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P00441 (SODC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 191. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]

EC=1.15.1.1
Alternative name(s):
Superoxide dismutase 1
Short name=hSod1
Gene names
Name:SOD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.41

Binds 1 zinc ion per subunit. Ref.41

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.33 Ref.34 Ref.35 Ref.38 Ref.39 Ref.41 Ref.42

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. Ref.27 Ref.84

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.

Palmitoylation helps nuclear targeting and decreases catalytic activity. Ref.27

Succinylation, adjacent to copper catalytic site probably inhibit activity. Desuccinylated by SIRT5, enhancing activity. Ref.28

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.31 Ref.35 Ref.36 Ref.37 Ref.43 Ref.44 Ref.47 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.73 Ref.74 Ref.75 Ref.77 Ref.78 Ref.79 Ref.80 Ref.81 Ref.82 Ref.83 Ref.84 Ref.85 Ref.86

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 componentCytoplasm
Nucleus
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMAcetylation
Disulfide bond
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation 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

auditory receptor cell stereocilium organization

Inferred from sequence or structural similarity. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cell aging

Inferred from mutant phenotype PubMed 12871978. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular iron ion homeostasis

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 cellular 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 catalytic activity

Inferred from direct assay PubMed 17324120. Source: UniProtKB

positive regulation of cytokine production

Inferred from direct assay PubMed 15544046. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype PubMed 12551919. Source: BHF-UCL

positive regulation of superoxide anion generation

Inferred from direct assay PubMed 18219391. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from direct assay Ref.28. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from direct assay PubMed 18219391. 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

regulation of protein kinase activity

Inferred from direct assay PubMed 16254550. 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: Ensembl

response to axon injury

Inferred from sequence or structural similarity. Source: UniProtKB

response to copper ion

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

response to organic substance

Inferred from direct assay PubMed 12921788. Source: UniProtKB

response to superoxide

Inferred from direct assay PubMed 16790527. Source: UniProtKB

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: Ensembl

superoxide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

thymus development

Non-traceable author statement PubMed 16716898. Source: UniProtKB

transmission of nerve impulse

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11527942PubMed 17077646PubMed 17504823Ref.84PubMed 9726962. Source: UniProtKB

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 region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 7172448PubMed 9453566. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

mitochondrial intermembrane space

Traceable author statement. Source: Reactome

mitochondrial matrix

Non-traceable author statement PubMed 17008312. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 16790527. 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_functionRac GTPase binding

Inferred from direct assay PubMed 18219391. Source: UniProtKB

chaperone binding

Inferred from physical interaction PubMed 9726962. Source: UniProtKB

copper ion binding

Inferred from direct assay PubMed 17008312. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 23831581. Source: IntAct

protein binding

Inferred from physical interaction PubMed 16790527. 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 17324120Ref.28. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 17381088. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-990792,EBI-990792
ChgaP263395EBI-990792,EBI-990900From a different organism.
ChgbP160146EBI-990792,EBI-990820From a different organism.
DYNC2LI1Q8TCX13EBI-990792,EBI-8568003

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16 Ref.17
Chain2 – 154153Superoxide dismutase [Cu-Zn]
PRO_0000164057

Sites

Metal binding471Copper; catalytic
Metal binding491Copper; catalytic
Metal binding641Copper; catalytic
Metal binding641Zinc; via pros nitrogen
Metal binding721Zinc; via pros nitrogen
Metal binding811Zinc; via pros nitrogen
Metal binding841Zinc; structural
Metal binding1211Copper; catalytic

Amino acid modifications

Modified residue21N-acetylalanine Ref.17 Ref.30
Modified residue41N6-succinyllysine By similarity
Modified residue101N6-succinyllysine By similarity
Modified residue921N6-succinyllysine By similarity
Modified residue991Phosphoserine Ref.22 Ref.25
Modified residue1231N6-acetyllysine; alternate Ref.23
Modified residue1231N6-succinyllysine; alternate Ref.28
Modified residue1371N6-acetyllysine; alternate By similarity
Modified residue1371N6-succinyllysine; alternate By similarity
Lipidation71S-palmitoyl cysteine Ref.27
Disulfide bond58 ↔ 147 Ref.21 Ref.30 Ref.35 Ref.39
Cross-link331-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)

