P00441 (SODC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Cu-Zn]
EC=1.15.1.1

Alternative name(s):
Superoxide dismutase 1
Short name=hSod1

Gene names

Name:

SOD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	154 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 copper ion per subunit. Ref.38 Binds 1 zinc ion per subunit. Ref.38
Subunit structure	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. Ref.21 Ref.24 Ref.30 Ref.31 Ref.32 Ref.35 Ref.36 Ref.38 Ref.39
Subcellular location	Cytoplasm. Note: The pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. Ref.81
Post-translational modification	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. 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.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20 Ref.28 Ref.32 Ref.33 Ref.34 Ref.40 Ref.41 Ref.44 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72 Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.79 Ref.80 Ref.81 Ref.82 Ref.83
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.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Disease	Amyotrophic lateral sclerosis Disease mutation Neurodegeneration
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Acetylation Disulfide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity Inferred from sequence or structural similarity. Source: UniProtKB anterograde axon cargo transport Inferred from sequence or structural similarity PubMed 20510358. Source: BHF-UCL apoptotic DNA fragmentation Inferred from sequence or structural similarity. Source: UniProtKB auditory receptor cell stereocilium organization Inferred from sequence or structural similarity. Source: UniProtKB cell aging Inferred from mutant phenotype PubMed 12871978. Source: UniProtKB cellular iron ion homeostasis Inferred from sequence or structural similarity. Source: UniProtKB double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB embryo implantation Inferred from sequence or structural similarity. Source: UniProtKB glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB heart contraction Inferred from direct assay PubMed 9539776. Source: UniProtKB hydrogen peroxide biosynthetic process Inferred from direct assay PubMed 15544046. Source: UniProtKB locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB muscle cell homeostasis Inferred from sequence or structural similarity. Source: UniProtKB myeloid cell homeostasis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cholesterol biosynthetic process Inferred from direct assay PubMed 15473258. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB neurofilament cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB ovarian follicle development Inferred from sequence or structural similarity. Source: UniProtKB peripheral nervous system myelin maintenance Inferred from sequence or structural similarity. Source: UniProtKB placenta development Non-traceable author statement PubMed 12485882. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of apoptotic process Inferred by curator PubMed 16790527. Source: UniProtKB positive regulation of cytokine production Inferred from direct assay PubMed 15544046. Source: UniProtKB regulation of T cell differentiation in thymus Non-traceable author statement PubMed 16716898. Source: UniProtKB regulation of blood pressure Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitochondrial membrane potential Inferred from mutant phenotype PubMed 16790527. Source: UniProtKB regulation of multicellular organism growth Inferred from sequence or structural similarity. Source: UniProtKB regulation of organ growth Non-traceable author statement PubMed 16716898. Source: UniProtKB relaxation of vascular smooth muscle Inferred from sequence or structural similarity. Source: UniProtKB removal of superoxide radicals Inferred from sequence or structural similarity. Source: UniProtKB response to amphetamine Inferred from electronic annotation. Source: Compara response to axon injury Inferred from sequence or structural similarity. Source: UniProtKB response to copper ion Inferred from electronic annotation. Source: Compara response to drug Inferred from sequence or structural similarity. Source: UniProtKB response to ethanol Inferred from sequence or structural similarity. Source: UniProtKB response to heat Inferred from sequence or structural similarity. Source: UniProtKB response to hydrogen peroxide Inferred from sequence or structural similarity. Source: UniProtKB response to nutrient levels Inferred from electronic annotation. Source: Compara retina homeostasis Inferred from sequence or structural similarity. Source: UniProtKB retrograde axon cargo transport Inferred from sequence or structural similarity PubMed 20510358. Source: BHF-UCL sensory perception of sound Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Inferred from sequence or structural similarity. Source: UniProtKB superoxide anion generation Inferred from electronic annotation. Source: Compara thymus development Non-traceable author statement PubMed 16716898. Source: UniProtKB
Cellular_component	cytoplasmic vesicle Inferred from direct assay PubMed 17077646. Source: UniProtKB cytosol Inferred from direct assay PubMed 16790527. Source: UniProtKB dendrite cytoplasm Inferred from direct assay PubMed 17324120. Source: UniProtKB extracellular matrix Inferred from direct assay PubMed 9699963. Source: UniProtKB extracellular space Inferred from direct assay PubMed 7172448PubMed 9453566. Source: UniProtKB mitochondrial matrix Non-traceable author statement PubMed 17008312. Source: UniProtKB neuronal cell body Inferred from direct assay PubMed 17324120. Source: UniProtKB nucleus Inferred from direct assay PubMed 1332049PubMed 17504823PubMed 9726962. Source: UniProtKB peroxisome Inferred from direct assay PubMed 1332049. Source: UniProtKB protein complex Inferred from direct assay PubMed 17324120. Source: UniProtKB
Molecular_function	copper ion binding Inferred from direct assay PubMed 17008312. Source: UniProtKB protein homodimerization activity Non-traceable author statement PubMed 10837872PubMed 9726962. Source: UniProtKB protein phosphatase 2B binding Inferred from direct assay PubMed 17324120. Source: UniProtKB superoxide dismutase activity Inferred from direct assay PubMed 15544046PubMed 17324120. Source: UniProtKB zinc ion binding Inferred from direct assay PubMed 17381088. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Chga	P26339	5	EBI-990792,EBI-990900	From a different organism.
Chgb	P16014	6	EBI-990792,EBI-990820	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.16 Ref.17

