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P00441

- SODC_HUMAN

UniProt

P00441 - SODC_HUMAN

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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Binds 1 copper ion per subunit.1 Publication
Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Copper; catalytic2 Publications
Metal bindingi49 – 491Copper; catalytic2 Publications
Metal bindingi64 – 641Copper; catalytic2 Publications
Metal bindingi64 – 641Zinc; via pros nitrogen1 Publication
Metal bindingi72 – 721Zinc; via pros nitrogen1 Publication
Metal bindingi81 – 811Zinc; via pros nitrogen1 Publication
Metal bindingi84 – 841Zinc; structural1 Publication
Metal bindingi121 – 1211Copper; catalytic2 Publications

GO - Molecular functioni

  1. chaperone binding Source: UniProtKB
  2. copper ion binding Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. protein homodimerization activity Source: UniProtKB
  5. protein phosphatase 2B binding Source: UniProtKB
  6. Rac GTPase binding Source: UniProtKB
  7. superoxide dismutase activity Source: UniProtKB
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: UniProtKB
  2. anterograde axon cargo transport Source: BHF-UCL
  3. auditory receptor cell stereocilium organization Source: UniProtKB
  4. blood coagulation Source: Reactome
  5. cell aging Source: UniProtKB
  6. cell death Source: UniProtKB-KW
  7. cellular iron ion homeostasis Source: UniProtKB
  8. embryo implantation Source: UniProtKB
  9. glutathione metabolic process Source: UniProtKB
  10. heart contraction Source: UniProtKB
  11. hydrogen peroxide biosynthetic process Source: UniProtKB
  12. locomotory behavior Source: UniProtKB
  13. muscle cell cellular homeostasis Source: UniProtKB
  14. myeloid cell homeostasis Source: UniProtKB
  15. negative regulation of cholesterol biosynthetic process Source: UniProtKB
  16. negative regulation of neuron apoptotic process Source: UniProtKB
  17. neurofilament cytoskeleton organization Source: UniProtKB
  18. ovarian follicle development Source: UniProtKB
  19. peripheral nervous system myelin maintenance Source: UniProtKB
  20. placenta development Source: UniProtKB
  21. platelet activation Source: Reactome
  22. platelet degranulation Source: Reactome
  23. positive regulation of apoptotic process Source: UniProtKB
  24. positive regulation of catalytic activity Source: UniProtKB
  25. positive regulation of cytokine production Source: UniProtKB
  26. positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  27. positive regulation of superoxide anion generation Source: UniProtKB
  28. reactive oxygen species metabolic process Source: UniProtKB
  29. regulation of blood pressure Source: UniProtKB
  30. regulation of mitochondrial membrane potential Source: UniProtKB
  31. regulation of multicellular organism growth Source: UniProtKB
  32. regulation of organ growth Source: UniProtKB
  33. regulation of protein kinase activity Source: UniProtKB
  34. regulation of Rac GTPase activity Source: UniProtKB
  35. regulation of T cell differentiation in thymus Source: UniProtKB
  36. relaxation of vascular smooth muscle Source: UniProtKB
  37. removal of superoxide radicals Source: UniProtKB
  38. response to amphetamine Source: Ensembl
  39. response to axon injury Source: UniProtKB
  40. response to copper ion Source: Ensembl
  41. response to drug Source: UniProtKB
  42. response to ethanol Source: UniProtKB
  43. response to heat Source: UniProtKB
  44. response to hydrogen peroxide Source: UniProtKB
  45. response to nutrient levels Source: Ensembl
  46. response to organic substance Source: UniProtKB
  47. response to superoxide Source: UniProtKB
  48. retina homeostasis Source: UniProtKB
  49. retrograde axon cargo transport Source: BHF-UCL
  50. sensory perception of sound Source: UniProtKB
  51. spermatogenesis Source: UniProtKB
  52. superoxide anion generation Source: Ensembl
  53. superoxide metabolic process Source: UniProtKB
  54. thymus development Source: UniProtKB
  55. transmission of nerve impulse Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Alternative name(s):
Superoxide dismutase 1
Short name:
hSod1
Gene namesi
Name:SOD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:11179. SOD1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. dendrite cytoplasm Source: UniProtKB
  5. extracellular matrix Source: UniProtKB
  6. extracellular region Source: Reactome
  7. extracellular space Source: UniProtKB
  8. extracellular vesicular exosome Source: UniProtKB
  9. mitochondrial intermembrane space Source: Reactome
  10. mitochondrial matrix Source: UniProtKB
  11. mitochondrion Source: UniProtKB
  12. neuronal cell body Source: UniProtKB
  13. nucleus Source: UniProtKB
  14. peroxisome Source: UniProtKB
  15. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.35 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51A → S in ALS1.
VAR_013518
Natural varianti5 – 51A → T in ALS1. 1 Publication
VAR_007130
Natural varianti5 – 51A → V in ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates.
VAR_007131
Natural varianti7 – 71C → F in ALS1. 1 Publication
VAR_008717
Natural varianti8 – 81V → E in ALS1. 1 Publication