Natural variations

Natural variant51A → S in ALS1.
VAR_013518
Natural variant51A → T in ALS1. Ref.50
VAR_007130
Natural variant51A → V in ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. Ref.35 Ref.37 Ref.74
VAR_007131
Natural variant71C → F in ALS1. Ref.68
VAR_008717
Natural variant81V → E in ALS1. Ref.51
VAR_007132
Natural variant91L → Q in ALS1. Ref.73
VAR_013519
Natural variant91L → V in ALS1. Ref.81
VAR_013520
Natural variant131G → R in ALS1. Ref.75
VAR_013521
Natural variant151V → G in ALS1.
VAR_013522
Natural variant151V → M in ALS1. Ref.62
VAR_007133
Natural variant171G → S in ALS1; sporadic young onset. Ref.70
VAR_007134
Natural variant211F → C in ALS1. Ref.81
VAR_045876
Natural variant221E → G in ALS1.
VAR_013523
Natural variant221E → K in ALS1. Ref.52
VAR_007135
Natural variant231Q → L in ALS1. Ref.81
VAR_045877
Natural variant381G → R in ALS1; mild form; ubiquitinated by RNF19A. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1. Ref.31 Ref.74 Ref.80 Ref.82
VAR_007136
Natural variant391L → R in ALS1.
VAR_013524
Natural variant391L → V in ALS1.
VAR_007137
Natural variant421G → D in ALS1.
VAR_007139
Natural variant421G → S in ALS1.
VAR_007138
Natural variant441H → R in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates. Ref.35
VAR_007140
Natural variant461F → C in ALS1; slow progression. Ref.78
VAR_013525
Natural variant471H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. Ref.36 Ref.55 Ref.74 Ref.80
VAR_007141
Natural variant491H → Q in ALS1. Ref.19 Ref.74
VAR_007142
Natural variant491H → R in ALS1. Ref.81
VAR_045878
Natural variant501E → K in ALS1.
VAR_013526
Natural variant551T → R in ALS1; reduces tendency to form fibrillar aggregates. Ref.81 Ref.83
VAR_045879
Natural variant661N → S in ALS1.
VAR_013527
Natural variant681L → P in ALS1. Ref.85
VAR_065560
Natural variant681L → R in ALS1.
VAR_013528
Natural variant731G → S in ALS1. Ref.71
VAR_008718
Natural variant771D → Y in ALS1.
VAR_013529
Natural variant811H → A in ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions. Ref.79
VAR_016874
Natural variant851L → F in ALS1.
VAR_013530
Natural variant851L → V in ALS1. Ref.62
VAR_007143
Natural variant861G → R in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1. Ref.43 Ref.44 Ref.74 Ref.80 Ref.82 Ref.84
VAR_007144
Natural variant871N → S in ALS1.
Corresponds to variant rs11556620 [ dbSNP | Ensembl ].
VAR_013531
Natural variant881V → A in ALS1. Ref.81
VAR_045880
Natural variant901A → T in ALS1. Ref.81
VAR_045881
Natural variant901A → V in ALS1.
VAR_013532
Natural variant911D → A in ALS1; does not seem to be linked with a decrease in activity. Ref.61 Ref.64 Ref.83
Corresponds to variant rs80265967 [ dbSNP | Ensembl ].
VAR_007145
Natural variant911D → V in ALS1.
VAR_013533
Natural variant941G → A in ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A. Ref.80 Ref.83 Ref.84
VAR_007146
Natural variant941G → C in ALS1.
VAR_007147
Natural variant941G → D in ALS1. Ref.53 Ref.83
VAR_007148
Natural variant941G → R in ALS1; 30% of wild-type activity. Ref.19 Ref.63 Ref.82
VAR_007149
Natural variant941G → V in ALS1. Ref.67
VAR_008719
Natural variant961A → G in ALS1. Ref.86
VAR_065194
Natural variant981V → M in ALS1; increases tendency to form fibrillar aggregates. Ref.81 Ref.83
VAR_045882
Natural variant1011E → G in ALS1.
VAR_007150
Natural variant1011E → K in ALS1.
VAR_013534
Natural variant1021D → G in ALS1. Ref.60
VAR_007151
Natural variant1021D → N in ALS1. Ref.57
VAR_007152
Natural variant1051I → F in ALS1. Ref.65
VAR_008720
Natural variant1061S → L in ALS1.
VAR_013535
Natural variant1071L → V in ALS1.
VAR_007153
Natural variant1091G → V in ALS1.
VAR_013536
Natural variant1131I → M in ALS1.
VAR_013537
Natural variant1131I → T in ALS1. Ref.19 Ref.53
VAR_007154
Natural variant1141I → T in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates. Ref.19 Ref.37 Ref.56 Ref.72 Ref.74
VAR_007155
Natural variant1151G → A in ALS1.
VAR_013538
Natural variant1161R → G in ALS1. Ref.54
VAR_007156
Natural variant1191V → L in ALS1. Ref.81
VAR_045883
Natural variant1191V → VFLQ in ALS1.
VAR_008721
Natural variant1251D → G in ALS1. Ref.81
VAR_045884
Natural variant1251D → V in ALS1. Ref.67
VAR_008722
Natural variant1261D → H in ALS1. Ref.19
VAR_007157
Natural variant1271L → S in ALS1. Ref.77
VAR_013539
Natural variant1341Missing in ALS. Ref.67
VAR_008723
Natural variant1351S → N in ALS1; reduced metal binding; increases tendency to form fibrillar aggregates. Ref.36 Ref.69
VAR_007158
Natural variant1401N → K in ALS1.
VAR_007159
Natural variant1451L → F in ALS1. Ref.83
VAR_007160
Natural variant1451L → S in ALS1. Ref.66
VAR_008724
Natural variant1461A → T in ALS1. Ref.66
VAR_008725
Natural variant1471C → R in ALS1.
VAR_013540
Natural variant1481G → R in ALS1. Ref.81
VAR_045885
Natural variant1491V → G in ALS1.
VAR_007161
Natural variant1491V → I in ALS1. Ref.59
VAR_007162
Natural variant1501I → T in ALS1. Ref.19
VAR_007163
Natural variant1521I → T in ALS1; seems to affect formation of homodimer. Ref.20
VAR_007164