Chain

2 – 154

153

Superoxide dismutase [Cu-Zn]

PRO_0000164057

Sites

Metal binding

47

1

Copper; catalytic

Metal binding

49

1

Copper; catalytic

Metal binding

64

1

Copper; catalytic

Metal binding

64

1

Zinc; via pros nitrogen

Metal binding

72

1

Zinc; via pros nitrogen

Metal binding

81

1

Zinc; via pros nitrogen

Metal binding

84

1

Zinc; structural

Metal binding

121

1

Copper; catalytic

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.27

Modified residue

71

1

N6-acetyllysine By similarity

Modified residue

99

1

Phosphoserine Ref.22 Ref.25

Modified residue

123

1

N6-acetyllysine Ref.23

Disulfide bond

58 ↔ 147

Ref.21 Ref.27 Ref.32 Ref.36

Cross-link

33

1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain)

Natural variations

Natural variant

5

1

A → S in ALS1.

VAR_013518

Natural variant

5

1

A → T in ALS1. Ref.47

VAR_007130

Natural variant

5

1

A → V in ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggegates. Ref.32 Ref.34 Ref.71

VAR_007131

Natural variant

7

1

C → F in ALS1. Ref.65

VAR_008717

Natural variant

8

1

V → E in ALS1. Ref.48

VAR_007132

Natural variant

9

1

L → Q in ALS1. Ref.70

VAR_013519

Natural variant

9

1

L → V in ALS1. Ref.78

VAR_013520

Natural variant

13

1

G → R in ALS1. Ref.72

VAR_013521

Natural variant

15

1

V → G in ALS1.

VAR_013522

Natural variant

15

1

V → M in ALS1. Ref.59

VAR_007133

Natural variant

17

1

G → S in ALS1; sporadic young onset. Ref.67

VAR_007134

Natural variant

21

1

F → C in ALS1. Ref.78

VAR_045876

Natural variant

22

1

E → G in ALS1.

VAR_013523

Natural variant

22

1

E → K in ALS1. Ref.49

VAR_007135

Natural variant

23

1

Q → L in ALS1. Ref.78

VAR_045877

Natural variant

38

1

G → R in ALS1; mild form; ubiquitinated by RNF19A. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1. Ref.28 Ref.71 Ref.77 Ref.79

VAR_007136

Natural variant

39

1

L → R in ALS1.

VAR_013524

Natural variant

39

1

L → V in ALS1.

VAR_007137

Natural variant

42

1

G → D in ALS1.

VAR_007139

Natural variant

42

1

G → S in ALS1.

VAR_007138

Natural variant

44

1

H → R in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggegates. Ref.32

VAR_007140

Natural variant

46

1

F → C in ALS1; slow progression. Ref.75

VAR_013525

Natural variant

47

1

H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. Ref.33 Ref.52 Ref.71 Ref.77

VAR_007141

Natural variant

49

1

H → Q in ALS1. Ref.19 Ref.71

VAR_007142

Natural variant

49

1

H → R in ALS1. Ref.78

VAR_045878

Natural variant

50

1

E → K in ALS1.

VAR_013526

Natural variant

55

1

T → R in ALS1; reduces tendency to form fibrillar aggregates. Ref.78 Ref.80

VAR_045879

Natural variant

66

1

N → S in ALS1.

VAR_013527

Natural variant

68

1

L → P in ALS1. Ref.82

VAR_065560

Natural variant

68

1

L → R in ALS1.

VAR_013528

Natural variant

73

1

G → S in ALS1. Ref.68

VAR_008718

Natural variant

77

1

D → Y in ALS1.

VAR_013529

Natural variant

81

1

H → A in ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions. Ref.76

VAR_016874

Natural variant

85

1

L → F in ALS1.

VAR_013530

Natural variant

85

1

L → V in ALS1. Ref.59

VAR_007143

Natural variant

86

1

G → R in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1. Ref.40 Ref.41 Ref.71 Ref.77 Ref.79 Ref.81

VAR_007144

Natural variant

87

1

N → S in ALS1.
Corresponds to variant rs11556620 [ dbSNP | Ensembl ].

VAR_013531

Natural variant

88

1

V → A in ALS1. Ref.78

VAR_045880

Natural variant

90

1

A → T in ALS1. Ref.78

VAR_045881

Natural variant

90

1

A → V in ALS1.

VAR_013532

Natural variant

91

1

D → A in ALS1; does not seem to be linked with a decrease in activity. Ref.58 Ref.61 Ref.80

VAR_007145

Natural variant

91

1

D → V in ALS1.

VAR_013533

Natural variant

94

1

G → A in ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A. Ref.77 Ref.80 Ref.81

VAR_007146

Natural variant

94

1

G → C in ALS1.

VAR_007147

Natural variant

94

1

G → D in ALS1. Ref.50 Ref.80

VAR_007148

Natural variant

94

1

G → R in ALS1; 30% of wild-type activity. Ref.19 Ref.60 Ref.79

VAR_007149

Natural variant

94

1

G → V in ALS1. Ref.64

VAR_008719

Natural variant

96

1

A → G in ALS1. Ref.83

VAR_065194

Natural variant

98

1

V → M in ALS1; increases tendency to form fibrillar aggregates. Ref.78 Ref.80

VAR_045882

Natural variant

101

1

E → G in ALS1.