VAR_007132
Natural varianti9 – 91L → Q in ALS1. 1 Publication
VAR_013519
Natural varianti9 – 91L → V in ALS1. 1 Publication
VAR_013520
Natural varianti13 – 131G → R in ALS1. 1 Publication
VAR_013521
Natural varianti15 – 151V → G in ALS1.
VAR_013522
Natural varianti15 – 151V → M in ALS1. 1 Publication
VAR_007133
Natural varianti17 – 171G → S in ALS1; sporadic young onset. 1 Publication
VAR_007134
Natural varianti21 – 211F → C in ALS1. 1 Publication
VAR_045876
Natural varianti22 – 221E → G in ALS1.
VAR_013523
Natural varianti22 – 221E → K in ALS1. 1 Publication
VAR_007135
Natural varianti23 – 231Q → L in ALS1. 1 Publication
VAR_045877
Natural varianti38 – 381G → R in ALS1; mild form; ubiquitinated by RNF19A. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1.
VAR_007136
Natural varianti39 – 391L → R in ALS1.
VAR_013524
Natural varianti39 – 391L → V in ALS1.
VAR_007137
Natural varianti42 – 421G → D in ALS1.
VAR_007139
Natural varianti42 – 421G → S in ALS1.
VAR_007138
Natural varianti44 – 441H → R in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates.
VAR_007140
Natural varianti46 – 461F → C in ALS1; slow progression. 1 Publication
VAR_013525
Natural varianti47 – 471H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. 1 Publication
VAR_007141
Natural varianti49 – 491H → Q in ALS1. 1 Publication
VAR_007142
Natural varianti49 – 491H → R in ALS1. 1 Publication
VAR_045878
Natural varianti50 – 501E → K in ALS1.
VAR_013526
Natural varianti55 – 551T → R in ALS1; reduces tendency to form fibrillar aggregates. 1 Publication
VAR_045879
Natural varianti66 – 661N → S in ALS1.
VAR_013527
Natural varianti68 – 681L → P in ALS1. 1 Publication
VAR_065560
Natural varianti68 – 681L → R in ALS1.
VAR_013528
Natural varianti73 – 731G → S in ALS1. 1 Publication
VAR_008718
Natural varianti77 – 771D → Y in ALS1.
VAR_013529
Natural varianti81 – 811H → A in ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions. 1 Publication
VAR_016874
Natural varianti85 – 851L → F in ALS1.
VAR_013530
Natural varianti85 – 851L → V in ALS1. 1 Publication
VAR_007143
Natural varianti86 – 861G → R in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1.
VAR_007144
Natural varianti87 – 871N → S in ALS1.
Corresponds to variant rs11556620 [ dbSNP | Ensembl ].
VAR_013531
Natural varianti88 – 881V → A in ALS1. 1 Publication
VAR_045880
Natural varianti90 – 901A → T in ALS1. 1 Publication
VAR_045881
Natural varianti90 – 901A → V in ALS1.
VAR_013532
Natural varianti91 – 911D → A in ALS1; does not seem to be linked with a decrease in activity. 2 Publications
Corresponds to variant rs80265967 [ dbSNP | Ensembl ].
VAR_007145
Natural varianti91 – 911D → V in ALS1.
VAR_013533
Natural varianti94 – 941G → A in ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A.
VAR_007146
Natural varianti94 – 941G → C in ALS1.
VAR_007147
Natural varianti94 – 941G → D in ALS1. 1 Publication
VAR_007148
Natural varianti94 – 941G → R in ALS1; 30% of wild-type activity. 2 Publications
VAR_007149
Natural varianti94 – 941G → V in ALS1. 1 Publication
VAR_008719
Natural varianti96 – 961A → G in ALS1. 1 Publication
VAR_065194
Natural varianti98 – 981V → M in ALS1; increases tendency to form fibrillar aggregates. 1 Publication
VAR_045882
Natural varianti101 – 1011E → G in ALS1.
VAR_007150
Natural varianti101 – 1011E → K in ALS1.
VAR_013534
Natural varianti102 – 1021D → G in ALS1. 1 Publication
VAR_007151
Natural varianti102 – 1021D → N in ALS1. 1 Publication
VAR_007152
Natural varianti105 – 1051I → F in ALS1. 1 Publication
VAR_008720
Natural varianti106 – 1061S → L in ALS1.
VAR_013535
Natural varianti107 – 1071L → V in ALS1.
VAR_007153
Natural varianti109 – 1091G → V in ALS1.
VAR_013536
Natural varianti113 – 1131I → M in ALS1.
VAR_013537
Natural varianti113 – 1131I → T in ALS1. 2 Publications
VAR_007154
Natural varianti114 – 1141I → T in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates. 3 Publications
VAR_007155
Natural varianti115 – 1151G → A in ALS1.
VAR_013538
Natural varianti116 – 1161R → G in ALS1. 1 Publication
VAR_007156
Natural varianti119 – 1191V → L in ALS1. 1 Publication
VAR_045883
Natural varianti119 – 1191V → VFLQ in ALS1.
VAR_008721
Natural varianti125 – 1251D → G in ALS1. 1 Publication
VAR_045884
Natural varianti125 – 1251D → V in ALS1. 1 Publication
VAR_008722
Natural varianti126 – 1261D → H in ALS1. 1 Publication
VAR_007157
Natural varianti127 – 1271L → S in ALS1. 1 Publication
VAR_013539
Natural varianti135 – 1351S → N in ALS1; reduced metal binding; increases tendency to form fibrillar aggregates. 1 Publication
VAR_007158
Natural varianti140 – 1401N → K in ALS1.
VAR_007159
Natural varianti145 – 1451L → F in ALS1.
VAR_007160
Natural varianti145 – 1451L → S in ALS1. 1 Publication
VAR_008724
Natural varianti146 – 1461A → T in ALS1. 1 Publication
VAR_008725
Natural varianti147 – 1471C → R in ALS1.
VAR_013540
Natural varianti148 – 1481G → R in ALS1. 1 Publication
VAR_045885
Natural varianti149 – 1491V → G in ALS1.
VAR_007161
Natural varianti149 – 1491V → I in ALS1. 1 Publication
VAR_007162
Natural varianti150 – 1501I → T in ALS1. 1 Publication
VAR_007163
Natural varianti152 – 1521I → T in ALS1; seems to affect formation of homodimer. 1 Publication
VAR_007164

