka T., Sakimura K., Mishina M., Takahashi H.,
Ikuta F., Honma Y., Fujii J., Taniguchi N., Tsuji S.;
"A novel mutation in Cu/Zn superoxide dismutase gene in Japanese
familial amyotrophic lateral sclerosis.";
Biochem. Biophys. Res. Commun. 200:695-703(1994).
[54]
VARIANT ALS1 GLU-8.
PubMed=7980516; DOI=10.1006/bbrc.1994.2497;
Hirano M., Fujii J., Nagai Y., Sonobe M., Okamoto K., Araki H.,
Taniguchi N., Ueno S.;
"A new variant Cu/Zn superoxide dismutase (Val7-->Glu) deduced from
lymphocyte mRNA sequences from Japanese patients with familial
amyotrophic lateral sclerosis.";
Biochem. Biophys. Res. Commun. 204:572-577(1994).
[55]
VARIANT ALS1 LYS-22.
PubMed=8069312; DOI=10.1093/hmg/3.4.649;
Jones C.T., Swinger R.J., Brock D.J.H.;
"Identification of a novel SOD1 mutation in an apparently sporadic
amyotrophic lateral sclerosis patient and the detection of Ile113Thr
in three others.";
Hum. Mol. Genet. 3:649-650(1994).
[56]
VARIANTS ALS1 ASP-94 AND THR-113.
PubMed=7951252; DOI=10.1093/hmg/3.6.997;
Esteban J., Rosen D.R., Bowling A.C., Sapp P., McKenna-Yasek D.,
O'Regan J.P., Beal M.F., Horvitz H.R., Brown R.H. Jr.;
"Identification of two novel mutations and a new polymorphism in the
gene for Cu/Zn superoxide dismutase in patients with amyotrophic
lateral sclerosis.";
Hum. Mol. Genet. 3:997-998(1994).
[57]
VARIANT ALS1 GLY-116.
PubMed=7881433; DOI=10.1093/hmg/3.12.2261;
Kostrzewa M., Burck-Lehmann U., Mueller U.;
"Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in
the Cu/Zn superoxide dismutase-1 gene.";
Hum. Mol. Genet. 3:2261-2262(1994).
[58]
VARIANT ALS1 ARG-47.
PubMed=7836951; DOI=10.1016/0022-510X(94)90097-3;
Aoki M., Ogasawara M., Matsubara Y., Narisawa K., Nakamura S.,
Itoyama Y., Abe K.;
"Familial amyotrophic lateral sclerosis (ALS) in Japan associated with
H46R mutation in Cu/Zn superoxide dismutase gene: a possible new
subtype of familial ALS.";
J. Neurol. Sci. 126:77-83(1994).
[59]
VARIANT ALS1 THR-114.
PubMed=7997024; DOI=10.1016/S0140-6736(94)92913-0;
Suthers G., Laing N., Wilton S., Dorosz S., Waddy H.;
"'Sporadic' motoneuron disease due to familial SOD1 mutation with low
penetrance.";
Lancet 344:1773-1773(1994).
[60]
VARIANT ALS1 ASN-102.
PubMed=7870076; DOI=10.1006/mcpr.1994.1046;
Jones C.T., Shaw P.J., Chari G., Brock D.J.;
"Identification of a novel exon 4 SOD1 mutation in a sporadic
amyotrophic lateral sclerosis patient.";
Mol. Cell. Probes 8:329-330(1994).
[61]
VARIANTS ALS1.
PubMed=7887412;
Pramatarova A., Figlewicz D.A., Krizus A., Han F.Y.,
Ceballos-Picot I., Nicole A., Dib M., Meininger V., Brown R.H. Jr.,
Rouleau G.A.;
"Identification of new mutations in the Cu/Zn superoxide dismutase
gene of patients with familial amyotrophic lateral sclerosis.";
Am. J. Hum. Genet. 56:592-596(1995).
[62]
VARIANT ALS1 ILE-149.
PubMed=7795609; DOI=10.1093/hmg/4.3.491;
Ikeda M., Abe K., Aoki M., Ogasawara M., Kameya T., Watanabe M.,
Shoji M., Hirai S., Itoyama Y.;
"A novel point mutation in the Cu/Zn superoxide dismutase gene in a
patient with familial amyotrophic lateral sclerosis.";
Hum. Mol. Genet. 4:491-492(1995).
[63]
VARIANT ALS1 GLY-102.
PubMed=7655468; DOI=10.1093/hmg/4.6.1101;
Yulug I.G., Katsanis N., de Belleroche J., Collinge J., Fisher E.M.C.;
"An improved protocol for the analysis of SOD1 gene mutations, and a
new mutation in exon 4.";
Hum. Mol. Genet. 4:1101-1104(1995).
[64]
VARIANT ALS1 ALA-91.
PubMed=7655469; DOI=10.1093/hmg/4.6.1105;
Sjaelander A., Beckman G., Deng H.-X., Iqbal Z., Tainer J.A.,
Siddique T.;
"The D90A mutation results in a polymorphism of Cu,Zn superoxide
dismutase that is prevalent in northern Sweden and Finland.";
Hum. Mol. Genet. 4:1105-1108(1995).
[65]
VARIANTS ALS1 MET-15 AND VAL-85.
PubMed=7655471; DOI=10.1093/hmg/4.6.1113;
Deng H.-X., Tainer J.A., Mitsumoto H., Ohnishi A., He X., Hung W.-Y.,
Zhao Y., Juneja T., Hentati A., Siddique T.;
"Two novel SOD1 mutations in patients with familial amyotrophic
lateral sclerosis.";
Hum. Mol. Genet. 4:1113-1116(1995).
[66]
VARIANT ALS1 ARG-94.
PubMed=7700376; DOI=10.1038/374504a0;
Orrell R., de Belleroche J., Marklund S., Bowe F., Hallewell R.;
"A novel SOD mutant and ALS.";
Nature 374:504-505(1995).
[67]
VARIANT ALS1 ALA-91.
PubMed=7647793; DOI=10.1038/ng0595-61;
Andersen P.M., Nilsson P., Ala-Hurula V., Keraenen M.-L.,
Tarvainen I., Haltia T., Nilsson L., Binzer M., Forsgren L.,
Marklund S.L.;
"Amyotrophic lateral sclerosis associated with homozygosity for an
Asp90Ala mutation in CuZn-superoxide dismutase.";
Nat. Genet. 10:61-66(1995).
[68]
VARIANT ALS1 PHE-105.
PubMed=7501156; DOI=10.1212/WNL.45.11.2038;
Ikeda M., Abe K., Aoki M., Sahara M., Watanabe M., Shoji M.,
St George-Hyslop P.H., Hirai S., Itoyama Y.;
"Variable clinical symptoms in familial amyotrophic lateral sclerosis
with a novel point mutation in the Cu/Zn superoxide dismutase gene.";
Neurology 45:2038-2042(1995).
[69]
VARIANTS ALS1 SER-145; THR-146 AND PHE-LEU-GLN-119 INS.
PubMed=7496169; DOI=10.1016/0960-8966(95)00007-A;
Sapp P.C., Rosen D.R., Hosler B.A., Esteban J., McKenna-Yasek D.,
O'Regan J.P., Horvitz H.R., Brown R.H. Jr.;
"Identification of three novel mutations in the gene for Cu/Zn
superoxide dismutase in patients with familial amyotrophic lateral
sclerosis.";
Neuromuscul. Disord. 5:353-357(1995).
[70]
VARIANTS ALS1 VAL-94; VAL-125 AND GLU-134 DEL.
PubMed=8938700; DOI=10.1016/0960-8966(96)00353-7;
Hosler B.A., Nicholson G.A., Sapp P.C., Chin W., Orrell R.W.,
de Belleroche J.S., Esteban J., Hayward L.J., Mckenna-Yasek D.,
Yeung L., Cherryson A.K., Dench J.E., Wilton S.D., Laing N.G.,
Horvitz R.H., Brown R.H. Jr.;
"Three novel mutations and two variants in the gene for Cu/Zn
superoxide dismutase in familial amyotrophic lateral sclerosis.";
Neuromuscul. Disord. 6:361-366(1996).