Experimental info

Mutagenesis71C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147. Ref.27 Ref.40 Ref.82
Mutagenesis71C → S: No palmitoylation, reduced nuclear targeting. Ref.27 Ref.40 Ref.82
Mutagenesis51 – 522FG → EE: Abolishes dimerization; when associated with Q-134.
Mutagenesis581C → A: Exhibits very slow copper acquisition. Ref.29 Ref.40 Ref.82
Mutagenesis581C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147. Ref.29 Ref.40 Ref.82
Mutagenesis811H → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84. Ref.41 Ref.82
Mutagenesis811H → S: Destabilization of dimer and loss of zinc binding; when associated with S-84. Ref.41 Ref.82
Mutagenesis841D → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81. Ref.41 Ref.82
Mutagenesis841D → S: Destabilization of dimer and loss of zinc binding; when associated with S-81. Ref.41 Ref.82
Mutagenesis1121C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147. Ref.40 Ref.82
Mutagenesis1231K → A: Deacreased succinylation. Ref.28
Mutagenesis1231K → E: Mimicks constitutive succinylation state; decreased activity. Ref.28
Mutagenesis1341E → Q: Abolishes dimerization; when associated with E-50 and E-51. Ref.33
Mutagenesis1471C → A: Exhibits very slow copper acquisition. Ref.29 Ref.40 Ref.82
Mutagenesis1471C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112. Ref.29 Ref.40 Ref.82
Sequence conflict181I → S no nucleotide entry Ref.3
Sequence conflict991S → V no nucleotide entry Ref.3

Secondary structure

............................................ 154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00441 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 25CA38DA8D564483

FASTA15415,936
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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].
[13]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. expand/collapse author list , 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].
[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.
[16]"Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase."
Jabusch J.R., Farb D.L., Kerschensteiner D.A., Deutsch H.F.
Biochemistry 19:2310-2316(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-154.
[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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
[18]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-24 AND 81-116.
Tissue: Fetal brain cortex.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases."
Marin E.P., Derakhshan B., Lam T.T., Davalos A., Sessa W.C.
Circ. Res. 110:1336-1344(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-7, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-7.
[28]"SIRT5 desuccinylates and activates SOD1 to eliminate ROS."
Lin Z.F., Xu H.B., Wang J.Y., Lin Q., Ruan Z., Liu F.B., Jin W., Huang H.H., Chen X.
Biochem. Biophys. Res. Commun. 441:191-195(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-123, DESUCCINYLATION BY SIRT5, MUTAGENESIS OF LYS-123.
[29]"Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants."
Banci L., Cantini F., Kozyreva T., Rubino J.T.
ChemBioChem 14:1839-1844(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-58 AND CYS-147.
[30]"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).
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
[47]"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. expand/collapse author list , 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.
[48]Erratum
Rosen D.R.
Nature 364:362-362(1993) [PubMed] [Europe PMC] [Abstract]
[49]"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.
[50]"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.
[51]"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.
[52]"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.
[53]"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.
[54]"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.
[55]"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.
[56]"'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.
[57]"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.
[58]"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.
[59]"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.
[60]"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.
[61]"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.
[62]"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.
[63]"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.
[64]"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.
[65]"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.
[66]"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.
[67]"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.
[68]"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.
[69]"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.
[70]"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.
[71]"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.
[72]"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.
[73]"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.
[74]"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.
[75]"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.
[76]Erratum
Penco S., Schenone A., Bordo D., Bolognesi M., Abbruzzese M., Bugiani O., Ajmar F., Garre C.
Neurology 57:1146-1146(2001)
[77]"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.
[78]"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.
[79]"'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.
[80]"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.
[81]"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.
[82]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[83]"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.
[84]"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.
[85]"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.
[86]"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. expand/collapse author list , 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

NIEHS-SNPs
Wikipedia

Superoxide dismutase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L44139 expand/collapse EMBL AC list , L44135, L44136, L44137 Genomic DNA. Translation: AAB05662.1.
L44139 expand/collapse EMBL AC list , 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.
CCDSCCDS33536.1.
PIRDSHUCZ. A22703.
RefSeqNP_000445.1. NM_000454.4.
UniGeneHs.443914.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZVX-ray1.90A/B2-154[»]
1BA9NMR-A2-154[»]
1DSWNMR-A2-154[»]
1FUNX-ray2.85A/B/C/D/E/F/G/H/I/J2-154[»]
1HL4X-ray1.82A/B/C/D2-154[»]
1HL5X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/S2-154[»]
1KMGNMR-A2-154[»]
1L3NNMR-A/B2-154[»]
1MFMX-ray1.02A2-154[»]
1N18X-ray2.00A/B/C/D/E/F/G/H/I/J1-154[»]
1N19X-ray1.86A/B1-154[»]
1OEZX-ray2.15W/X/Y/Z2-154[»]
1OZTX-ray2.50G/H/I/J/K/L/M/N2-154[»]
1OZUX-ray1.30A/B2-154[»]
1P1VX-ray1.40A/B/C2-154[»]
1PTZX-ray1.80A/B2-154[»]
1PU0X-ray1.70A/B/C/D/E/F/G/H/I/J2-154[»]
1RK7NMR-A2-154[»]
1SOSX-ray2.50A/B/C/D/E/F/G/H/I/J2-154[»]
1SPDX-ray2.40A/B2-154[»]
1UXLX-ray1.60A/B/C/D/E/F/G/H/I/J2-154[»]
1UXMX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L2-154[»]
2AF2NMR-A/B2-154[»]
2C9SX-ray1.24A/F2-154[»]
2C9UX-ray1.24A/F2-154[»]
2C9VX-ray1.07A/F2-154[»]
2GBTX-ray1.70A/B/C/D2-154[»]
2GBUX-ray2.00A/B/C/D2-154[»]
2GBVX-ray2.00A/B/C/D/E/F/G/H/I/J2-154[»]
2LU5NMR-A2-154[»]
2NNXX-ray2.30A/B/C/D2-154[»]
2R27X-ray2.00A/B1-154[»]
2V0AX-ray1.15A/F2-154[»]
2VR6X-ray1.30A/F2-154[»]
2VR7X-ray1.58A/F2-154[»]
2VR8X-ray1.36A/F2-154[»]
2WKOX-ray1.97A/F2-154[»]
2WYTX-ray1.00A/F2-154[»]
2WYZX-ray1.70A/F2-154[»]
2WZ0X-ray1.72A/F2-154[»]
2WZ5X-ray1.50A/F2-154[»]
2WZ6X-ray1.55A/F2-154[»]
2XJKX-ray1.45A2-154[»]
2XJLX-ray1.55A2-154[»]
2ZKWX-ray1.90A/B1-154[»]
2ZKXX-ray2.72A/B/C/D1-154[»]
2ZKYX-ray2.40A/B/C/D/E/F/G/H/I/J1-154[»]
3CQPX-ray1.95A/B/C/D2-154[»]
3CQQX-ray1.90A/B2-154[»]
3ECUX-ray1.90A/B/C/D2-154[»]
3ECVX-ray1.90A/B/C/D2-154[»]
3ECWX-ray2.15A/B/C/D2-154[»]
3GQFX-ray2.20A/B/C/D/E/F2-154[»]
3GTVX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L2-81[»]
3GZOX-ray2.10A/B/C/D/E/F/G/H/I/J2-154[»]
3GZPX-ray3.10A/B/C/D2-154[»]
3GZQX-ray1.40A/B2-154[»]
3H2PX-ray1.55A/B2-154[»]
3H2QX-ray1.85A/B/C/D2-154[»]
3HFFX-ray2.20A2-154[»]
3K91X-ray1.75A/B2-154[»]
3KH3X-ray3.50A/B/C/D/E/F/G/H/I/J/K/L2-154[»]
3KH4X-ray3.50A/B/C/D/E/F2-154[»]
3LTVX-ray2.45A/B/C/D/E/F4-154[»]
3QQDX-ray1.65A/B2-154[»]
3RE0X-ray2.28A/B/C/D2-154[»]
3T5WX-ray1.80A/B/D/E/F/G/H/I/J/K/L/M2-154[»]
4A7GX-ray1.24A/F2-154[»]
4A7QX-ray1.22A/F2-154[»]
4A7SX-ray1.06A/F2-154[»]
4A7TX-ray1.45A/F2-154[»]
4A7UX-ray0.98A/F2-154[»]
4A7VX-ray1.00A/F2-154[»]
4B3EX-ray2.15A/B/C/D/E/F/G/H/I/J1-154[»]
4BCYX-ray1.27A2-154[»]
4BCZX-ray1.93A/B2-49[»]
A/B83-124[»]
A/B141-154[»]
4BD4X-ray2.78A/B/C/D/E/F/G/H/I2-49[»]
A/B/C/D/E/F/G/H/I83-124[»]
A/B/C/D/E/F/G/H/I141-154[»]
4FF9X-ray2.50A/B2-154[»]
4NINX-ray1.40A102-108[»]
4NIOX-ray1.30A148-154[»]
4NIPX-ray1.90A148-154[»]
4SODmodel-A1-154[»]
DisProtDP00652.
ProteinModelPortalP00441.
SMRP00441. Positions 2-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112530. 44 interactions.
DIPDIP-44941N.
IntActP00441. 12 interactions.
MINTMINT-204523.
STRING9606.ENSP00000270142.