VAR_007150

Natural variant

101

1

E → K in ALS1.

VAR_013534

Natural variant

102

1

D → G in ALS1. Ref.57

VAR_007151

Natural variant

102

1

D → N in ALS1. Ref.54

VAR_007152

Natural variant

105

1

I → F in ALS1. Ref.62

VAR_008720

Natural variant

106

1

S → L in ALS1.

VAR_013535

Natural variant

107

1

L → V in ALS1.

VAR_007153

Natural variant

109

1

G → V in ALS1.

VAR_013536

Natural variant

113

1

I → M in ALS1.

VAR_013537

Natural variant

113

1

I → T in ALS1. Ref.19 Ref.50

VAR_007154

Natural variant

114

1

I → T in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates. Ref.19 Ref.34 Ref.53 Ref.69 Ref.71

VAR_007155

Natural variant

115

1

G → A in ALS1.

VAR_013538

Natural variant

116

1

R → G in ALS1. Ref.51

VAR_007156

Natural variant

119

1

V → L in ALS1. Ref.78

VAR_045883

Natural variant

119

1

V → VFLQ in ALS1.

VAR_008721

Natural variant

125

1

D → G in ALS1. Ref.78

VAR_045884

Natural variant

125

1

D → V in ALS1. Ref.64

VAR_008722

Natural variant

126

1

D → H in ALS1. Ref.19

VAR_007157

Natural variant

127

1

L → S in ALS1. Ref.74

VAR_013539

Natural variant

134

1

Missing in ALS. Ref.64

VAR_008723

Natural variant

135

1

S → N in ALS1; reduced metal binding; increases tendency to form fibrillar aggegates. Ref.33 Ref.66

VAR_007158

Natural variant

140

1

N → K in ALS1.

VAR_007159

Natural variant

145

1

L → F in ALS1. Ref.80

VAR_007160

Natural variant

145

1

L → S in ALS1. Ref.63

VAR_008724

Natural variant

146

1

A → T in ALS1. Ref.63

VAR_008725

Natural variant

147

1

C → R in ALS1.

VAR_013540

Natural variant

148

1

G → R in ALS1. Ref.78

VAR_045885

Natural variant

149

1

V → G in ALS1.

VAR_007161

Natural variant

149

1

V → I in ALS1. Ref.56

VAR_007162

Natural variant

150

1

I → T in ALS1. Ref.19

VAR_007163

Natural variant

152

1

I → T in ALS1; seems to affect formation of homodimer. Ref.20

VAR_007164

Experimental info

Mutagenesis

7

1

C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147. Ref.37 Ref.79

Mutagenesis

51 – 52

2

FG → EE: Abolishes dimerization; when associated with Q-134.

Mutagenesis

58

1

C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147. Ref.37 Ref.79

Mutagenesis

81

1

H → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84. Ref.38 Ref.79

Mutagenesis

81

1

H → S: Destabilization of dimer and loss of zinc binding; when associated with S-84. Ref.38 Ref.79

Mutagenesis

84

1

D → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81. Ref.38 Ref.79

Mutagenesis

84

1

D → S: Destabilization of dimer and loss of zinc binding; when associated with S-81. Ref.38 Ref.79

Mutagenesis

112

1

C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147. Ref.37 Ref.79

Mutagenesis

134

1

E → Q: Abolishes dimerization; when associated with E-50 and E-51. Ref.30

Mutagenesis

147

1

C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112. Ref.37 Ref.79

Sequence conflict

18

1

I → S no nucleotide entry Ref.3

Sequence conflict

99

1

S → V no nucleotide entry Ref.3

Secondary structure

1

.