[71]
VARIANT ALS1 PHE-7.
PubMed=8907321; DOI=10.1016/0304-3940(96)12378-8;
Morita M., Aoki M., Abe K., Hasegawa T., Sakuma R., Onodera Y.,
Ichikawa N., Nishizawa M., Itoyama Y.;
"A novel two-base mutation in the Cu/Zn superoxide dismutase gene
associated with familial amyotrophic lateral sclerosis in Japan.";
Neurosci. Lett. 205:79-82(1996).
[72]
VARIANT ALS1 ASN-135.
PubMed=8990014;
DOI=10.1002/(SICI)1098-1004(1997)9:1<69::AID-HUMU14>3.0.CO;2-N;
Watanabe M., Aoki M., Abe K., Shoji M., Lizuka T., Ikeda Y., Hirai S.,
Kurokawa K., Kato T., Sasaki H., Itoyama Y.;
"A novel missense point mutation (S134N) of the Cu/Zn superoxide
dismutase gene in a patient with familial motor neuron disease.";
Hum. Mutat. 9:69-71(1997).
[73]
VARIANT ALS1 SER-17.
PubMed=9101297;
DOI=10.1002/(SICI)1098-1004(1997)9:4<356::AID-HUMU9>3.0.CO;2-3;
Kawamata J., Shimohama S., Takano S., Harada K., Ueda K., Kimura J.;
"Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with
apparently sporadic young-onset amyotrophic lateral sclerosis.";
Hum. Mutat. 9:356-358(1997).
[74]
VARIANT ALS1 SER-73.
PubMed=9455977; DOI=10.1016/S0022-510X(97)00181-0;
Orrell R.W., Marklund S.L., deBelleroche J.S.;
"Familial ALS is associated with mutations in all exons of SOD1: a
novel mutation in exon 3 (Gly72Ser).";
J. Neurol. Sci. 153:46-49(1997).
[75]
VARIANT ALS1 THR-114.
PubMed=10732812; DOI=10.1007/s100480050016;
Kikugawa K., Nakano R., Inuzuka T., Kokubo Y., Narita Y., Kuzuhara S.,
Yoshida S., Tsuji S.;
"A missense mutation in the SOD1 gene in patients with amyotrophic
lateral sclerosis from the Kii Peninsula and its vicinity, Japan.";
Neurogenetics 1:113-115(1997).
[76]
VARIANT ALS1 GLN-9.
PubMed=9131652; DOI=10.1016/S0960-8966(96)00419-1;
Bereznai B., Winkler A., Borasio G.D., Gasser T.;
"A novel SOD1 mutation in an Austrian family with amyotrophic lateral
sclerosis.";
Neuromuscul. Disord. 7:113-116(1997).
[77]
CHARACTERIZATION OF VARIANTS ALS1 VAL-5; ARG-38; ARG-47; GLN-49;
ARG-86 AND THR-114.
PubMed=10400992; DOI=10.1093/hmg/8.8.1451;
Ratovitski T., Corson L.B., Strain J., Wong P., Cleveland D.W.,
Culotta V.C., Borchelt D.R.;
"Variation in the biochemical/biophysical properties of mutant
superoxide dismutase 1 enzymes and the rate of disease progression in
familial amyotrophic lateral sclerosis kindreds.";
Hum. Mol. Genet. 8:1451-1460(1999).
[78]
VARIANT ALS1 ARG-13.
PubMed=10430435; DOI=10.1212/WNL.53.2.404;
Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M.,
Bugiani O., Ajmar F., Garre C.;
"A SOD1 gene mutation in a patient with slowly progressing familial
ALS.";
Neurology 53:404-406(1999).
[79]
ERRATUM.
Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M.,
Bugiani O., Ajmar F., Garre C.;
Neurology 57:1146-1146(2001).
[80]
VARIANT ALS1 SER-127.
PubMed=11535232; DOI=10.1016/S0022-510X(01)00558-5;
Murakami T., Warita H., Hayashi T., Sato K., Manabe Y., Mizuno S.,
Yamane K., Abe K.;
"A novel SOD1 gene mutation in familial ALS with low penetrance in
females.";
J. Neurol. Sci. 189:45-47(2001).
[81]
VARIANT ALS1 CYS-46.
PubMed=11369193; DOI=10.1016/S0960-8966(00)00215-7;
Gellera C., Castellotti B., Riggio M.C., Silani V., Morandi L.,
Testa D., Casali C., Taroni F., Di Donato S., Zeviani M., Mariotti C.;
"Superoxide dismutase gene mutations in Italian patients with familial
and sporadic amyotrophic lateral sclerosis: identification of three
novel missense mutations.";
Neuromuscul. Disord. 11:404-410(2001).
[82]
VARIANT ALS1 ALA-81.
PubMed=12402272; DOI=10.1002/ana.10369;
Alexander M.D., Traynor B.J., Miller N., Corr B., Frost E.,
McQuaid S., Brett F.M., Green A., Hardiman O.;
"'True' sporadic ALS associated with a novel SOD-1 mutation.";
Ann. Neurol. 52:680-683(2002).
[83]
CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-47; ARG-86 AND ALA-94,
INTERACTION WITH RNF19A, AND UBIQUITINATION.
PubMed=12145308; DOI=10.1074/jbc.M206559200;
Niwa J., Ishigaki S., Hishikawa N., Yamamoto M., Doyu M., Murata S.,
Tanaka K., Taniguchi N., Sobue G.;
"Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated
neurotoxicity.";
J. Biol. Chem. 277:36793-36798(2002).
[84]
VARIANTS ALS1 VAL-9; CYS-21; LEU-23; ARG-49; ARG-55; ALA-88; THR-90;
MET-98; LEU-119; GLY-125 AND ARG-148.
PubMed=14506936; DOI=10.1080/14660820310011700;
Andersen P.M., Sims K.B., Xin W.W., Kiely R., O'Neill G., Ravits J.,
Pioro E., Harati Y., Brower R.D., Levine J.S., Heinicke H.U.,
Seltzer W., Boss M., Brown R.H. Jr.;
"Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in
amyotrophic lateral sclerosis: a decade of discoveries, defects and
disputes.";
Amyotroph. Lateral Scler. 4:62-73(2003).
[85]
CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-86 AND ARG-94,
MUTAGENESIS OF CYS-7; 51-PHE-GLY-52; CYS-58; HIS-81; ASP-84; CYS-112
AND CYS-147, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18552350; DOI=10.1074/jbc.M802083200;
Furukawa Y., Kaneko K., Yamanaka K., O'Halloran T.V., Nukina N.;
"Complete loss of post-translational modifications triggers fibrillar
aggregation of SOD1 in the familial form of amyotrophic lateral
sclerosis.";
J. Biol. Chem. 283:24167-24176(2008).
[86]
CHARACTERIZATION OF VARIANTS ALS1 ARG-55; ALA-91; ALA-94; ASP-94;
MET-98 AND PHE-145.
PubMed=18301754; DOI=10.1371/journal.pone.0001677;
Banci L., Bertini I., Boca M., Girotto S., Martinelli M.,
Valentine J.S., Vieru M.;
"SOD1 and amyotrophic lateral sclerosis: mutations and
oligomerization.";
PLoS ONE 3:E1677-E1677(2008).
[87]
CHARACTERIZATION OF VARIANTS ALS1 ARG-86 AND ALA-94, UBIQUITINATION BY
MARCH5, AND SUBCELLULAR LOCATION.
PubMed=19741096; DOI=10.1091/mbc.E09-02-0112;
Yonashiro R., Sugiura A., Miyachi M., Fukuda T., Matsushita N.,
Inatome R., Ogata Y., Suzuki T., Dohmae N., Yanagi S.;
"Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and
attenuates mutant SOD1-induced reactive oxygen species generation.";
Mol. Biol. Cell 20:4524-4530(2009).
[88]
VARIANT ALS1 PRO-68.