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147. 3 Publications
Mutagenesisi7 – 71C → S: No palmitoylation, reduced nuclear targeting. 3 Publications
Mutagenesisi51 – 522FG → EE: Abolishes dimerization; when associated with Q-134. 2 Publications
Mutagenesisi58 – 581C → A: Exhibits very slow copper acquisition. 3 Publications
Mutagenesisi58 – 581C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147. 3 Publications
Mutagenesisi81 – 811H → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84. 2 Publications
Mutagenesisi81 – 811H → S: Destabilization of dimer and loss of zinc binding; when associated with S-84. 2 Publications
Mutagenesisi84 – 841D → A: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81. 2 Publications
Mutagenesisi84 – 841D → S: Destabilization of dimer and loss of zinc binding; when associated with S-81. 2 Publications
Mutagenesisi112 – 1121C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147. 2 Publications
Mutagenesisi123 – 1231K → A: Deacreased succinylation. 1 Publication
Mutagenesisi123 – 1231K → E: Mimicks constitutive succinylation state; decreased activity. 1 Publication
Mutagenesisi134 – 1341E → Q: Abolishes dimerization; when associated with E-50 and E-51. 1 Publication
Mutagenesisi147 – 1471C → A: Exhibits very slow copper acquisition. 3 Publications
Mutagenesisi147 – 1471C → S: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112. 3 Publications

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

MIMi105400. phenotype.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA334.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 154153Superoxide dismutase [Cu-Zn]PRO_0000164057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei4 – 41N6-succinyllysineBy similarity
Lipidationi7 – 71S-palmitoyl cysteine1 Publication
Modified residuei10 – 101N6-succinyllysineBy similarity
Cross-linki33 – 331-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)
Disulfide bondi58 ↔ 1474 Publications
Modified residuei92 – 921N6-succinyllysineBy similarity
Modified residuei99 – 991Phosphoserine2 Publications
Modified residuei123 – 1231N6-acetyllysine; alternate1 Publication
Modified residuei123 – 1231N6-succinyllysine; alternate1 Publication
Modified residuei137 – 1371N6-acetyllysine; alternateBy similarity
Modified residuei137 – 1371N6-succinyllysine; alternateBy similarity

Post-translational modificationi

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.2 Publications
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.1 Publication
Succinylation, adjacent to copper catalytic site probably inhibit activity. Desuccinylated by SIRT5, enhancing activity.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP00441.
PaxDbiP00441.
PeptideAtlasiP00441.
PRIDEiP00441.

2D gel databases

DOSAC-COBS-2DPAGEP00441.
OGPiP00441.
REPRODUCTION-2DPAGEIPI00783680.
SWISS-2DPAGEP00441.
UCD-2DPAGEP00441.

PTM databases

PhosphoSiteiP00441.

Expressioni

Gene expression databases

BgeeiP00441.
CleanExiHS_SOD1.
ExpressionAtlasiP00441. baseline and differential.
GenevestigatoriP00441.

Organism-specific databases

HPAiCAB008670.
HPA001401.

Interactioni

Subunit structurei

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.10 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112530. 46 interactions.
DIPiDIP-44941N.
IntActiP00441. 13 interactions.
MINTiMINT-204523.
STRINGi9606.ENSP00000270142.

Structurei

Secondary structure

1
154
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108
Beta strandi12 – 143
Beta strandi16 – 2510
Beta strandi26 – 283
Beta strandi30 – 389
Beta strandi41 – 5010
Helixi54 – 563
Helixi58 – 614
Beta strandi63 – 653
Beta strandi67 – 693
Beta strandi74 – 763
Beta strandi77 – 793
Beta strandi84 – 907
Helixi92 – 943
Beta strandi96 – 1049
Beta strandi106 – 1083
Helixi109 – 1113
Beta strandi112 – 1154
Beta strandi116 – 1238
Beta strandi127 – 1293
Beta strandi130 – 1323
Helixi133 – 1364
Turni138 – 1403
Beta strandi143 – 1497
Beta strandi151 – 1533

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4MCMX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L2-154[»]
4MCNX-ray2.60A/B2-154[»]
4NINX-ray1.40A102-108[»]
4NIOX-ray1.30A148-154[»]
4NIPX-ray1.90A148-154[»]
4SODmodel-A1-154[»]
DisProtiDP00652.
ProteinModelPortaliP00441.
SMRiP00441. Positions 2-154.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00441.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiCOG2032.
HOVERGENiHBG000062.
InParanoidiP00441.
KOiK04565.
OMAiNDPNAKR.
OrthoDBiEOG776SR4.
PhylomeDBiP00441.
TreeFamiTF105131.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00441-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE
60 70 80 90 100
FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI
110 120 130 140 150
EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVI

GIAQ
Length:154
Mass (Da):15,936
Last modified:January 23, 2007 - v2
Checksum:i25CA38DA8D564483
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181I → S no nucleotide entry (PubMed:3889846)Curated
Sequence conflicti99 – 991S → V no nucleotide entry (PubMed:3889846)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51A → S in ALS1.
VAR_013518
Natural varianti5 – 51A → T in ALS1. 1 Publication
VAR_007130
Natural varianti5 – 51A → V in ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates.
VAR_007131
Natural varianti7 – 71C → F in ALS1. 1 Publication
VAR_008717
Natural varianti8 – 81V → E in ALS1. 1 Publication
VAR_007132
Natural varianti9 – 91L → Q in ALS1. 1 Publication
VAR_013519
Natural varianti9 – 91L → V in ALS1. 1 Publication
VAR_013520
Natural varianti13 – 131G → R in ALS1. 1 Publication
VAR_013521
Natural varianti15 – 151V → G in ALS1.
VAR_013522
Natural varianti15 – 151V → M in ALS1. 1 Publication
VAR_007133
Natural varianti17 – 171G → S in ALS1; sporadic young onset. 1 Publication
VAR_007134
Natural varianti21 – 211F → C in ALS1. 1 Publication
VAR_045876
Natural varianti22 – 221E → G in ALS1.
VAR_013523
Natural varianti22 – 221E → K in ALS1. 1 Publication
VAR_007135
Natural varianti23 – 231Q → L in ALS1. 1 Publication
VAR_045877
Natural varianti38 – 381G → R in ALS1; mild form; ubiquitinated by RNF19A. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1.
VAR_007136
Natural varianti39 – 391L → R in ALS1.
VAR_013524
Natural varianti39 – 391L → V in ALS1.
VAR_007137
Natural varianti42 – 421G → D in ALS1.
VAR_007139
Natural varianti42 – 421G → S in ALS1.
VAR_007138
Natural varianti44 – 441H → R in ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates.
VAR_007140
Natural varianti46 – 461F → C in ALS1; slow progression. 1 Publication
VAR_013525
Natural varianti47 – 471H → R in ALS1; "benign" form; 80% of wild-type activity; ubiquitinated by RNF19A. 1 Publication
VAR_007141
Natural varianti49 – 491H → Q in ALS1. 1 Publication
VAR_007142
Natural varianti49 – 491H → R in ALS1. 1 Publication
VAR_045878
Natural varianti50 – 501E → K in ALS1.
VAR_013526
Natural varianti55 – 551T → R in ALS1; reduces tendency to form fibrillar aggregates. 1 Publication
VAR_045879
Natural varianti66 – 661N → S in ALS1.
VAR_013527
Natural varianti68 – 681L → P in ALS1. 1 Publication
VAR_065560
Natural varianti68 – 681L → R in ALS1.
VAR_013528
Natural varianti73 – 731G → S in ALS1. 1 Publication
VAR_008718
Natural varianti77 – 771D → Y in ALS1.
VAR_013529
Natural varianti81 – 811H → A in ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions. 1 Publication
VAR_016874
Natural varianti85 – 851L → F in ALS1.
VAR_013530
Natural varianti85 – 851L → V in ALS1. 1 Publication
VAR_007143
Natural varianti86 – 861G → R in ALS1; ubiquitinated by RNF19A; interferes with zinc-binding. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1.
VAR_007144
Natural varianti87 – 871N → S in ALS1.
Corresponds to variant rs11556620 [ dbSNP | Ensembl ].
VAR_013531
Natural varianti88 – 881V → A in ALS1. 1 Publication
VAR_045880
Natural varianti90 – 901A → T in ALS1. 1 Publication
VAR_045881
Natural varianti90 – 901A → V in ALS1.
VAR_013532
Natural varianti91 – 911D → A in ALS1; does not seem to be linked with a decrease in activity. 2 Publications
Corresponds to variant rs80265967 [ dbSNP | Ensembl ].
VAR_007145
Natural varianti91 – 911D → V in ALS1.
VAR_013533
Natural varianti94 – 941G → A in ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A.
VAR_007146
Natural varianti94 – 941G → C in ALS1.
VAR_007147
Natural varianti94 – 941G → D in ALS1. 1 Publication
VAR_007148
Natural varianti94 – 941G → R in ALS1; 30% of wild-type activity. 2 Publications
VAR_007149
Natural varianti94 – 941G → V in ALS1. 1 Publication
VAR_008719
Natural varianti96 – 961A → G in ALS1. 1 Publication
VAR_065194
Natural varianti98 – 981V → M in ALS1; increases tendency to form fibrillar aggregates. 1 Publication
VAR_045882
Natural varianti101 – 1011E → G in ALS1.
VAR_007150
Natural varianti101 – 1011E → K in ALS1.
VAR_013534
Natural varianti102 – 1021D → G in ALS1. 1 Publication
VAR_007151
Natural varianti102 – 1021D → N in ALS1. 1 Publication
VAR_007152
Natural varianti105 – 1051I → F in ALS1. 1 Publication
VAR_008720
Natural varianti106 – 1061S → L in ALS1.
VAR_013535
Natural varianti107 – 1071L → V in ALS1.
VAR_007153
Natural varianti109 – 1091G → V in ALS1.
VAR_013536
Natural varianti113 – 1131I → M in ALS1.
VAR_013537
Natural varianti113 – 1131I → T in ALS1. 2 Publications
VAR_007154
Natural varianti114 – 1141I → T in ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates. 3 Publications
VAR_007155
Natural varianti115 – 1151G → A in ALS1.
VAR_013538
Natural varianti116 – 1161R → G in ALS1. 1 Publication
VAR_007156
Natural varianti119 – 1191V → L in ALS1. 1 Publication
VAR_045883
Natural varianti119 – 1191V → VFLQ in ALS1.
VAR_008721
Natural varianti125 – 1251D → G in ALS1. 1 Publication
VAR_045884
Natural varianti125 – 1251D → V in ALS1. 1 Publication
VAR_008722
Natural varianti126 – 1261D → H in ALS1. 1 Publication
VAR_007157
Natural varianti127 – 1271L → S in ALS1. 1 Publication
VAR_013539
Natural varianti134 – 1341Missing in ALS. 1 Publication
VAR_008723
Natural varianti135 – 1351S → N in ALS1; reduced metal binding; increases tendency to form fibrillar aggregates. 1 Publication
VAR_007158
Natural varianti140 – 1401N → K in ALS1.
VAR_007159
Natural varianti145 – 1451L → F in ALS1.
VAR_007160
Natural varianti145 – 1451L → S in ALS1. 1 Publication
VAR_008724
Natural varianti146 – 1461A → T in ALS1. 1 Publication
VAR_008725
Natural varianti147 – 1471C → R in ALS1.
VAR_013540
Natural varianti148 – 1481G → R in ALS1. 1 Publication
VAR_045885
Natural varianti149 – 1491V → G in ALS1.
VAR_007161
Natural varianti149 – 1491V → I in ALS1. 1 Publication
VAR_007162
Natural varianti150 – 1501I → T in ALS1. 1 Publication
VAR_007163
Natural varianti152 – 1521I → T in ALS1; seems to affect formation of homodimer. 1 Publication
VAR_007164