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154

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Beta strand

12 – 14

3

Beta strand

16 – 25

10

Beta strand

26 – 28

3

Beta strand

30 – 38

9

Beta strand

41 – 50

10

Helix

54 – 56

3

Helix

58 – 61

4

Beta strand

63 – 65

3

Beta strand

67 – 69

3

Beta strand

74 – 76

3

Beta strand

77 – 79

3

Beta strand

84 – 90

7

Helix

92 – 94

3

Beta strand

96 – 104

9

Beta strand

106 – 108

3

Helix

109 – 111

3

Beta strand

112 – 115

4

Beta strand

116 – 123

8

Beta strand

127 – 129

3

Beta strand

130 – 132

3

Helix

133 – 136

4

Turn

138 – 140

3

Beta strand

143 – 149

7

Beta strand

151 – 153

3

Sequences

	Sequence		Length	Mass (Da)
	P00441 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 25CA38DA8D564483	FASTA	154	15,936
	10 20 30 40 50 60 MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE FGDNTAGCTS 70 80 90 100 110 120 AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI EDSVISLSGD HCIIGRTLVV 130 140 150 HEKADDLGKG GNEESTKTGN AGSRLACGVI GIAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA." Sherman L., Dafni N., Lieman-Hurwitz J., Groner Y. Proc. Natl. Acad. Sci. U.S.A. 80:5465-5469(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase." Levanon D., Lieman-Hurwitz J., Dafni N., Wigderson M., Sherman L., Bernstein Y., Laver-Rudich Z., Danciger E., Stein O., Groner Y. EMBO J. 4:77-84(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising high levels of active or inactive enzyme from an expression library." 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. Nucleic Acids Res. 13:2017-2034(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Comparison of properties between human recombinant and placental copper-zinc SOD." Kajihara J., Enomoto M., Nishijima K., Yabuuchi M., Katoh K. J. Biochem. 104:851-854(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	Xu Y., Hu X., Zhou Y., Peng X., Yuan J., Qiang B. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	Lu X., Hui L. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"Direct sequencing and cloning of superoxide dismutase 1 from peripheral blood." Staege M.S., Bergmann S., Heins S. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[8]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[9]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." 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. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[12]	NIEHS SNPs program Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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[15]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
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[17]	"The complete amino acid sequence of human Cu/Zn superoxide dismutase." Barra D., Martini F., Bannister J.V., Schinina M.E., Rotilio G., Bannister W.H., Bossa F. FEBS Lett. 120:53-56(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-154.
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[19]	"Two novel mutations in the gene for copper zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis." 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. Hum. Mol. Genet. 4:1239-1240(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-56 AND 120-154, VARIANTS ALS1 GLN-49; ARG-94; THR-113; THR-114; HIS-126 AND THR-150.
[20]	"Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis." Kostrzewa M., Daamian M., Mueller U. Hum. Genet. 98:48-50(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-154, VARIANT ALS1 THR-152.
[21]	"The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status." Arnesano F., Banci L., Bertini I., Martinelli M., Furukawa Y., O'Halloran T.V. J. Biol. Chem. 279:47998-48003(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, DISULFIDE BOND.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, MASS SPECTROMETRY.
[24]	"A ditryptophan cross-link is responsible for the covalent dimerization of human superoxide dismutase 1 during its bicarbonate-dependent peroxidase activity." Medinas D.B., Gozzo F.C., Santos L.F., Iglesias A.H., Augusto O. Free Radic. Biol. Med. 49:1046-1053(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, DITRYPTOPHAN CROSS-LINK AT TRP-33.
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[26]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase." Parge H.E., Hallewell R.A., Tainer J.A. Proc. Natl. Acad. Sci. U.S.A. 89:6109-6113(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[28]	"Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis." Hart P.J., Liu H., Pellegrini M., Nersissian A.M., Gralla E.B., Valentine J.S., Eisenberg D. Protein Sci. 7:545-555(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ALS1 ARG-38.
[29]	"Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?" Banci L., Benedetto M., Bertini I., del Conte R., Piccioli M., Viezzoli M.S. Biochemistry 37:11780-11791(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[30]	"The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited." Ferraroni M., Rypniewski W., Wilson K.S., Viezzoli M.S., Banci L., Bertini I., Mangani S. J. Mol. Biol. 288:413-426(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) OF MUTANT GLU-51/GLU-52/GLN-134, SUBUNIT, MUTAGENESIS OF 51-PHE-GLY-52 AND GLU-134.
[31]	"Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding." Banci L., Bertini I., Cramaro F., Del Conte R., Viezzoli M.S. Biochemistry 42:9543-9553(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF MUTANT GLU51/GLU-52/GLN-134, SUBUNIT.
[32]	"ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization." 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. J. Mol. Biol. 332:601-615(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS, DISULFIDE BOND, SUBUNIT, CHARACTERIZATION OF VARIANTS ALS1 VAL-5 AND ARG-44.
[33]	"Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS." 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. Nat. Struct. Biol. 10:461-467(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANTS ALS1 ASN-135 AND ARG-47, FORMATION OF FIBRILLAR AGGREGATES.
[34]	"Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants." 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. Proc. Natl. Acad. Sci. U.S.A. 101:5976-5981(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF VARIANTS ALS1 VAL-5 AND THR-114, CHARACTERIZATION OF VARIANTS ALS1 VAL-5 AND THR-114.