PubMed=21247266; DOI=10.3109/17482968.2011.551939;
del Grande A., Luigetti M., Conte A., Mancuso I., Lattante S.,
Marangi G., Stipa G., Zollino M., Sabatelli M.;
"A novel L67P SOD1 mutation in an Italian ALS patient.";
Amyotroph. Lateral Scler. 12:150-152(2011).
[89]
VARIANT ALS1 GLY-96.
PubMed=21220647; DOI=10.1001/archneurol.2010.352;
Chio A., Borghero G., Pugliatti M., Ticca A., Calvo A., Moglia C.,
Mutani R., Brunetti M., Ossola I., Marrosu M.G., Murru M.R.,
Floris G., Cannas A., Parish L.D., Cossu P., Abramzon Y.,
Johnson J.O., Nalls M.A., Arepalli S., Chong S., Hernandez D.G.,
Traynor B.J., Restagno G.;
"Large proportion of amyotrophic lateral sclerosis cases in Sardinia
due to a single founder mutation of the TARDBP gene.";
Arch. Neurol. 68:594-598(2011).
[90]
VARIANTS ALS1 SER-87; ALA-88; ASN-102; GLY-102 AND TYR-112.
PubMed=27604643; DOI=10.1038/srep32478;
Hou L., Jiao B., Xiao T., Zhou L., Zhou Z., Du J., Yan X., Wang J.,
Tang B., Shen L.;
"Screening of SOD1, FUS and TARDBP genes in patients with amyotrophic
lateral sclerosis in central-southern China.";
Sci. Rep. 6:32478-32478(2016).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000269|PubMed:17888947};
Note=Binds 1 copper ion per subunit.
{ECO:0000269|PubMed:17888947};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:17888947};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17888947};
-!- SUBUNIT: Homodimer; non-disulfide linked. Homodimerization may
take place via the ditryptophan cross-link at Trp-33. The
pathogenic variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94
interact with RNF19A, whereas wild-type protein does not. The
pathogenic variants ALS1 Arg-86 and Ala-94 interact with MARCH5,
whereas wild-type protein does not. {ECO:0000269|PubMed:10329151,
ECO:0000269|PubMed:12911296, ECO:0000269|PubMed:12963370,
ECO:0000269|PubMed:15326189, ECO:0000269|PubMed:16291742,
ECO:0000269|PubMed:16406071, ECO:0000269|PubMed:17548825,
ECO:0000269|PubMed:17888947, ECO:0000269|PubMed:20600836,
ECO:0000269|PubMed:20727846}.
-!- INTERACTION:
Self; NbExp=19; IntAct=EBI-990792, EBI-990792;
P26339:Chga (xeno); NbExp=5; IntAct=EBI-990792, EBI-990900;
P16014:Chgb (xeno); NbExp=6; IntAct=EBI-990792, EBI-990820;
Q8TCX1:DYNC2LI1; NbExp=3; IntAct=EBI-990792, EBI-8568003;
P20029:Hspa5 (xeno); NbExp=7; IntAct=EBI-990792, EBI-772325;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19741096}.
Mitochondrion {ECO:0000269|PubMed:19741096}. Nucleus
{ECO:0000269|PubMed:22496122}. Note=Predominantly cytoplasmic; the
pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates
and accumulates in mitochondria. {ECO:0000269|PubMed:19741096}.
-!- PTM: Unlike wild-type protein, the pathogenic variants ALS1 Arg-
38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A
leading to their proteasomal degradation. The pathogenic variants
ALS1 Arg-86 and Ala-94 are ubiquitinated by MARCH5 leading to
their proteasomal degradation. {ECO:0000269|PubMed:12145308,
ECO:0000269|PubMed:19741096}.
-!- PTM: The ditryptophan cross-link at Trp-33 is responsible for the
non-disulfide-linked homodimerization. Such modification might
only occur in extreme conditions and additional experimental
evidence is required. {ECO:0000269|PubMed:20600836}.
-!- PTM: Palmitoylation helps nuclear targeting and decreases
catalytic activity. {ECO:0000269|PubMed:22496122}.
-!- PTM: Succinylation, adjacent to copper catalytic site, probably
inhibits activity. Desuccinylation by SIRT5 enhances activity.
{ECO:0000269|PubMed:24140062}.
-!- DISEASE: Amyotrophic lateral sclerosis 1 (ALS1) [MIM:105400]: A
neurodegenerative disorder affecting upper motor neurons in the
brain and lower motor neurons in the brain stem and spinal cord,
resulting in fatal paralysis. Sensory abnormalities are absent.
The pathologic hallmarks of the disease include pallor of the
corticospinal tract due to loss of motor neurons, presence of
ubiquitin-positive inclusions within surviving motor neurons, and
deposition of pathologic aggregates. The etiology of amyotrophic
lateral sclerosis is likely to be multifactorial, involving both
genetic and environmental factors. The disease is inherited in 5-
10% of the cases. {ECO:0000269|PubMed:10400992,
ECO:0000269|PubMed:10430435, ECO:0000269|PubMed:10732812,
ECO:0000269|PubMed:11369193, ECO:0000269|PubMed:11535232,
ECO:0000269|PubMed:12145308, ECO:0000269|PubMed:12402272,
ECO:0000269|PubMed:12754496, ECO:0000269|PubMed:12963370,
ECO:0000269|PubMed:14506936, ECO:0000269|PubMed:15056757,
ECO:0000269|PubMed:18301754, ECO:0000269|PubMed:18378676,
ECO:0000269|PubMed:18552350, ECO:0000269|PubMed:19741096,
ECO:0000269|PubMed:21220647, ECO:0000269|PubMed:21247266,
ECO:0000269|PubMed:27604643, ECO:0000269|PubMed:7496169,
ECO:0000269|PubMed:7501156, ECO:0000269|PubMed:7647793,
ECO:0000269|PubMed:7655468, ECO:0000269|PubMed:7655469,
ECO:0000269|PubMed:7655471, ECO:0000269|PubMed:7700376,
ECO:0000269|PubMed:7795609, ECO:0000269|PubMed:7836951,
ECO:0000269|PubMed:7870076, ECO:0000269|PubMed:7881433,
ECO:0000269|PubMed:7887412, ECO:0000269|PubMed:7951252,
ECO:0000269|PubMed:7980516, ECO:0000269|PubMed:7997024,
ECO:0000269|PubMed:8069312, ECO:0000269|PubMed:8179602,
ECO:0000269|PubMed:8351519, ECO:0000269|PubMed:8446170,
ECO:0000269|PubMed:8528216, ECO:0000269|PubMed:8682505,
ECO:0000269|PubMed:8907321, ECO:0000269|PubMed:8938700,
ECO:0000269|PubMed:8990014, ECO:0000269|PubMed:9101297,
ECO:0000269|PubMed:9131652, ECO:0000269|PubMed:9455977,
ECO:0000269|PubMed:9541385}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The protein (both wild-type and ALS1 variants) has
a tendency to form fibrillar aggregates in the absence of the
intramolecular disulfide bond or of bound zinc ions. These
aggregates may have cytotoxic effects. Zinc binding promotes
dimerization and stabilizes the native form.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Alsod; Note=ALS genetic mutations db;
URL="http://alsod.iop.kcl.ac.uk/Als/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/sod1/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Superoxide dismutase entry;
URL="https://en.wikipedia.org/wiki/Superoxide_dismutase";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L44139; AAB05662.1; -; Genomic_DNA.
EMBL; L44135; AAB05662.1; JOINED; Genomic_DNA.
EMBL; L44136; AAB05662.1; JOINED; Genomic_DNA.
EMBL; L44137; AAB05662.1; JOINED; Genomic_DNA.
EMBL; L44139; AAB05661.1; -; Genomic_DNA.
EMBL; L44135; AAB05661.1; JOINED; Genomic_DNA.
EMBL; L44136; AAB05661.1; JOINED; Genomic_DNA.
EMBL; L44137; AAB05661.1; JOINED; Genomic_DNA.
EMBL; X02317; CAA26182.1; -; mRNA.
EMBL; X01780; CAA25915.1; -; Genomic_DNA.
EMBL; X01781; CAA25916.1; -; Genomic_DNA.