Chemistry

BindingDBP00441.
ChEMBLCHEMBL2354.

PTM databases

PhosphoSiteP00441.

2D gel databases

DOSAC-COBS-2DPAGEP00441.
OGPP00441.
REPRODUCTION-2DPAGEIPI00783680.
SWISS-2DPAGEP00441.
UCD-2DPAGEP00441.

Proteomic databases

MaxQBP00441.
PaxDbP00441.
PeptideAtlasP00441.
PRIDEP00441.

Protocols and materials databases

DNASU6647.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270142; ENSP00000270142; ENSG00000142168.
GeneID6647.
KEGGhsa:6647.
UCSCuc002ypa.3. human.

Organism-specific databases

CTD6647.
GeneCardsGC21P033031.
GeneReviewsSOD1.
HGNCHGNC:11179. SOD1.
HPACAB008670.
HPA001401.
MIM105400. phenotype.
147450. gene.
neXtProtNX_P00441.
Orphanet803. Amyotrophic lateral sclerosis.
PharmGKBPA334.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2032.
HOVERGENHBG000062.
InParanoidP00441.
KOK04565.
OMANDPNAKR.
OrthoDBEOG776SR4.
PhylomeDBP00441.
TreeFamTF105131.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP00441.
BgeeP00441.
CleanExHS_SOD1.
GenevestigatorP00441.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SSF49329. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSOD1. human.
EvolutionaryTraceP00441.
GeneWikiSOD1.
GenomeRNAi6647.
NextBio25903.
PROP00441.
SOURCESearch...

Entry information

Entry nameSODC_HUMAN
AccessionPrimary (citable) accession number: P00441
Secondary accession number(s): A6NHJ0 expand/collapse secondary AC list , 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: July 9, 2014
This is version 191 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM