Reviewed, UniProtKB/Swiss-Prot P00441 (SODC_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

SOD1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.36 Binds 1 zinc ion per subunit. Ref.36
Subunit structure	Homodimer. The pathogenics variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 interact with RNF19A, whereas wild-type protein does not. Ref.36 Ref.21 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.37
Subcellular location	Cytoplasm.
Post-translational modification	Unlike wild-type protein, the pathogenics variants ALS1 Arg-38, Arg-47, Arg-86 and Ala-94 are polyubiquitinated by RNF19A; which leads to their proteasomal degradation.
Involvement in disease	Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:105400]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. 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 cases leading to familial forms. Ref.30 Ref.19 Ref.20 Ref.26 Ref.31 Ref.32 Ref.38 Ref.39 Ref.41 Ref.43 Ref.44 Ref.45 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.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77
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
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptosis Inferred from sequence or structural similarity. Source: UniProtKB activation of MAPK activity 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. 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 Non-traceable author statement. Source: UniProtKB glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB heart contraction Inferred from direct assay. Source: UniProtKB hydrogen peroxide biosynthetic process Inferred from direct assay. Source: UniProtKB locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB muscle homeostasis Inferred from sequence or structural similarity. Source: UniProtKB myelin maintenance in the peripheral nervous system 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. Source: UniProtKB negative regulation of neuron apoptosis 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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW placenta development Non-traceable author statement. Source: UniProtKB positive regulation of apoptosis Inferred by curator. Source: UniProtKB positive regulation of cytokine production Inferred from direct assay. Source: UniProtKB regulation of T cell differentiation in the thymus Non-traceable author statement. Source: UniProtKB regulation of blood pressure Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitochondrial membrane potential Inferred from mutant phenotype. Source: UniProtKB regulation of multicellular organism growth Inferred from sequence or structural similarity. Source: UniProtKB regulation of organ growth Non-traceable author statement. 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 axon injury Inferred from sequence or structural similarity. Source: UniProtKB 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 superoxide Inferred from direct assay. Source: UniProtKB retina homeostasis Inferred from sequence or structural similarity. Source: UniProtKB sensory perception of sound Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Inferred from sequence or structural similarity. Source: UniProtKB thymus development Non-traceable author statement. Source: UniProtKB
Cellular component	cell soma Inferred from direct assay. Source: UniProtKB cytoplasmic vesicle Inferred from direct assay. Source: UniProtKB cytosol Inferred from direct assay. Source: UniProtKB dendrite cytoplasm Inferred from direct assay. Source: UniProtKB extracellular matrix Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB mitochondrial matrix Non-traceable author statement. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB peroxisome Non-traceable author statement. Source: UniProtKB protein complex Inferred from direct assay. Source: UniProtKB
Molecular function	antioxidant activity Inferred from electronic annotation. Source: UniProtKB-KW chaperone binding Inferred from physical interaction. Source: UniProtKB copper ion binding Inferred from direct assay. Source: UniProtKB protein homodimerization activity Non-traceable author statement. Source: UniProtKB protein phosphatase 2B binding Inferred from direct assay. Source: UniProtKB superoxide dismutase activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Chga	P26339	2	EBI-990792,EBI-990900	From a different organism.
Chgb	P16014	2	EBI-990792,EBI-990820	From a different organism.
Tgoln1	Q62313	1	EBI-990792,EBI-991369	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; structural

Metal binding

72

1

Zinc; structural

Metal binding

81

1

Zinc; structural

Metal binding

84

1

Zinc; structural

Metal binding

121

1

Copper; catalytic

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.25

Modified residue

71

1

N6-acetyllysine By similarity

Modified residue

99

1

Phosphoserine Ref.22

Modified residue

123

1

N6-acetyllysine Ref.24

Disulfide bond

58 ↔ 147

Ref.21 Ref.30 Ref.34 Ref.25

Natural variations

Natural variant

5

1

A → S in ALS1.

VAR_013518

Natural variant

5

1

A → T in ALS1. Ref.44

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.30 Ref.32 Ref.68

VAR_007131

Natural variant

7

1

C → F in ALS1. Ref.62

VAR_008717

Natural variant

8

1

V → E in ALS1. Ref.45

VAR_007132

Natural variant

9

1

L → Q in ALS1. Ref.67

VAR_013519

Natural variant

9

1

L → V in ALS1. Ref.75

VAR_013520

Natural variant

13

1

G → R in ALS1. Ref.69

VAR_013521

Natural variant

15

1

V → G in ALS1.

VAR_013522

Natural variant

15

1

V → M in ALS1. Ref.56

VAR_007133

Natural variant

17

1

G → S in ALS1; sporadic young onset. Ref.64

VAR_007134

Natural variant

21

1

F → C in ALS1. Ref.75

VAR_045876

Natural variant

22

1

E → G in ALS1.

VAR_013523

Natural variant

22

1

E → K in ALS1. Ref.46

VAR_007135

Natural variant

23

1

Q → L in ALS1. Ref.75

VAR_045877

Natural variant

38

1

G → R in ALS1; mild form; ubiquitinated by RNF19A. Ref.26 Ref.68 Ref.74 Ref.76

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.30

VAR_007140

Natural variant

46

1

F → C in ALS1; slow progression. Ref.72

VAR_013525

Natural variant

47

1

H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. Ref.31 Ref.49 Ref.68 Ref.74

VAR_007141

Natural variant

49

1

H → Q in ALS1. Ref.19 Ref.68

VAR_007142

Natural variant

49

1

H → R in ALS1. Ref.75

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.75 Ref.77

VAR_045879

Natural variant

66

1

N → S in ALS1.

VAR_013527

Natural variant

68

1

L → R in ALS1.

VAR_013528

Natural variant

73

1

G → S in ALS1. Ref.65

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.73

VAR_016874

Natural variant

85

1

L → F in ALS1.

VAR_013530

Natural variant

85

1

L → V in ALS1. Ref.56

VAR_007143

Natural variant

86

1

G → R in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding. Ref.38 Ref.39 Ref.68 Ref.74 Ref.76

VAR_007144

Natural variant

87

1

N → S in ALS1.

VAR_013531

Natural variant

88

1

V → A in ALS1. Ref.75

VAR_045880

Natural variant

90

1

A → T in ALS1. Ref.75

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.55 Ref.58 Ref.77

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.74 Ref.77

VAR_007146

Natural variant

94

1

G → C in ALS1.

VAR_007147

Natural variant

94

1

G → D in ALS1. Ref.47 Ref.77

VAR_007148

Natural variant

94

1

G → R in ALS1; 30% of wild-type activity. Ref.19 Ref.57 Ref.76

VAR_007149

Natural variant

94

1

G → V in ALS1. Ref.61

VAR_008719

Natural variant

98

1

V → M in ALS1; increases tendency to form fibrillar aggregates. Ref.75 Ref.77

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.54

VAR_007151

Natural variant

102

1

D → N in ALS1. Ref.51

VAR_007152

Natural variant

105

1

I → F in ALS1. Ref.59

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.47

VAR_007154

Natural variant

114

1

I → T in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates. Ref.19 Ref.32 Ref.50 Ref.66 Ref.68

VAR_007155

Natural variant

115

1

G → A in ALS1.

VAR_013538

Natural variant

116

1

R → G in ALS1. Ref.48

VAR_007156

Natural variant

119

1

V → L in ALS1. Ref.75

VAR_045883

Natural variant

119

1

V → VFLQ in ALS1.

VAR_008721

Natural variant

125

1

D → G in ALS1. Ref.75

VAR_045884

Natural variant

125

1

D → V in ALS1. Ref.61

VAR_008722

Natural variant

126

1

D → H in ALS1. Ref.19

VAR_007157

Natural variant

127

1

L → S in ALS1. Ref.71

VAR_013539

Natural variant

134

1

Missing in ALS.

VAR_008723

Natural variant

135

1

S → N in ALS1; reduced metal binding; increases tendency to form fibrillar aggegates. Ref.31 Ref.63

VAR_007158

Natural variant

140

1

N → K in ALS1.

VAR_007159

Natural variant

145

1

L → F in ALS1. Ref.77

VAR_007160

Natural variant

145

1

L → S in ALS1. Ref.60

VAR_008724

Natural variant

146

1

A → T in ALS1. Ref.60

VAR_008725

Natural variant

147

1

C → R in ALS1.

VAR_013540

Natural variant

148

1

G → R in ALS1. Ref.75

VAR_045885

Natural variant

149

1

V → G in ALS1.