EMBL; X01782; CAA25917.1; ALT_SEQ; Genomic_DNA.
EMBL; X01783; CAA25918.1; -; Genomic_DNA.
EMBL; X01784; CAA25919.1; ALT_SEQ; Genomic_DNA.
EMBL; AY049787; AAL15444.1; -; mRNA.
EMBL; AY450286; AAR21563.1; -; mRNA.
EMBL; EF151142; ABL96616.1; -; mRNA.
EMBL; AK312116; BAG35052.1; -; mRNA.
EMBL; CR450355; CAG29351.1; -; mRNA.
EMBL; CR541742; CAG46542.1; -; mRNA.
EMBL; BT006676; AAP35322.1; -; mRNA.
EMBL; AY835629; AAV80422.1; -; Genomic_DNA.
EMBL; AP000253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09889.1; -; Genomic_DNA.
EMBL; CH471079; EAX09890.1; -; Genomic_DNA.
EMBL; BC001034; AAH01034.1; -; mRNA.
EMBL; L46374; AAB59626.1; -; Genomic_DNA.
EMBL; L46375; AAB59627.1; -; Genomic_DNA.
EMBL; L44746; AAC41773.1; ALT_SEQ; Genomic_DNA.
EMBL; X95228; CAA64520.1; -; Genomic_DNA.
CCDS; CCDS33536.1; -.
PIR; A22703; DSHUCZ.
RefSeq; NP_000445.1; NM_000454.4.
UniGene; Hs.443914; -.
PDB; 1AZV; X-ray; 1.90 A; A/B=2-154.
PDB; 1BA9; NMR; -; A=2-154.
PDB; 1DSW; NMR; -; A=2-154.
PDB; 1FUN; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J=2-154.
PDB; 1HL4; X-ray; 1.82 A; A/B/C/D=2-154.
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.
PDB; 1KMG; NMR; -; A=2-154.
PDB; 1L3N; NMR; -; A/B=2-154.
PDB; 1MFM; X-ray; 1.02 A; A=2-154.
PDB; 1N18; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=1-154.
PDB; 1N19; X-ray; 1.86 A; A/B=1-154.
PDB; 1OEZ; X-ray; 2.15 A; W/X/Y/Z=2-154.
PDB; 1OZT; X-ray; 2.50 A; G/H/I/J/K/L/M/N=2-154.
PDB; 1OZU; X-ray; 1.30 A; A/B=2-154.
PDB; 1P1V; X-ray; 1.40 A; A/B/C=2-154.
PDB; 1PTZ; X-ray; 1.80 A; A/B=2-154.
PDB; 1PU0; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-154.
PDB; 1RK7; NMR; -; A=2-154.
PDB; 1SOS; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=2-154.
PDB; 1SPD; X-ray; 2.40 A; A/B=2-154.
PDB; 1UXL; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J=2-154.
PDB; 1UXM; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154.
PDB; 2AF2; NMR; -; A/B=2-154.
PDB; 2C9S; X-ray; 1.24 A; A/F=2-154.
PDB; 2C9U; X-ray; 1.24 A; A/F=2-154.
PDB; 2C9V; X-ray; 1.07 A; A/F=2-154.
PDB; 2GBT; X-ray; 1.70 A; A/B/C/D=2-154.
PDB; 2GBU; X-ray; 2.00 A; A/B/C/D=2-154.
PDB; 2GBV; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=2-154.
PDB; 2LU5; NMR; -; A=2-154.
PDB; 2MP3; NMR; -; A=2-126.
PDB; 2NAM; NMR; -; A=2-154.
PDB; 2NNX; X-ray; 2.30 A; A/B/C/D=2-154.
PDB; 2R27; X-ray; 2.00 A; A/B=1-154.
PDB; 2V0A; X-ray; 1.15 A; A/F=2-154.
PDB; 2VR6; X-ray; 1.30 A; A/F=2-154.
PDB; 2VR7; X-ray; 1.58 A; A/F=2-154.
PDB; 2VR8; X-ray; 1.36 A; A/F=2-154.
PDB; 2WKO; X-ray; 1.97 A; A/F=2-154.
PDB; 2WYT; X-ray; 1.00 A; A/F=2-154.
PDB; 2WYZ; X-ray; 1.70 A; A/F=2-154.
PDB; 2WZ0; X-ray; 1.72 A; A/F=2-154.
PDB; 2WZ5; X-ray; 1.50 A; A/F=2-154.
PDB; 2WZ6; X-ray; 1.55 A; A/F=2-154.
PDB; 2XJK; X-ray; 1.45 A; A=2-154.
PDB; 2XJL; X-ray; 1.55 A; A=2-154.
PDB; 2ZKW; X-ray; 1.90 A; A/B=1-154.
PDB; 2ZKX; X-ray; 2.72 A; A/B/C/D=1-154.
PDB; 2ZKY; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-154.
PDB; 3CQP; X-ray; 1.95 A; A/B/C/D=2-154.
PDB; 3CQQ; X-ray; 1.90 A; A/B=2-154.
PDB; 3ECU; X-ray; 1.90 A; A/B/C/D=2-154.
PDB; 3ECV; X-ray; 1.90 A; A/B/C/D=2-154.
PDB; 3ECW; X-ray; 2.15 A; A/B/C/D=2-154.
PDB; 3GQF; X-ray; 2.20 A; A/B/C/D/E/F=2-154.
PDB; 3GTV; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-81.
PDB; 3GZO; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=2-154.
PDB; 3GZP; X-ray; 3.10 A; A/B/C/D=2-154.
PDB; 3GZQ; X-ray; 1.40 A; A/B=2-154.
PDB; 3H2P; X-ray; 1.55 A; A/B=2-154.
PDB; 3H2Q; X-ray; 1.85 A; A/B/C/D=2-154.
PDB; 3HFF; X-ray; 2.20 A; A=2-154.
PDB; 3K91; X-ray; 1.75 A; A/B=2-154.
PDB; 3KH3; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154.
PDB; 3KH4; X-ray; 3.50 A; A/B/C/D/E/F=2-154.
PDB; 3LTV; X-ray; 2.45 A; A/B/C/D/E/F=82-154.
PDB; 3QQD; X-ray; 1.65 A; A/B=2-154.
PDB; 3RE0; X-ray; 2.28 A; A/B/C/D=2-154.
PDB; 3T5W; X-ray; 1.80 A; A/B/D/E/F/G/H/I/J/K/L/M=2-154.
PDB; 4A7G; X-ray; 1.24 A; A/F=2-154.
PDB; 4A7Q; X-ray; 1.22 A; A/F=2-154.
PDB; 4A7S; X-ray; 1.06 A; A/F=2-154.
PDB; 4A7T; X-ray; 1.45 A; A/F=2-154.
PDB; 4A7U; X-ray; 0.98 A; A/F=2-154.
PDB; 4A7V; X-ray; 1.00 A; A/F=2-154.
PDB; 4B3E; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J=1-154.
PDB; 4BCY; X-ray; 1.27 A; A=2-154.
PDB; 4BCZ; X-ray; 1.93 A; A/B=2-49, A/B=83-124, A/B=141-154.
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.
PDB; 4FF9; X-ray; 2.50 A; A/B=2-154.
PDB; 4MCM; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154.
PDB; 4MCN; X-ray; 2.60 A; A/B=2-154.
PDB; 4NIN; X-ray; 1.40 A; A=102-108.
PDB; 4NIO; X-ray; 1.30 A; A=148-154.
PDB; 4NIP; X-ray; 1.90 A; A=148-154.
PDB; 4OH2; X-ray; 2.38 A; A/B/C/D/E/F/G/H/I/J=2-154.
PDB; 4SOD; Model; -; A=1-154.
PDB; 4XCR; X-ray; 3.60 A; A/B=2-154.
PDB; 5DLI; X-ray; 2.10 A; A/B/C/D/E/F/G/H=29-39.
PDB; 5IIW; X-ray; 2.00 A; A/B/C/D/E/F/G/H=29-39.
PDB; 5J07; X-ray; 2.00 A; A/B=14-49, A/B=84-124, A/B=141-154.
PDB; 5J0C; X-ray; 1.60 A; A/B=29-49, A/B=84-124.
PDB; 5J0F; X-ray; 1.25 A; A/B=83-124.
PDB; 5J0G; X-ray; 2.50 A; A/B=2-124.
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.
PDB; 5U9M; X-ray; 2.35 A; A/C=2-154.
PDBsum; 1AZV; -.
PDBsum; 1BA9; -.
PDBsum; 1DSW; -.
PDBsum; 1FUN; -.
PDBsum; 1HL4; -.
PDBsum; 1HL5; -.
PDBsum; 1KMG; -.
PDBsum; 1L3N; -.
PDBsum; 1MFM; -.
PDBsum; 1N18; -.
PDBsum; 1N19; -.
PDBsum; 1OEZ; -.
PDBsum; 1OZT; -.
PDBsum; 1OZU; -.
PDBsum; 1P1V; -.
PDBsum; 1PTZ; -.
PDBsum; 1PU0; -.
PDBsum; 1RK7; -.
PDBsum; 1SOS; -.
PDBsum; 1SPD; -.
PDBsum; 1UXL; -.
PDBsum; 1UXM; -.
PDBsum; 2AF2; -.
PDBsum; 2C9S; -.
PDBsum; 2C9U; -.
PDBsum; 2C9V; -.
PDBsum; 2GBT; -.
PDBsum; 2GBU; -.
PDBsum; 2GBV; -.
PDBsum; 2LU5; -.
PDBsum; 2MP3; -.
PDBsum; 2NAM; -.
PDBsum; 2NNX; -.
PDBsum; 2R27; -.
PDBsum; 2V0A; -.
PDBsum; 2VR6; -.
PDBsum; 2VR7; -.
PDBsum; 2VR8; -.
PDBsum; 2WKO; -.
PDBsum; 2WYT; -.
PDBsum; 2WYZ; -.
PDBsum; 2WZ0; -.
PDBsum; 2WZ5; -.
PDBsum; 2WZ6; -.
PDBsum; 2XJK; -.
PDBsum; 2XJL; -.
PDBsum; 2ZKW; -.
PDBsum; 2ZKX; -.
PDBsum; 2ZKY; -.
PDBsum; 3CQP; -.
PDBsum; 3CQQ; -.
PDBsum; 3ECU; -.
PDBsum; 3ECV; -.
PDBsum; 3ECW; -.
PDBsum; 3GQF; -.
PDBsum; 3GTV; -.
PDBsum; 3GZO; -.
PDBsum; 3GZP; -.
PDBsum; 3GZQ; -.
PDBsum; 3H2P; -.
PDBsum; 3H2Q; -.
PDBsum; 3HFF; -.
PDBsum; 3K91; -.
PDBsum; 3KH3; -.
PDBsum; 3KH4; -.
PDBsum; 3LTV; -.
PDBsum; 3QQD; -.
PDBsum; 3RE0; -.
PDBsum; 3T5W; -.
PDBsum; 4A7G; -.
PDBsum; 4A7Q; -.
PDBsum; 4A7S; -.
PDBsum; 4A7T; -.
PDBsum; 4A7U; -.
PDBsum; 4A7V; -.
PDBsum; 4B3E; -.
PDBsum; 4BCY; -.
PDBsum; 4BCZ; -.
PDBsum; 4BD4; -.
PDBsum; 4FF9; -.
PDBsum; 4MCM; -.
PDBsum; 4MCN; -.
PDBsum; 4NIN; -.
PDBsum; 4NIO; -.
PDBsum; 4NIP; -.
PDBsum; 4OH2; -.
PDBsum; 4SOD; -.
PDBsum; 4XCR; -.
PDBsum; 5DLI; -.
PDBsum; 5IIW; -.
PDBsum; 5J07; -.
PDBsum; 5J0C; -.
PDBsum; 5J0F; -.
PDBsum; 5J0G; -.
PDBsum; 5K02; -.
PDBsum; 5U9M; -.
DisProt; DP00652; -.
ProteinModelPortal; P00441; -.
SMR; P00441; -.
BioGrid; 112530; 164.
DIP; DIP-44941N; -.
IntAct; P00441; 39.
MINT; MINT-204523; -.
STRING; 9606.ENSP00000270142; -.
BindingDB; P00441; -.
ChEMBL; CHEMBL2354; -.
DrugBank; DB05025; Arimoclomol.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB03382; S-Oxy Cysteine.
DrugBank; DB00163; Vitamin E.
iPTMnet; P00441; -.
PhosphoSitePlus; P00441; -.
SwissPalm; P00441; -.
BioMuta; SOD1; -.
DOSAC-COBS-2DPAGE; P00441; -.
OGP; P00441; -.
REPRODUCTION-2DPAGE; IPI00783680; -.
SWISS-2DPAGE; P00441; -.
UCD-2DPAGE; P00441; -.
EPD; P00441; -.
PaxDb; P00441; -.
PeptideAtlas; P00441; -.
PRIDE; P00441; -.
TopDownProteomics; P00441; -.
DNASU; 6647; -.
Ensembl; ENST00000270142; ENSP00000270142; ENSG00000142168.
GeneID; 6647; -.
KEGG; hsa:6647; -.
CTD; 6647; -.
DisGeNET; 6647; -.
EuPathDB; HostDB:ENSG00000142168.14; -.
GeneCards; SOD1; -.
GeneReviews; SOD1; -.
HGNC; HGNC:11179; SOD1.
HPA; CAB008670; -.
HPA; HPA001401; -.
MalaCards; SOD1; -.
MIM; 105400; phenotype.
MIM; 147450; gene.
neXtProt; NX_P00441; -.
OpenTargets; ENSG00000142168; -.
Orphanet; 803; Amyotrophic lateral sclerosis.
PharmGKB; PA334; -.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOVERGEN; HBG000062; -.
InParanoid; P00441; -.
KO; K04565; -.
OMA; IHTFGDN; -.
OrthoDB; EOG091G0OG2; -.
PhylomeDB; P00441; -.
TreeFam; TF105131; -.
BioCyc; MetaCyc:HS06899-MONOMER; -.
BRENDA; 1.15.1.1; 2681.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SIGNOR; P00441; -.
ChiTaRS; SOD1; human.
EvolutionaryTrace; P00441; -.
GeneWiki; SOD1; -.
GenomeRNAi; 6647; -.
PRO; PR:P00441; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000142168; -.
CleanEx; HS_SOD1; -.
ExpressionAtlas; P00441; baseline and differential.
Genevisible; P00441; HS.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB.
GO; GO:0031045; C:dense core granule; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
GO; GO:0005759; C:mitochondrial matrix; NAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
GO; GO:0030346; F:protein phosphatase 2B binding; IDA:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; ISS:BHF-UCL.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
GO; GO:0007569; P:cell aging; IMP:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
GO; GO:0060047; P:heart contraction; IDA:UniProtKB.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IDA:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB.
GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB.
GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB.
GO; GO:0001890; P:placenta development; NAS:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; IC:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:UniProtKB.
GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:0046620; P:regulation of organ growth; NAS:UniProtKB.
GO; GO:0045859; P:regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0033081; P:regulation of T cell differentiation in thymus; NAS:UniProtKB.
GO; GO:0060087; P:relaxation of vascular smooth muscle; ISS:UniProtKB.
GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl.
GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; ISS:UniProtKB.
GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
GO; GO:0009408; P:response to heat; ISS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
GO; GO:0000303; P:response to superoxide; IDA:UniProtKB.
GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; ISS:BHF-UCL.
GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
GO; GO:0006801; P:superoxide metabolic process; IDA:BHF-UCL.
GO; GO:0048538; P:thymus development; NAS:UniProtKB.
GO; GO:0019226; P:transmission of nerve impulse; ISS:UniProtKB.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00087; SOD_CU_ZN_1; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Amyotrophic lateral sclerosis; Antioxidant;
Complete proteome; Copper; Cytoplasm; Direct protein sequencing;
Disease mutation; Disulfide bond; Lipoprotein; Metal-binding;
Mitochondrion; Neurodegeneration; Nucleus; Oxidoreductase; Palmitate;
Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:6770891,
ECO:0000269|PubMed:7002610}.