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L44139
, L44135, L44136, L44137 Genomic DNA. Translation: AAB05662.1.
L44139
, L44135, L44136, L44137 Genomic DNA. Translation: AAB05661.1.
X02317 mRNA. Translation: CAA26182.1.
X01780 Genomic DNA. Translation: CAA25915.1.
X01781 Genomic DNA. Translation: CAA25916.1.
X01782 Genomic DNA. Translation: CAA25917.1. Sequence problems.
X01783 Genomic DNA. Translation: CAA25918.1.
X01784 Genomic DNA. Translation: CAA25919.1. Sequence problems.
AY049787 mRNA. Translation: AAL15444.1.
AY450286 mRNA. Translation: AAR21563.1.
EF151142 mRNA. Translation: ABL96616.1.
AK312116 mRNA. Translation: BAG35052.1.
CR450355 mRNA. Translation: CAG29351.1.
CR541742 mRNA. Translation: CAG46542.1.
BT006676 mRNA. Translation: AAP35322.1.
AY835629 Genomic DNA. Translation: AAV80422.1.
AP000253 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09889.1.
CH471079 Genomic DNA. Translation: EAX09890.1.
BC001034 mRNA. Translation: AAH01034.1.
L46374 Genomic DNA. Translation: AAB59626.1.
L46375 Genomic DNA. Translation: AAB59627.1.
L44746 Genomic DNA. Translation: AAC41773.1. Sequence problems.
X95228 Genomic DNA. Translation: CAA64520.1.
CCDSiCCDS33536.1.
PIRiA22703. DSHUCZ.
RefSeqiNP_000445.1. NM_000454.4.
UniGeneiHs.443914.

Genome annotation databases

EnsembliENST00000270142; ENSP00000270142; ENSG00000142168.
GeneIDi6647.
KEGGihsa:6647.
UCSCiuc002ypa.3. human.

Cross-referencesi

Web resourcesi

Alsod

ALS genetic mutations db

NIEHS-SNPs
Wikipedia

Superoxide dismutase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L44139
, L44135 , L44136 , L44137 Genomic DNA. Translation: AAB05662.1 .
L44139
, L44135 , L44136 , L44137 Genomic DNA. Translation: AAB05661.1 .
X02317 mRNA. Translation: CAA26182.1 .
X01780 Genomic DNA. Translation: CAA25915.1 .
X01781 Genomic DNA. Translation: CAA25916.1 .
X01782 Genomic DNA. Translation: CAA25917.1 . Sequence problems.
X01783 Genomic DNA. Translation: CAA25918.1 .
X01784 Genomic DNA. Translation: CAA25919.1 . Sequence problems.
AY049787 mRNA. Translation: AAL15444.1 .
AY450286 mRNA. Translation: AAR21563.1 .
EF151142 mRNA. Translation: ABL96616.1 .
AK312116 mRNA. Translation: BAG35052.1 .
CR450355 mRNA. Translation: CAG29351.1 .
CR541742 mRNA. Translation: CAG46542.1 .
BT006676 mRNA. Translation: AAP35322.1 .
AY835629 Genomic DNA. Translation: AAV80422.1 .
AP000253 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09889.1 .
CH471079 Genomic DNA. Translation: EAX09890.1 .
BC001034 mRNA. Translation: AAH01034.1 .
L46374 Genomic DNA. Translation: AAB59626.1 .
L46375 Genomic DNA. Translation: AAB59627.1 .
L44746 Genomic DNA. Translation: AAC41773.1 . Sequence problems.
X95228 Genomic DNA. Translation: CAA64520.1 .
CCDSi CCDS33536.1.
PIRi A22703. DSHUCZ.
RefSeqi NP_000445.1. NM_000454.4.
UniGenei Hs.443914.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2-154 [» ]
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 2-154 [» ]
1L3N NMR - A/B 2-154 [» ]
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 2-154 [» ]
1PTZ X-ray 1.80 A/B 2-154 [» ]
1PU0 X-ray 1.70 A/B/C/D/E/F/G/H/I/J 2-154 [» ]
1RK7 NMR - A 2-154 [» ]
1SOS X-ray 2.50 A/B/C/D/E/F/G/H/I/J 2-154 [» ]
1SPD X-ray 2.40 A/B 2-154 [» ]
1UXL X-ray 1.60 A/B/C/D/E/F/G/H/I/J 2-154 [» ]
1UXM X-ray 1.90 A/B/C/D/E/F/G/H/I/J/K/L 2-154 [» ]
2AF2 NMR - A/B 2-154 [» ]
2C9S X-ray 1.24 A/F 2-154 [» ]
2C9U X-ray 1.24 A/F 2-154 [» ]
2C9V X-ray 1.07 A/F 2-154 [» ]
2GBT X-ray 1.70 A/B/C/D 2-154 [» ]
2GBU X-ray 2.00 A/B/C/D 2-154 [» ]
2GBV X-ray 2.00 A/B/C/D/E/F/G/H/I/J 2-154 [» ]
2LU5 NMR - A 2-154 [» ]
2NNX X-ray 2.30 A/B/C/D 2-154 [» ]
2R27 X-ray 2.00 A/B 1-154 [» ]
2V0A X-ray 1.15 A/F 2-154 [» ]
2VR6 X-ray 1.30 A/F 2-154 [» ]
2VR7 X-ray 1.58 A/F 2-154 [» ]
2VR8 X-ray 1.36 A/F 2-154 [» ]
2WKO X-ray 1.97 A/F 2-154 [» ]
2WYT X-ray 1.00 A/F 2-154 [» ]
2WYZ X-ray 1.70 A/F 2-154 [» ]
2WZ0 X-ray 1.72 A/F 2-154 [» ]
2WZ5 X-ray 1.50 A/F 2-154 [» ]
2WZ6 X-ray 1.55 A/F 2-154 [» ]
2XJK X-ray 1.45 A 2-154 [» ]
2XJL X-ray 1.55 A 2-154 [» ]
2ZKW X-ray 1.90 A/B 1-154 [» ]
2ZKX X-ray 2.72 A/B/C/D 1-154 [» ]
2ZKY X-ray 2.40 A/B/C/D/E/F/G/H/I/J 1-154 [» ]
3CQP X-ray 1.95 A/B/C/D 2-154 [» ]
3CQQ X-ray 1.90 A/B 2-154 [» ]
3ECU X-ray 1.90 A/B/C/D 2-154 [» ]
3ECV X-ray 1.90 A/B/C/D 2-154 [» ]
3ECW X-ray 2.15 A/B/C/D 2-154 [» ]
3GQF X-ray 2.20 A/B/C/D/E/F 2-154 [» ]
3GTV X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L 2-81 [» ]
3GZO X-ray 2.10 A/B/C/D/E/F/G/H/I/J 2-154 [» ]
3GZP X-ray 3.10 A/B/C/D 2-154 [» ]
3GZQ X-ray 1.40 A/B 2-154 [» ]
3H2P X-ray 1.55 A/B 2-154 [» ]
3H2Q X-ray 1.85 A/B/C/D 2-154 [» ]
3HFF X-ray 2.20 A 2-154 [» ]
3K91 X-ray 1.75 A/B 2-154 [» ]
3KH3 X-ray 3.50 A/B/C/D/E/F/G/H/I/J/K/L 2-154 [» ]
3KH4 X-ray 3.50 A/B/C/D/E/F 2-154 [» ]
3LTV X-ray 2.45 A/B/C/D/E/F 4-154 [» ]
3QQD X-ray 1.65 A/B 2-154 [» ]
3RE0 X-ray 2.28 A/B/C/D 2-154 [» ]
3T5W X-ray 1.80 A/B/D/E/F/G/H/I/J/K/L/M 2-154 [» ]
4A7G X-ray 1.24 A/F 2-154 [» ]
4A7Q X-ray 1.22 A/F 2-154 [» ]
4A7S X-ray 1.06 A/F 2-154 [» ]
4A7T X-ray 1.45 A/F 2-154 [» ]
4A7U X-ray 0.98 A/F 2-154 [» ]
4A7V X-ray 1.00 A/F 2-154 [» ]
4B3E X-ray 2.15 A/B/C/D/E/F/G/H/I/J 1-154 [» ]
4BCY X-ray 1.27 A 2-154 [» ]
4BCZ X-ray 1.93 A/B 2-49 [» ]
A/B 83-124 [» ]
A/B 141-154 [» ]
4BD4 X-ray 2.78 A/B/C/D/E/F/G/H/I 2-49 [» ]
A/B/C/D/E/F/G/H/I 83-124 [» ]
A/B/C/D/E/F/G/H/I 141-154 [» ]
4FF9 X-ray 2.50 A/B 2-154 [» ]
4MCM X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L 2-154 [» ]
4MCN X-ray 2.60 A/B 2-154 [» ]
4NIN X-ray 1.40 A 102-108 [» ]
4NIO X-ray 1.30 A 148-154 [» ]
4NIP X-ray 1.90 A 148-154 [» ]
4SOD model - A 1-154 [» ]
DisProti DP00652.
ProteinModelPortali P00441.
SMRi P00441. Positions 2-154.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112530. 46 interactions.
DIPi DIP-44941N.
IntActi P00441. 13 interactions.
MINTi MINT-204523.
STRINGi 9606.ENSP00000270142.