[35]	"Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form." Banci L., Bertini I., Cantini F., D'Amelio N., Gaggelli E. J. Biol. Chem. 281:2333-2337(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF MUTANT ALA-7/SER-112, SUBUNIT.
[36]	"Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes." Strange R.W., Antonyuk S.V., Hough M.A., Doucette P.A., Valentine J.S., Hasnain S.S. J. Mol. Biol. 356:1152-1162(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEXES WITH COPPER AND ZINC IONS, DISULFIDE BOND, SUBUNIT.
[37]	"The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase." Hoernberg A., Logan D.T., Marklund S.L., Oliveberg M. J. Mol. Biol. 365:333-342(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ALA-7/ALA-112 AND ALA-7/ALA-58/ALA-112/ALA-147, MUTAGENESIS OF CYS-7; CYS-58; CYS-112 AND CYS-147.
[38]	"Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS." 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. J. Mol. Biol. 373:877-890(2007) [PubMed] [Europe PMC] [Abstract] Cited for: 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, COFACTOR.
[39]	"Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase." Strange R.W., Yong C.W., Smith W., Hasnain S.S. Proc. Natl. Acad. Sci. U.S.A. 104:10040-10044(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS, SUBUNIT, FORMATION OF FIBRILLAR AGGREGATES BY ZINC-DEPLETED SOD1.
[40]	"Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis." 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. J. Biol. Chem. 283:16169-16177(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANT ALS1 ARG-86, CHARACTERIZATION OF VARIANT ALS1 ARG-86.
[41]	"Crystal structure of human Cu-Zn superoxide dismutase mutant G85R (P21)." RIKEN structural genomics initiative (RSGI) Submitted (APR-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ALS1 ARG-86.
[42]	"Familial amyotrophic lateral sclerosis/motor neurone disease (FALS): a review of current developments." de Belleroche J., Orrell R., King A. J. Med. Genet. 32:841-847(1995) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[43]	"Structures of mouse SOD1 and human/mouse SOD1 chimeras." Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J. Arch. Biochem. Biophys. 503:183-190(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
[44]	"Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis." 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. Nature 362:59-62(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ALS1.
[45]	Erratum Rosen D.R. Nature 364:362-362(1993) [PubMed] [Europe PMC] [Abstract]
[46]	"Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase." 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. Science 261:1047-1051(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ALS1.
[47]	"A novel mutation in Cu/Zn superoxide dismutase gene in Japanese familial amyotrophic lateral sclerosis." Nakano R., Sato S., Inuzuka T., Sakimura K., Mishina M., Takahashi H., Ikuta F., Honma Y., Fujii J., Taniguchi N., Tsuji S. Biochem. Biophys. Res. Commun. 200:695-703(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 THR-5.
[48]	"A new variant Cu/Zn superoxide dismutase (Val7-->Glu) deduced from lymphocyte mRNA sequences from Japanese patients with familial amyotrophic lateral sclerosis." Hirano M., Fujii J., Nagai Y., Sonobe M., Okamoto K., Araki H., Taniguchi N., Ueno S. Biochem. Biophys. Res. Commun. 204:572-577(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 GLU-8.
[49]	"Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of Ile113Thr in three others." Jones C.T., Swinger R.J., Brock D.J.H. Hum. Mol. Genet. 3:649-650(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 LYS-22.
[50]	"Identification of two novel mutations and a new polymorphism in the gene for Cu/Zn superoxide dismutase in patients with amyotrophic lateral sclerosis." 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. Hum. Mol. Genet. 3:997-998(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ALS1 ASP-94 AND THR-113.
[51]	"Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in the Cu/Zn superoxide dismutase-1 gene." Kostrzewa M., Burck-Lehmann U., Mueller U. Hum. Mol. Genet. 3:2261-2262(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 GLY-116.
[52]	"Familial amyotrophic lateral sclerosis (ALS) in Japan associated with H46R mutation in Cu/Zn superoxide dismutase gene: a possible new subtype of familial ALS." Aoki M., Ogasawara M., Matsubara Y., Narisawa K., Nakamura S., Itoyama Y., Abe K. J. Neurol. Sci. 126:77-83(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ARG-47.
[53]	"'Sporadic' motoneuron disease due to familial SOD1 mutation with low penetrance." Suthers G., Laing N., Wilton S., Dorosz S., Waddy H. Lancet 344:1773-1773(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 THR-114.
[54]	"Identification of a novel exon 4 SOD1 mutation in a sporadic amyotrophic lateral sclerosis patient." Jones C.T., Shaw P.J., Chari G., Brock D.J. Mol. Cell. Probes 8:329-330(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ASN-102.
[55]	"Identification of new mutations in the Cu/Zn superoxide dismutase gene of patients with familial amyotrophic lateral sclerosis." 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. Am. J. Hum. Genet. 56:592-596(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ALS1.
[56]	"A novel point mutation in the Cu/Zn superoxide dismutase gene in a patient with familial amyotrophic lateral sclerosis." Ikeda M., Abe K., Aoki M., Ogasawara M., Kameya T., Watanabe M., Shoji M., Hirai S., Itoyama Y. Hum. Mol. Genet. 4:491-492(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ILE-149.
[57]	"An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4." Yulug I.G., Katsanis N., de Belleroche J., Collinge J., Fisher E.M.C. Hum. Mol. Genet. 4:1101-1104(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 GLY-102.
[58]	"The D90A mutation results in a polymorphism of Cu,Zn superoxide dismutase that is prevalent in northern Sweden and Finland." Sjaelander A., Beckman G., Deng H.-X., Iqbal Z., Tainer J.A., Siddique T. Hum. Mol. Genet. 4:1105-1108(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ALA-91.
[59]	"Two novel SOD1 mutations in patients with familial amyotrophic lateral sclerosis." Deng H.-X., Tainer J.A., Mitsumoto H., Ohnishi A., He X., Hung W.-Y., Zhao Y., Juneja T., Hentati A., Siddique T. Hum. Mol. Genet. 4:1113-1116(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ALS1 MET-15 AND VAL-85.
[60]	"A novel SOD mutant and ALS." Orrell R., de Belleroche J., Marklund S., Bowe F., Hallewell R. Nature 374:504-505(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ARG-94.
[61]	"Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase." Andersen P.M., Nilsson P., Ala-Hurula V., Keraenen M.-L., Tarvainen I., Haltia T., Nilsson L., Binzer M., Forsgren L., Marklund S.L. Nat. Genet. 10:61-66(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ALA-91.
[62]	"Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene." Ikeda M., Abe K., Aoki M., Sahara M., Watanabe M., Shoji M., St George-Hyslop P.H., Hirai S., Itoyama Y. Neurology 45:2038-2042(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 PHE-105.
[63]	"Identification of three novel mutations in the gene for Cu/Zn superoxide dismutase in patients with familial amyotrophic lateral sclerosis." 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. Neuromuscul. Disord. 5:353-357(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ALS1 SER-145; THR-146 AND PHE-LEU-GLN-119 INS.
[64]	"Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral sclerosis." 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. Neuromuscul. Disord. 6:361-366(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ALS1 VAL-94; VAL-125 AND GLU-134 DEL.
[65]	"A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan." Morita M., Aoki M., Abe K., Hasegawa T., Sakuma R., Onodera Y., Ichikawa N., Nishizawa M., Itoyama Y. Neurosci. Lett. 205:79-82(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 PHE-7.
[66]	"A novel missense point mutation (S134N) of the Cu/Zn superoxide dismutase gene in a patient with familial motor neuron disease." Watanabe M., Aoki M., Abe K., Shoji M., Lizuka T., Ikeda Y., Hirai S., Kurokawa K., Kato T., Sasaki H., Itoyama Y. Hum. Mutat. 9:69-71(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ASN-135.
[67]	"Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with apparently sporadic young-onset amyotrophic lateral sclerosis." Kawamata J., Shimohama S., Takano S., Harada K., Ueda K., Kimura J. Hum. Mutat. 9:356-358(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 SER-17.
[68]	"Familial ALS is associated with mutations in all exons of SOD1: a novel mutation in exon 3 (Gly72Ser)." Orrell R.W., Marklund S.L., deBelleroche J.S. J. Neurol. Sci. 153:46-49(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 SER-73.
[69]	"A missense mutation in the SOD1 gene in patients with amyotrophic lateral sclerosis from the Kii Peninsula and its vicinity, Japan." Kikugawa K., Nakano R., Inuzuka T., Kokubo Y., Narita Y., Kuzuhara S., Yoshida S., Tsuji S. Neurogenetics 1:113-115(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 THR-114.
[70]	"A novel SOD1 mutation in an Austrian family with amyotrophic lateral sclerosis." Bereznai B., Winkler A., Borasio G.D., Gasser T. Neuromuscul. Disord. 7:113-116(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 GLN-9.
[71]	"Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds." Ratovitski T., Corson L.B., Strain J., Wong P., Cleveland D.W., Culotta V.C., Borchelt D.R. Hum. Mol. Genet. 8:1451-1460(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ALS1 VAL-5; ARG-38; ARG-47; GLN-49; ARG-86 AND THR-114.
[72]	"A SOD1 gene mutation in a patient with slowly progressing familial ALS." Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M., Bugiani O., Ajmar F., Garre C. Neurology 53:404-406(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ARG-13.
[73]	Erratum Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M., Bugiani O., Ajmar F., Garre C. Neurology 57:1146-1146(2001)
[74]	"A novel SOD1 gene mutation in familial ALS with low penetrance in females." Murakami T., Warita H., Hayashi T., Sato K., Manabe Y., Mizuno S., Yamane K., Abe K. J. Neurol. Sci. 189:45-47(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 SER-127.
[75]	"Superoxide dismutase gene mutations in Italian patients with familial and sporadic amyotrophic lateral sclerosis: identification of three novel missense mutations." Gellera C., Castellotti B., Riggio M.C., Silani V., Morandi L., Testa D., Casali C., Taroni F., Di Donato S., Zeviani M., Mariotti C. Neuromuscul. Disord. 11:404-410(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 CYS-46.
[76]	"'True' sporadic ALS associated with a novel SOD-1 mutation." Alexander M.D., Traynor B.J., Miller N., Corr B., Frost E., McQuaid S., Brett F.M., Green A., Hardiman O. Ann. Neurol. 52:680-683(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 ALA-81.
[77]	"Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity." Niwa J., Ishigaki S., Hishikawa N., Yamamoto M., Doyu M., Murata S., Tanaka K., Taniguchi N., Sobue G. J. Biol. Chem. 277:36793-36798(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-47; ARG-86 AND ALA-94, INTERACTION WITH RNF19A, UBIQUITINATION.
[78]	"Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes." 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. Amyotroph. Lateral Scler. 4:62-73(2003) [PubMed] [Europe PMC] [Abstract] Cited for: 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.
[79]	"Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis." Furukawa Y., Kaneko K., Yamanaka K., O'Halloran T.V., Nukina N. J. Biol. Chem. 283:24167-24176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: 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, MASS SPECTROMETRY.
[80]	"SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization." Banci L., Bertini I., Boca M., Girotto S., Martinelli M., Valentine J.S., Vieru M. PLoS ONE 3:E1677-E1677(2008) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ALS1 ARG-55; ALA-91; ALA-94; ASP-94; MET-98 AND PHE-145.
[81]	"Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation." Yonashiro R., Sugiura A., Miyachi M., Fukuda T., Matsushita N., Inatome R., Ogata Y., Suzuki T., Dohmae N., Yanagi S. Mol. Biol. Cell 20:4524-4530(2009) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ALS1 ARG-86 AND ALA-94, UBIQUITINATION BY MARCH5, SUBCELLULAR LOCATION.
[82]	"A novel L67P SOD1 mutation in an Italian ALS patient." del Grande A., Luigetti M., Conte A., Mancuso I., Lattante S., Marangi G., Stipa G., Zollino M., Sabatelli M. Amyotroph. Lateral Scler. 12:150-152(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 PRO-68.
[83]	"Large Proportion of Amyotrophic Lateral Sclerosis Cases in Sardinia Due to a Single Founder Mutation of the TARDBP Gene." 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. Arch. Neurol. 68:594-598(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALS1 GLY-96.
+	Additional computationally mapped references.

Web resources

Alsod

ALS genetic mutations db

GeneReviews

NIEHS-SNPs

Wikipedia

Superoxide dismutase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L44139 , L44135, L44136, L44137 Genomic DNA. Translation: AAB05662.1.
L44139 , L44135, L44136, L44137 Genomic DNA. Translation: AAB05661.1.
X02317 mRNA. Translation: CAA26182.1.
X01780 Genomic DNA. Translation: CAA25915.1.
X01781 Genomic DNA. Translation: CAA25916.1.
X01782 Genomic DNA. Translation: CAA25917.1. Sequence problems.
X01783 Genomic DNA. Translation: CAA25918.1.
X01784 Genomic DNA. Translation: CAA25919.1. Sequence problems.
AY049787 mRNA. Translation: AAL15444.1.
AY450286 mRNA. Translation: AAR21563.1.
EF151142 mRNA. Translation: ABL96616.1.
AK312116 mRNA. Translation: BAG35052.1.
CR450355 mRNA. Translation: CAG29351.1.
CR541742 mRNA. Translation: CAG46542.1.
BT006676 mRNA. Translation: AAP35322.1.
AY835629 Genomic DNA. Translation: AAV80422.1.
AP000253 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09889.1.
CH471079 Genomic DNA. Translation: EAX09890.1.
BC001034 mRNA. Translation: AAH01034.1.
L46374 Genomic DNA. Translation: AAB59626.1.
L46375 Genomic DNA. Translation: AAB59627.1.
L44746 Genomic DNA. Translation: AAC41773.1. Sequence problems.
X95228 Genomic DNA. Translation: CAA64520.1.

IPI

IPI00218733.

PIR

DSHUCZ. A22703.

RefSeq

NP_000445.1. NM_000454.4.

UniGene

Hs.443914.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZV	X-ray	1.90	A/B	2-154	[»]
1BA9	NMR	-	A	2-154	[»]
1DSW	NMR	-	A	2-154	[»]
1FUN	X-ray	2.85	A/B/C/D/E/F/G/H/I/J	2-153	[»]
1HL4	X-ray	1.82	A/B/C/D	2-154	[»]
1HL5	X-ray	1.80	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/S	2-154	[»]
1KMG	NMR	-	A	2-153	[»]
1L3N	NMR	-	A/B	2-153	[»]
1MFM	X-ray	1.02	A	2-154	[»]
1N18	X-ray	2.00	A/B/C/D/E/F/G/H/I/J	1-154	[»]
1N19	X-ray	1.86	A/B	1-154	[»]
1OEZ	X-ray	2.15	W/X/Y/Z	2-154	[»]
1OZT	X-ray	2.50	G/H/I/J/K/L/M/N	2-154	[»]
1OZU	X-ray	1.30	A/B	2-154	[»]
1P1V	X-ray	1.40	A/B/C	2-153	[»]
1PTZ	X-ray	1.80	A/B	2-154	[»]
1PU0	X-ray	1.70	A/B/C/D/E/F/G/H/I/J	2-154	[»]
1RK7	NMR	-	A	2-154	[»]
1SOS	X-ray	2.50	A/B/C/D/E/F/G/H/I/J	2-154	[»]
1SPD	X-ray	2.40	A/B	2-154	[»]
1UXL	X-ray	1.60	A/B/C/D/E/F/G/H/I/J	2-154	[»]
1UXM	X-ray	1.90	A/B/C/D/E/F/G/H/I/J/K/L	2-154	[»]
2AF2	NMR	-	A/B	2-154	[»]
2C9S	X-ray	1.24	A/F	2-154	[»]
2C9U	X-ray	1.24	A/F	2-154	[»]
2C9V	X-ray	1.07	A/F	2-154	[»]
2GBT	X-ray	1.70	A/B/C/D	2-154	[»]
2GBU	X-ray	2.00	A/B/C/D	2-154	[»]
2GBV	X-ray	2.00	A/B/C/D/E/F/G/H/I/J	2-154	[»]
2LU5	NMR	-	A	2-154	[»]
2NNX	X-ray	2.30	A/B/C/D	2-153	[»]
2R27	X-ray	2.00	A/B	1-154	[»]
2V0A	X-ray	1.15	A/F	2-154	[»]
2VR6	X-ray	1.30	A/F	2-154	[»]
2VR7	X-ray	1.58	A/F	2-154	[»]
2VR8	X-ray	1.36	A/F	2-154	[»]
2WKO	X-ray	1.97	A/F	2-154	[»]
2WYT	X-ray	1.00	A/F	2-154	[»]
2WYZ	X-ray	1.70	A/F	2-154	[»]
2WZ0	X-ray	1.72	A/F	2-154	[»]
2WZ5	X-ray	1.50	A/F	2-154	[»]
2WZ6	X-ray	1.55	A/F	2-154	[»]
2XJK	X-ray	1.45	A	2-154	[»]
2XJL	X-ray	1.55	A	2-154	[»]
2ZKW	X-ray	1.90	A/B	1-154	[»]
2ZKX	X-ray	2.72	A/B/C/D	1-154	[»]
2ZKY	X-ray	2.40	A/B/C/D/E/F/G/H/I/J	1-154	[»]
3CQP	X-ray	1.95	A/B/C/D	2-154	[»]
3CQQ	X-ray	1.90	A/B	2-154	[»]
3ECU	X-ray	1.90	A/B/C/D	2-154	[»]
3ECV	X-ray	1.90	A/B/C/D	2-154	[»]
3ECW	X-ray	2.15	A/B/C/D	2-154	[»]
3GQF	X-ray	2.20	A/B/C/D/E/F	2-154	[»]
3GTV	X-ray	2.20	A/B/C/D/E/F/G/H/I/J/K/L	2-81	[»]
3GZO	X-ray	2.10	A/B/C/D/E/F/G/H/I/J	2-154	[»]
3GZP	X-ray	3.10	A/B/C/D	2-154	[»]
3GZQ	X-ray	1.40	A/B	2-154	[»]
3H2P	X-ray	1.55	A/B	2-154	[»]
3H2Q	X-ray	1.85	A/B/C/D	2-154	[»]
3HFF	X-ray	2.20	A	2-154	[»]
3K91	X-ray	1.75	A/B	2-154	[»]
3KH3	X-ray	3.50	A/B/C/D/E/F/G/H/I/J/K/L	2-154	[»]
3KH4	X-ray	3.50	A/B/C/D/E/F	2-154	[»]
3LTV	X-ray	2.45	A/B/C/D/E/F	4-154	[»]
3QQD	X-ray	1.65	A/B	2-154	[»]
3RE0	X-ray	2.28	A/B/C/D	2-154	[»]
3T5W	X-ray	1.80	A/B/D/E/F/G/H/I/J/K/L/M	2-154	[»]
4A7G	X-ray	1.24	A/F	2-154	[»]
4A7Q	X-ray	1.22	A/F	2-154	[»]
4A7S	X-ray	1.06	A/F	2-154	[»]
4A7T	X-ray	1.45	A/F	2-154	[»]
4A7U	X-ray	0.98	A/F	2-154	[»]
4A7V	X-ray	1.00	A/F	2-154	[»]
4B3E	X-ray	2.15	A/B/C/D/E/F/G/H/I/J	1-154	[»]
4BCY	X-ray	1.27	A	2-154	[»]
4BCZ	X-ray	1.93	A/B	2-154	[»]
4BD4	X-ray	2.78	A/B/C/D/E/F/G/H/I	2-154	[»]
4SOD	model	-	A	1-154	[»]

ProteinModelPortal

P00441.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44941N.

IntAct

P00441. 5 interactions.

MINT

MINT-204523.

STRING

9606.ENSP00000270142.

PTM databases

PhosphoSite

P00441.

Polymorphism databases

DMDM

134611.

2D gel databases

DOSAC-COBS-2DPAGE

P00441.

OGP

P00441.

REPRODUCTION-2DPAGE

IPI00783680.

SWISS-2DPAGE

P00441.

UCD-2DPAGE

P00441.

Proteomic databases

PaxDb

P00441.

PeptideAtlas

P00441.

PRIDE

P00441.

Protocols and materials databases

DNASU

6647.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000270142; ENSP00000270142; ENSG00000142168.

GeneID

6647.

KEGG

hsa:6647.

UCSC

uc002ypa.3. human.

Organism-specific databases

CTD

6647.

GeneCards

GC21P033031.

HGNC

HGNC:11179. SOD1.

HPA

CAB008670.
HPA001401.

MIM

105400. phenotype.
147450. gene.

neXtProt

NX_P00441.

Orphanet

803. Amyotrophic lateral sclerosis.

PharmGKB

PA334.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2032.

HOVERGEN

HBG000062.

InParanoid

P00441.

KO

K04565.

OMA

APRFESS.

OrthoDB

EOG45HRZM.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3apathway. FOXA1 transcription factor network.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P00441.

Bgee

P00441.

CleanEx

HS_SOD1.

Genevestigator

P00441.

GermOnline

ENSG00000142168. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.200. 1 hit.

InterPro

IPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]

PANTHER

PTHR10003. PTHR10003. 1 hit.

Pfam

PF00080. Sod_Cu. 1 hit.
[Graphical view]

PRINTS

PR00068. CUZNDISMTASE.

SUPFAM

SSF49329. SOD_Cu_Zn. 1 hit.

PROSITE

PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00441.

ChEMBL

CHEMBL2354.

ChiTaRS

SOD1. human.

EvolutionaryTrace

P00441.

GenomeRNAi

6647.

NextBio

25903.

SOURCE

Search...

Entry information

Entry name

SODC_HUMAN

Accession

Primary (citable) accession number: P00441
Secondary accession number(s): A6NHJ0 , D3DSE4, Q16669, Q16711, Q16838, Q16839, Q16840, Q6NR85

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 178 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.