CHAIN 2 154 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000164057.
METAL 47 47 Copper; catalytic.
{ECO:0000269|PubMed:12963370,
ECO:0000269|PubMed:17548825}.
METAL 49 49 Copper; catalytic.
{ECO:0000269|PubMed:12963370,
ECO:0000269|PubMed:17548825}.
METAL 64 64 Copper; catalytic.
{ECO:0000269|PubMed:12963370,
ECO:0000269|PubMed:17548825}.
METAL 64 64 Zinc; via pros nitrogen.
{ECO:0000269|PubMed:20727846}.
METAL 72 72 Zinc; via pros nitrogen.
{ECO:0000269|PubMed:20727846}.
METAL 81 81 Zinc; via pros nitrogen.
{ECO:0000269|PubMed:20727846}.
METAL 84 84 Zinc; structural.
{ECO:0000269|PubMed:20727846}.
METAL 121 121 Copper; catalytic.
{ECO:0000269|PubMed:12963370,
ECO:0000269|PubMed:17548825}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:1463506,
ECO:0000269|PubMed:7002610}.
MOD_RES 4 4 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 10 10 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 92 92 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000250|UniProtKB:P07632}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 123 123 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:24140062}.
MOD_RES 137 137 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
MOD_RES 137 137 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P08228}.
LIPID 7 7 S-palmitoyl cysteine.
{ECO:0000269|PubMed:22496122}.
DISULFID 58 147 {ECO:0000269|PubMed:12963370,
ECO:0000269|PubMed:1463506,
ECO:0000269|PubMed:15326189,
ECO:0000269|PubMed:16406071}.
CROSSLNK 33 33 1-(tryptophan-3-yl)-tryptophan (Trp-Trp)
(interchain with W-33).
{ECO:0000269|PubMed:20600836}.
VARIANT 5 5 A -> S (in ALS1).
/FTId=VAR_013518.
VARIANT 5 5 A -> T (in ALS1; dbSNP:rs121912444).
{ECO:0000269|PubMed:8179602}.
/FTId=VAR_007130.
VARIANT 5 5 A -> V (in ALS1; severe form; reduces
structural stability and enzyme activity;
increases tendency to form fibrillar
aggregates; dbSNP:rs121912442).
{ECO:0000269|PubMed:10400992,
ECO:0000269|PubMed:12963370,
ECO:0000269|PubMed:15056757}.
/FTId=VAR_007131.
VARIANT 7 7 C -> F (in ALS1; dbSNP:rs121912448).
{ECO:0000269|PubMed:8907321}.
/FTId=VAR_008717.
VARIANT 8 8 V -> E (in ALS1).
{ECO:0000269|PubMed:7980516}.
/FTId=VAR_007132.
VARIANT 9 9 L -> Q (in ALS1).
{ECO:0000269|PubMed:9131652}.
/FTId=VAR_013519.
VARIANT 9 9 L -> V (in ALS1).
{ECO:0000269|PubMed:14506936}.
/FTId=VAR_013520.
VARIANT 13 13 G -> R (in ALS1; dbSNP:rs121912456).
{ECO:0000269|PubMed:10430435}.
/FTId=VAR_013521.
VARIANT 15 15 V -> G (in ALS1).
/FTId=VAR_013522.
VARIANT 15 15 V -> M (in ALS1).
{ECO:0000269|PubMed:7655471}.
/FTId=VAR_007133.
VARIANT 17 17 G -> S (in ALS1; sporadic young onset;
dbSNP:rs121912453).
{ECO:0000269|PubMed:9101297}.
/FTId=VAR_007134.
VARIANT 21 21 F -> C (in ALS1).
{ECO:0000269|PubMed:14506936}.
/FTId=VAR_045876.
VARIANT 22 22 E -> G (in ALS1).
/FTId=VAR_013523.
VARIANT 22 22 E -> K (in ALS1; dbSNP:rs121912450).
{ECO:0000269|PubMed:8069312}.
/FTId=VAR_007135.
VARIANT 23 23 Q -> L (in ALS1).
{ECO:0000269|PubMed:14506936}.
/FTId=VAR_045877.
VARIANT 38 38 G -> R (in ALS1; mild form; ubiquitinated
by RNF19A. Ubiquitinated by MARCH5;
leading to the degradation of
mitochondrial SOD1; dbSNP:rs121912431).
{ECO:0000269|PubMed:10400992,
ECO:0000269|PubMed:12145308,
ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:9541385}.
/FTId=VAR_007136.
VARIANT 39 39 L -> R (in ALS1).
/FTId=VAR_013524.
VARIANT 39 39 L -> V (in ALS1; dbSNP:rs121912432).
/FTId=VAR_007137.
VARIANT 42 42 G -> D (in ALS1; dbSNP:rs121912434).
/FTId=VAR_007139.
VARIANT 42 42 G -> S (in ALS1; dbSNP:rs121912433).
/FTId=VAR_007138.
VARIANT 44 44 H -> R (in ALS1; reduces structural
stability and enzyme activity; increases
tendency to form fibrillar aggregates;
dbSNP:rs121912435).
{ECO:0000269|PubMed:12963370}.
/FTId=VAR_007140.
VARIANT 46 46 F -> C (in ALS1; slow progression;
dbSNP:rs121912457).
{ECO:0000269|PubMed:11369193}.
/FTId=VAR_013525.
VARIANT 47 47 H -> R (in ALS1; "benign" form; 80% of
wild-type activity; ubiquitinated by
RNF19A; dbSNP:rs121912443).
{ECO:0000269|PubMed:10400992,
ECO:0000269|PubMed:12145308,
ECO:0000269|PubMed:12754496,
ECO:0000269|PubMed:7836951}.
/FTId=VAR_007141.
VARIANT 49 49 H -> Q (in ALS1).
{ECO:0000269|PubMed:10400992,
ECO:0000269|PubMed:8528216}.
/FTId=VAR_007142.
VARIANT 49 49 H -> R (in ALS1).
{ECO:0000269|PubMed:14506936}.
/FTId=VAR_045878.
VARIANT 50 50 E -> K (in ALS1).
/FTId=VAR_013526.
VARIANT 55 55 T -> R (in ALS1; reduces tendency to form
fibrillar aggregates).
{ECO:0000269|PubMed:14506936,
ECO:0000269|PubMed:18301754}.
/FTId=VAR_045879.
VARIANT 66 66 N -> S (in ALS1).
/FTId=VAR_013527.
VARIANT 68 68 L -> P (in ALS1).
{ECO:0000269|PubMed:21247266}.
/FTId=VAR_065560.
VARIANT 68 68 L -> R (in ALS1).
/FTId=VAR_013528.
VARIANT 73 73 G -> S (in ALS1; dbSNP:rs121912455).
{ECO:0000269|PubMed:9455977}.
/FTId=VAR_008718.
VARIANT 77 77 D -> Y (in ALS1).
/FTId=VAR_013529.
VARIANT 81 81 H -> A (in ALS1; sporadic form;
interferes with zinc binding; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:12402272}.
/FTId=VAR_016874.
VARIANT 85 85 L -> F (in ALS1).
/FTId=VAR_013530.
VARIANT 85 85 L -> V (in ALS1; dbSNP:rs121912452).
{ECO:0000269|PubMed:7655471}.
/FTId=VAR_007143.
VARIANT 86 86 G -> R (in ALS1; ubiquitinated by RNF19A;
interferes with zinc-binding;
ubiquitinated by MARCH5; leading to the
degradation of mitochondrial SOD1;
dbSNP:rs121912436).
{ECO:0000269|PubMed:10400992,
ECO:0000269|PubMed:12145308,
ECO:0000269|PubMed:18378676,
ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:19741096,
ECO:0000269|Ref.47}.
/FTId=VAR_007144.
VARIANT 87 87 N -> S (in ALS1; dbSNP:rs11556620).