Chemistry

BindingDBi P00441.
ChEMBLi CHEMBL2354.
DrugBanki DB00958. Carboplatin.
DB00515. Cisplatin.
DB00526. Oxaliplatin.
DB00163. Vitamin E.

PTM databases

PhosphoSitei P00441.

2D gel databases

DOSAC-COBS-2DPAGE P00441.
OGPi P00441.
REPRODUCTION-2DPAGE IPI00783680.
SWISS-2DPAGE P00441.
UCD-2DPAGE P00441.

Proteomic databases

MaxQBi P00441.
PaxDbi P00441.
PeptideAtlasi P00441.
PRIDEi P00441.

Protocols and materials databases

DNASUi 6647.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000270142 ; ENSP00000270142 ; ENSG00000142168 .
GeneIDi 6647.
KEGGi hsa:6647.
UCSCi uc002ypa.3. human.

Organism-specific databases

CTDi 6647.
GeneCardsi GC21P033031.
GeneReviewsi SOD1.
HGNCi HGNC:11179. SOD1.
HPAi CAB008670.
HPA001401.
MIMi 105400. phenotype.
147450. gene.
neXtProti NX_P00441.
Orphaneti 803. Amyotrophic lateral sclerosis.
PharmGKBi PA334.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2032.
HOVERGENi HBG000062.
InParanoidi P00441.
KOi K04565.
OMAi NDPNAKR.
OrthoDBi EOG776SR4.
PhylomeDBi P00441.
TreeFami TF105131.

Enzyme and pathway databases

Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSi SOD1. human.
EvolutionaryTracei P00441.
GeneWikii SOD1.
GenomeRNAii 6647.
NextBioi 25903.
PROi P00441.
SOURCEi Search...

Gene expression databases

Bgeei P00441.
CleanExi HS_SOD1.
ExpressionAtlasi P00441. baseline and differential.
Genevestigatori P00441.

Family and domain databases

Gene3Di 2.60.40.200. 1 hit.
InterProi IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view ]
Pfami PF00080. Sod_Cu. 1 hit.
[Graphical view ]
PRINTSi PR00068. CUZNDISMTASE.
SUPFAMi SSF49329. SSF49329. 1 hit.
PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA."
    Sherman L., Dafni N., Lieman-Hurwitz J., Groner Y.
    Proc. Natl. Acad. Sci. U.S.A. 80:5465-5469(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase."
    Levanon D., Lieman-Hurwitz J., Dafni N., Wigderson M., Sherman L., Bernstein Y., Laver-Rudich Z., Danciger E., Stein O., Groner Y.
    EMBO J. 4:77-84(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising high levels of active or inactive enzyme from an expression library."
    Hallewell R.A., Masiarz F.R., Najarian R.C., Puma J.P., Quiroga M.R., Randolph A., Sanchez-Pescador R., Scandella C.J., Smith B., Steimer K.S., Mullenbach G.T.
    Nucleic Acids Res. 13:2017-2034(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Comparison of properties between human recombinant and placental copper-zinc SOD."
    Kajihara J., Enomoto M., Nishijima K., Yabuuchi M., Katoh K.
    J. Biochem. 104:851-854(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. Xu Y., Hu X., Zhou Y., Peng X., Yuan J., Qiang B.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. Lu X., Hui L.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. "Direct sequencing and cloning of superoxide dismutase 1 from peripheral blood."
    Staege M.S., Bergmann S., Heins S.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  10. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  11. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  12. NIEHS SNPs program
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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.
    , 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. 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. 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
  47. Cited for: VARIANTS ALS1.
  48. Erratum
    Rosen D.R.
    Nature 364:362-362(1993) [PubMed] [Europe PMC] [Abstract]
  49. 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. 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.,