VAR_007161

Natural variant

149

1

V → I in ALS1. Ref.53

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.76 Ref.35

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.76 Ref.35

Mutagenesis

81

1

H → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84. Ref.36 Ref.76

Mutagenesis

81

1

H → S: Destabilization of dimer and loss of zinc binding; when associated with S-84. Ref.36 Ref.76

Mutagenesis

84

1

D → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81. Ref.36 Ref.76

Mutagenesis

84

1

D → S: Destabilization of dimer and loss of zinc binding; when associated with S-81. Ref.36 Ref.76

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.76 Ref.35

Mutagenesis

134

1

E → Q: Abolishes dimerization; when associated with E-50 and E-51. Ref.28

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.76 Ref.35

Sequence conflict

18

1

I → S Ref.3

Sequence conflict

99

1

S → V Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

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.

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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

30 – 38

9

Beta strand

41 – 50

10

Helix

57 – 59

3

Beta strand

77 – 79

3

Beta strand

84 – 90

7

Beta strand

96 – 104

9

Beta strand

107 – 109

3

Beta strand

116 – 123

8

Beta strand

130 – 132

3

Helix

135 – 138

4

Beta strand

143 – 149

7

Sequences

	Sequence		Length	Mass (Da)
	P00441-1 [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: 6577438] [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: 3160582] [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: 3889846] [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: 2853161] [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: 14702039] [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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[14]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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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: 8528216] [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.
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[27]	"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: 9718300] [Abstract] Cited for: STRUCTURE BY NMR.
[28]	"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: 10329151] [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.
[29]	"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: 12911296] [Abstract] Cited for: STRUCTURE BY NMR OF MUTANT GLU51/GLU-52/GLN-134, SUBUNIT.
[30]	"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: 12963370] [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.
[31]	"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: 12754496] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANTS ALS1 ASN-135 AND ARG-47, FORMATION OF FIBRILLAR AGGREGATES.
[32]	"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: 15056757] [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.
[33]	"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: 16291742] [Abstract] Cited for: STRUCTURE BY NMR OF MUTANT ALA-7/SER-112, SUBUNIT.
[34]	"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: 16406071] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEXES WITH COPPER AND ZINC IONS, DISULFIDE BOND, SUBUNIT.
[35]	"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: 17070542] [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.
[36]	"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: 17888947] [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.
[37]	"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: 17548825] [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.
[38]	"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: 18378676] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF VARIANT ALS1 ARG-86, CHARACTERIZATION OF VARIANT ALS1 ARG-86.
[39]	"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.
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[41]	"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: 8446170] [Abstract] Cited for: VARIANTS ALS1.
[42]	Erratum Rosen D.R. Nature 364:362-362(1993) [PubMed: 8332197] [Abstract]
[43]	"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: 8351519] [Abstract] Cited for: VARIANTS ALS1.
[44]	"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: 8179602] [Abstract] Cited for: VARIANT ALS1 THR-5.
[45]	"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: 7980516] [Abstract] Cited for: VARIANT ALS1 GLU-8.
[46]	"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: 8069312] [Abstract] Cited for: VARIANT ALS1 LYS-22.
[47]	"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: 7951252] [Abstract] Cited for: VARIANTS ALS1 ASP-94 AND THR-113.
[48]	"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: 7881433] [Abstract] Cited for: VARIANT ALS1 GLY-116.
[49]	"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: 7836951] [Abstract] Cited for: VARIANT ALS1 ARG-47.
[50]	"'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: 7997024] [Abstract] Cited for: VARIANT ALS1 THR-114.
[51]	"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: 7870076] [Abstract] Cited for: VARIANT ALS1 ASN-102.
[52]	"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: 7887412] [Abstract] Cited for: VARIANTS ALS1.
[53]	"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: 7795609] [Abstract] Cited for: VARIANT ALS1 ILE-149.
[54]	"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: 7655468] [Abstract] Cited for: VARIANT ALS1 GLY-102.
[55]	"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: 7655469] [Abstract] Cited for: VARIANT ALS1 ALA-91.
[56]	"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: 7655471] [Abstract] Cited for: VARIANTS ALS1 MET-15 AND VAL-85.
[57]	"A novel SOD mutant and ALS." Orrell R., de Belleroche J., Marklund S., Bowe F., Hallewell R. Nature 374:504-505(1995) [PubMed: 7700376] [Abstract] Cited for: VARIANT ALS1 ARG-94.
[58]	"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: 7647793] [Abstract] Cited for: VARIANT ALS1 ALA-91.
[59]	"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: 7501156] [Abstract] Cited for: VARIANT ALS1 PHE-105.
[60]	"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: 7496169] [Abstract] Cited for: VARIANTS ALS1 SER-145; THR-146 AND PHE-LEU-GLN-119 INS.
[61]	"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: 8938700] [Abstract] Cited for: VARIANTS ALS1 VAL-94; VAL-125 AND GLU-134 DEL.
[62]	"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: 8907321] [Abstract] Cited for: VARIANT ALS1 PHE-7.
[63]	"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: 8990014] [Abstract] Cited for: VARIANT ALS1 ASN-135.
[64]	"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: 9101297] [Abstract] Cited for: VARIANT ALS1 SER-17.
[65]	"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: 9455977] [Abstract] Cited for: VARIANT ALS1 SER-73.
[66]	"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: 10732812] [Abstract] Cited for: VARIANT ALS1 THR-114.
[67]	"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: 9131652] [Abstract] Cited for: VARIANT ALS1 GLN-9.
[68]	"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: 10400992] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ALS1 VAL-5; ARG-38; ARG-47; GLN-49; ARG-86 AND THR-114.
[69]	"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: 10430435] [Abstract] Cited for: VARIANT ALS1 ARG-13.
[70]	Erratum Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M., Bugiani O., Ajmar F., Garre C. Neurology 57:1146-1146(2001)
[71]	"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: 11535232] [Abstract] Cited for: VARIANT ALS1 SER-127.
[72]	"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: 11369193] [Abstract] Cited for: VARIANT ALS1 CYS-46.
[73]	"'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: 12402272] [Abstract] Cited for: VARIANT ALS1 ALA-81.
[74]	"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: 12145308] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ALS1 ARG-38; ARG-47; ARG-86 AND ALA-94, INTERACTION WITH RNF19A, UBIQUITINATION.
[75]	"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: 14506936] [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.
[76]	"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: 18552350] [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.
[77]	"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: 18301754] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ALS1 ARG-55; ALA-91; ALA-94; ASP-94; MET-98 AND PHE-145.
+	Additional computationally mapped references.

Web resources

Alsod

ALS genetic mutations db

GeneReviews

NIEHS-SNPs

Wikipedia

Superoxide dismutase entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
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.

UniGene

Hs.443914

3D structure databases

PDBPDBe

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	[»]
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	[»]
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	[»]
3HFF	X-ray	2.20	A	2-154	[»]
4SOD	model	-	A	1-154	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P00441. 3 interactions.

STRING

P00441.

PTM databases

PhosphoSite

P00441.

2-D gel databases

SWISS-2DPAGE

P00441.

Aarhus/Ghent-2DPAGE

4127. IEF.

DOSAC-COBS-2DPAGE

P00441.

OGP

P00441.

REPRODUCTION-2DPAGE

IPI00783680.

Siena-2DPAGE

P00441.

Proteomic databases

PeptideAtlas

P00441.

PRIDE

P00441.

Genome annotation databases

Ensembl

ENST00000270142; ENSP00000270142; ENSG00000142168; Homo sapiens. [Genome view]
ENST00000389995; ENSP00000374645; ENSG00000142168; Homo sapiens. [Genome view]

GeneID

6647.

KEGG

hsa:6647.

UCSC

uc002ypa.1. human.

Organism-specific databases

CTD

6647.

GeneCards

GC21P031953.

H-InvDB

HIX0016056.

HGNC

HGNC:11179. SOD1.

HPA

CAB008670.
HPA001401.

MIM

105400. phenotype.
147450. gene.

Orphanet

803. Amyotrophic lateral sclerosis.

PharmGKB

PA334.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P00441.

OMA

KAVCVIN.

Enzyme and pathway databases

BRENDA

1.15.1.1. 247.

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

InterPro

IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[Graphical view]

Gene3D

G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.

PANTHER

PTHR10003. SOD_Cu_Zn. 1 hit.

Pfam

PF00080. Sod_Cu. 1 hit.
[Graphical view]

PRINTS

PR00068. CUZNDISMTASE.

ProDom

PD000469. SOD_CU_ZN. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

25903.

SOURCE

Search...

Entry information

Entry name

SODC_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.