{ECO:0000269|PubMed:27604643}.
/FTId=VAR_013531.
VARIANT 88 88 V -> A (in ALS1).
{ECO:0000269|PubMed:14506936,
ECO:0000269|PubMed:27604643}.
/FTId=VAR_045880.
VARIANT 90 90 A -> T (in ALS1).
{ECO:0000269|PubMed:14506936}.
/FTId=VAR_045881.
VARIANT 90 90 A -> V (in ALS1).
/FTId=VAR_013532.
VARIANT 91 91 D -> A (in ALS1; does not seem to be
linked with a decrease in activity;
dbSNP:rs80265967).
{ECO:0000269|PubMed:18301754,
ECO:0000269|PubMed:7647793,
ECO:0000269|PubMed:7655469}.
/FTId=VAR_007145.
VARIANT 91 91 D -> V (in ALS1).
/FTId=VAR_013533.
VARIANT 94 94 G -> A (in ALS1; increases tendency to
form fibrillar aggregates; ubiquitinated
by RNF19A; dbSNP:rs121912438).
{ECO:0000269|PubMed:12145308,
ECO:0000269|PubMed:18301754,
ECO:0000269|PubMed:19741096}.
/FTId=VAR_007146.
VARIANT 94 94 G -> C (in ALS1; dbSNP:rs121912437).
/FTId=VAR_007147.
VARIANT 94 94 G -> D (in ALS1).
{ECO:0000269|PubMed:18301754,
ECO:0000269|PubMed:7951252}.
/FTId=VAR_007148.
VARIANT 94 94 G -> R (in ALS1; 30% of wild-type
activity; dbSNP:rs121912437).
{ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:7700376,
ECO:0000269|PubMed:8528216}.
/FTId=VAR_007149.
VARIANT 94 94 G -> V (in ALS1).
{ECO:0000269|PubMed:8938700}.
/FTId=VAR_008719.
VARIANT 96 96 A -> G (in ALS1).
{ECO:0000269|PubMed:21220647}.
/FTId=VAR_065194.
VARIANT 98 98 V -> M (in ALS1; increases tendency to
form fibrillar aggregates).
{ECO:0000269|PubMed:14506936,
ECO:0000269|PubMed:18301754}.
/FTId=VAR_045882.
VARIANT 101 101 E -> G (in ALS1; dbSNP:rs121912439).
/FTId=VAR_007150.
VARIANT 101 101 E -> K (in ALS1).
/FTId=VAR_013534.
VARIANT 102 102 D -> G (in ALS1).
{ECO:0000269|PubMed:27604643,
ECO:0000269|PubMed:7655468}.
/FTId=VAR_007151.
VARIANT 102 102 D -> N (in ALS1).
{ECO:0000269|PubMed:27604643,
ECO:0000269|PubMed:7870076}.
/FTId=VAR_007152.
VARIANT 105 105 I -> F (in ALS1; dbSNP:rs121912445).
{ECO:0000269|PubMed:7501156}.
/FTId=VAR_008720.
VARIANT 106 106 S -> L (in ALS1).
/FTId=VAR_013535.
VARIANT 107 107 L -> V (in ALS1; dbSNP:rs121912440).
/FTId=VAR_007153.
VARIANT 109 109 G -> V (in ALS1).
/FTId=VAR_013536.
VARIANT 112 112 C -> Y (in ALS1).
{ECO:0000269|PubMed:27604643}.
/FTId=VAR_077327.
VARIANT 113 113 I -> M (in ALS1).
/FTId=VAR_013537.
VARIANT 113 113 I -> T (in ALS1; dbSNP:rs74315452).
{ECO:0000269|PubMed:7951252,
ECO:0000269|PubMed:8528216}.
/FTId=VAR_007154.
VARIANT 114 114 I -> T (in ALS1; destabilizes dimeric
protein structure and increases tendency
to form fibrillar aggregates;
dbSNP:rs121912441).
{ECO:0000269|PubMed:10400992,
ECO:0000269|PubMed:10732812,
ECO:0000269|PubMed:15056757,
ECO:0000269|PubMed:7997024,
ECO:0000269|PubMed:8528216}.
/FTId=VAR_007155.
VARIANT 115 115 G -> A (in ALS1).
/FTId=VAR_013538.
VARIANT 116 116 R -> G (in ALS1).
{ECO:0000269|PubMed:7881433}.
/FTId=VAR_007156.
VARIANT 119 119 V -> L (in ALS1).
{ECO:0000269|PubMed:14506936}.
/FTId=VAR_045883.
VARIANT 119 119 V -> VFLQ (in ALS1).
/FTId=VAR_008721.
VARIANT 125 125 D -> G (in ALS1).
{ECO:0000269|PubMed:14506936}.
/FTId=VAR_045884.
VARIANT 125 125 D -> V (in ALS1).
{ECO:0000269|PubMed:8938700}.
/FTId=VAR_008722.
VARIANT 126 126 D -> H (in ALS1).
{ECO:0000269|PubMed:8528216}.
/FTId=VAR_007157.
VARIANT 127 127 L -> S (in ALS1).
{ECO:0000269|PubMed:11535232}.
/FTId=VAR_013539.
VARIANT 134 134 Missing (in ALS).
{ECO:0000269|PubMed:8938700}.
/FTId=VAR_008723.
VARIANT 135 135 S -> N (in ALS1; reduced metal binding;
increases tendency to form fibrillar
aggregates; dbSNP:rs121912451).
{ECO:0000269|PubMed:12754496,
ECO:0000269|PubMed:8990014}.
/FTId=VAR_007158.
VARIANT 140 140 N -> K (in ALS1).
/FTId=VAR_007159.
VARIANT 145 145 L -> F (in ALS1).
{ECO:0000269|PubMed:18301754}.
/FTId=VAR_007160.
VARIANT 145 145 L -> S (in ALS1; dbSNP:rs121912446).
{ECO:0000269|PubMed:7496169}.
/FTId=VAR_008724.
VARIANT 146 146 A -> T (in ALS1; dbSNP:rs121912447).
{ECO:0000269|PubMed:7496169}.
/FTId=VAR_008725.
VARIANT 147 147 C -> R (in ALS1).
/FTId=VAR_013540.
VARIANT 148 148 G -> R (in ALS1).
{ECO:0000269|PubMed:14506936}.
/FTId=VAR_045885.
VARIANT 149 149 V -> G (in ALS1).
/FTId=VAR_007161.
VARIANT 149 149 V -> I (in ALS1; dbSNP:rs567511139).
{ECO:0000269|PubMed:7795609}.
/FTId=VAR_007162.
VARIANT 150 150 I -> T (in ALS1).
{ECO:0000269|PubMed:8528216}.
/FTId=VAR_007163.
VARIANT 152 152 I -> T (in ALS1; dbSNP:rs121912449).
{ECO:0000269|PubMed:8682505}.
/FTId=VAR_007164.
MUTAGEN 7 7 C->S: Enhances formation of fibrillar
aggregates in the absence of bound zinc;
when associated with S-58; S-112 and S-
147. {ECO:0000269|PubMed:17070542,
ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:22496122}.
MUTAGEN 7 7 C->S: No palmitoylation, reduced nuclear
targeting. {ECO:0000269|PubMed:17070542,
ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:22496122}.
MUTAGEN 51 52 FG->EE: Abolishes dimerization; when
associated with Q-134.
{ECO:0000269|PubMed:10329151,
ECO:0000269|PubMed:18552350}.
MUTAGEN 58 58 C->A: Exhibits very slow copper
acquisition.
{ECO:0000269|PubMed:17070542,
ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:23625804}.
MUTAGEN 58 58 C->S: Enhances formation of fibrillar
aggregates in the absence of bound zinc;
when associated with S-7; S-112 and S-
147. {ECO:0000269|PubMed:17070542,
ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:23625804}.
MUTAGEN 81 81 H->A: Loss of zinc binding and enhanced
tendency to form aggregates; when
associated with A-84.
{ECO:0000269|PubMed:17888947,
ECO:0000269|PubMed:18552350}.
MUTAGEN 81 81 H->S: Destabilization of dimer and loss
of zinc binding; when associated with S-
84. {ECO:0000269|PubMed:17888947,
ECO:0000269|PubMed:18552350}.
MUTAGEN 84 84 D->A: Loss of zinc binding and enhanced
tendency to form aggregates; when
associated with A-81.
{ECO:0000269|PubMed:17888947,
ECO:0000269|PubMed:18552350}.
MUTAGEN 84 84 D->S: Destabilization of dimer and loss
of zinc binding; when associated with S-
81. {ECO:0000269|PubMed:17888947,
ECO:0000269|PubMed:18552350}.
MUTAGEN 112 112 C->S: Enhances formation of fibrillar
aggregates in the absence of bound zinc;
when associated with S-7; S-58 and S-147.
{ECO:0000269|PubMed:17070542,
ECO:0000269|PubMed:18552350}.
MUTAGEN 123 123 K->A: Deacreased succinylation.
{ECO:0000269|PubMed:24140062}.
MUTAGEN 123 123 K->E: Mimicks constitutive succinylation
state; decreased activity.
{ECO:0000269|PubMed:24140062}.
MUTAGEN 134 134 E->Q: Abolishes dimerization; when
associated with E-50 and E-51.
{ECO:0000269|PubMed:10329151}.
MUTAGEN 147 147 C->A: Exhibits very slow copper
acquisition.
{ECO:0000269|PubMed:17070542,
ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:23625804}.
MUTAGEN 147 147 C->S: Enhances formation of fibrillar
aggregates in the absence of bound zinc;
when associated with S-7; S-58 and S-112.
{ECO:0000269|PubMed:17070542,
ECO:0000269|PubMed:18552350,
ECO:0000269|PubMed:23625804}.
CONFLICT 18 18 I -> S (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 99 99 S -> V (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
STRAND 3 10 {ECO:0000244|PDB:4A7U}.
STRAND 12 14 {ECO:0000244|PDB:4A7U}.
STRAND 16 25 {ECO:0000244|PDB:4A7U}.
STRAND 26 28 {ECO:0000244|PDB:1RK7}.
STRAND 30 38 {ECO:0000244|PDB:4A7U}.
STRAND 41 50 {ECO:0000244|PDB:4A7U}.
STRAND 51 53 {ECO:0000244|PDB:2NAM}.
HELIX 54 56 {ECO:0000244|PDB:1BA9}.
HELIX 58 61 {ECO:0000244|PDB:4A7U}.
STRAND 63 65 {ECO:0000244|PDB:1KMG}.
STRAND 67 69 {ECO:0000244|PDB:1KMG}.
STRAND 74 76 {ECO:0000244|PDB:1RK7}.
STRAND 77 79 {ECO:0000244|PDB:1MFM}.
TURN 80 82 {ECO:0000244|PDB:2MP3}.
STRAND 84 90 {ECO:0000244|PDB:4A7U}.
HELIX 92 94 {ECO:0000244|PDB:1SPD}.
STRAND 96 104 {ECO:0000244|PDB:4A7U}.
STRAND 106 108 {ECO:0000244|PDB:4A7U}.
HELIX 109 111 {ECO:0000244|PDB:4A7U}.
STRAND 112 115 {ECO:0000244|PDB:2AF2}.
STRAND 116 123 {ECO:0000244|PDB:4A7U}.
STRAND 127 129 {ECO:0000244|PDB:2LU5}.
STRAND 130 132 {ECO:0000244|PDB:4A7U}.
HELIX 133 136 {ECO:0000244|PDB:4A7U}.
TURN 138 140 {ECO:0000244|PDB:1AZV}.
STRAND 143 149 {ECO:0000244|PDB:4A7U}.
STRAND 151 153 {ECO:0000244|PDB:2C9S}.
SEQUENCE 154 AA; 15936 MW; 25CA38DA8D564483 CRC64;
MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS
AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV
HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ


Related products :

Catalog number Product name Quantity
U0596h CLIA Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
E0596h ELISA kit Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
E0596h ELISA Homo sapiens,hSod1,Human,SOD1,Superoxide dismutase [Cu-Zn],Superoxide dismutase 1 96T
ESOD-100 EnzyChrom™ Superoxide Dismutase Assay Kit, Quantitative determination of superoxide dismutase (SOD) enzyme activity by colorimetric (440nm) method 100Tests
ESOD-100 EnzyChrom™ Superoxide Dismutase Assay Kit, Quantitative determination of superoxide dismutase (SOD) enzyme activity by colorimetric (440nm) method. Procedure 1 hr. Kit size 100 tests. Detection limi 100tests
EIAAB39207 EC-SOD,Extracellular superoxide dismutase [Cu-Zn],Rat,Rattus norvegicus,Sod3,Sod-3,Superoxide dismutase B
orb81377 Human Superoxide Dismutase-1 protein Recombinant Human Cu_Zn Superoxide Dismutase produced in E.coli is a single monomeric non-glycosylated polypeptide chain containing 154 amino acids and having tota 5
LF-MA0065 anti-Superoxide Dismutase 2 (4F10) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0019 anti-Superoxide Dismutase 4 (11G1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG1, Host Mouse 100 ul
LF-MA0023 anti-Superoxide Dismutase 1 (72B1), Mouse monoclonal to Superoxide Dismutase 1, Isotype IgG1, Host Mouse 100 ul
LF-MA0121 anti-Superoxide Dismutase 3 (1H12), Mouse monoclonal to Superoxide Dismutase 3, Isotype IgG2b, Host Mouse 100 ul
LF-MA0066 anti-Superoxide Dismutase 2 (23G5) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
SCH-MCA2595 MOUSE ANTI SUPEROXIDE DISMUTASE (Cu_Zn), Product Type Monoclonal Antibody, Specificity SUPEROXIDE DISMUTASE , Target Species Bovine, Host Mouse, Format Purified, Isotypes IgG1, Applications C, 0.1 mg
MCA2595 MOUSE ANTI SUPEROXIDE DISMUTASE (Cu_Zn), Product Type Monoclonal Antibody, Specificity SUPEROXIDE DISMUTASE , Target Species Bovine, Host Mouse, Format Purified, Isotypes IgG1, Applications C, 0.1 mg
LF-MA0030 anti-Superoxide Dismutase 2 (2A1), Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG1, Host Mouse 100 ul
LF-MA0035 anti-Superoxide Dismutase 2 (1E8) , Mouse monoclonal to Superoxide Dismutase 2, Isotype IgG2b, Host Mouse 100 ul
LF-MA0016 anti-Superoxide Dismutase 4 (2A1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG1, Host Mouse 100 ul
LF-MA0042 anti-Superoxide Dismutase 4 (3A1), Mouse monoclonal to Superoxide Dismutase 4, Isotype IgG2a, Host Mouse 100 ul
LF-MA0029 anti-Superoxide Dismutase 1 (8A1), Mouse monoclonal to Superoxide Dismutase 1, Isotype IgG1, Host Mouse 100 ul
LF-PA10015 anti-Superoxide Dismutase 2, Mouse polyclonal to Superoxide Dismutase 2, Isotype , Host Mouse 50 ug
LF-PA0021 anti-Superoxide Dismutase 2, Rabbit polyclonal to Superoxide Dismutase 2, Isotype IgG, Host Rabbit 100 ul
LF-PA0013 anti-Superoxide Dismutase 1, Rabbit polyclonal to Superoxide Dismutase 1, Isotype IgG, Host Rabbit 100 ul
orb80178 Human Superoxide Dismutase (homodimer) protein Recombinant Human Cu_Zn Superoxide Dismutase produced in E.coli is homodimer, non-glycosylated polypeptide chain containing 2x 154 amino acids and having 100
8475-0204 NATIVE BOVINE SUPEROXIDE DISMUTASE, Product Type Purified Protein, Specificity SUPEROXIDE DISMUTASE, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 KU
SCH-8475-0204 NATIVE BOVINE SUPEROXIDE DISMUTASE, Product Type Purified Protein, Specificity SUPEROXIDE DISMUTASE, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 100 KU


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur