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P00441

- SODC_HUMAN

UniProt

P00441 - SODC_HUMAN

Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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 binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein phosphatase 2B binding Source: UniProtKB
    7. Rac GTPase binding Source: UniProtKB
    8. superoxide dismutase activity Source: UniProtKB
    9. 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

    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: UniProt
    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

    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.
    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

    ArrayExpressiP00441.
    BgeeiP00441.
    CleanExiHS_SOD1.
    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. 44 interactions.
    DIPiDIP-44941N.
    IntActiP00441. 12 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[»]
    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

    MATKAVCVLK GDGPVQGIIN FEQKESNGPV KVWGSIKGLT EGLHGFHVHE    50
    FGDNTAGCTS AGPHFNPLSR KHGGPKDEER HVGDLGNVTA DKDGVADVSI 100
    EDSVISLSGD HCIIGRTLVV HEKADDLGKG GNEESTKTGN AGSRLACGVI 150
    GIAQ 154
    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 [» ]
    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. 44 interactions.
    DIPi DIP-44941N.
    IntActi P00441. 12 interactions.
    MINTi MINT-204523.
    STRINGi 9606.ENSP00000270142.

    Chemistry

    BindingDBi P00441.
    ChEMBLi CHEMBL2354.

    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

    ArrayExpressi P00441.
    Bgeei P00441.
    CleanExi HS_SOD1.
    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

    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., 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.,