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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:

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

  • chaperone binding Source: UniProtKB
  • copper ion binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase 2B binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB
  • superoxide dismutase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi1.15.1.1. 2681.
ReactomeiREACT_264249. Detoxification of Reactive Oxygen Species.
REACT_318. Platelet degranulation.

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 Componenti: 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

  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite cytoplasm Source: UniProtKB
  • dense core granule Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • lysosome Source: Ensembl
  • mitochondrial intermembrane space Source: Reactome
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • peroxisome Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Amyotrophic lateral sclerosis 1 (ALS1)35 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:105400
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. 3 Publications
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. 4 Publications
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. 1 Publication
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. 4 Publications
VAR_007141
Natural varianti49 – 491H → Q in ALS1. 2 Publications
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. 2 Publications
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. 6 Publications
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. 3 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. 3 Publications
VAR_007146
Natural varianti94 – 941G → C in ALS1.
VAR_007147
Natural varianti94 – 941G → D in ALS1. 2 Publications
VAR_007148
Natural varianti94 – 941G → R in ALS1; 30% of wild-type activity. 3 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. 2 Publications
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. 5 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. 2 Publications
VAR_007158
Natural varianti140 – 1401N → K in ALS1.
VAR_007159
Natural varianti145 – 1451L → F in ALS1. 1 Publication
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. 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.

Chemistry

DrugBankiDB00958. Carboplatin.
DB00515. Cisplatin.
DB00526. Oxaliplatin.
DB00163. Vitamin E.

Polymorphism and mutation databases

BioMutaiSOD1.

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)1 Publication
Disulfide bondi58 ↔ 1474 Publications
Modified residuei92 – 921N6-succinyllysineBy similarity
Modified residuei99 – 991Phosphoserine3 Publications
Modified residuei103 – 1031Phosphoserine1 Publication
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.1 Publication
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

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.
GenevisibleiP00441. HS.

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. 53 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 – 108Combined sources
Beta strandi12 – 143Combined sources
Beta strandi16 – 2510Combined sources
Beta strandi26 – 283Combined sources
Beta strandi30 – 389Combined sources
Beta strandi41 – 5010Combined sources
Helixi54 – 563Combined sources
Helixi58 – 614Combined sources
Beta strandi63 – 653Combined sources
Beta strandi67 – 693Combined sources
Beta strandi74 – 763Combined sources
Beta strandi77 – 793Combined sources
Beta strandi84 – 907Combined sources
Helixi92 – 943Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi106 – 1083Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi130 – 1323Combined sources
Helixi133 – 1364Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 1497Combined sources
Beta strandi151 – 1533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
2MP3NMR-A2-126[»]
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[»]
4OH2X-ray2.38A/B/C/D/E/F/G/H/I/J2-154[»]
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.
GeneTreeiENSGT00530000063226.
HOVERGENiHBG000062.
InParanoidiP00441.
KOiK04565.
OMAiVCVLKGT.
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

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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. 3 Publications
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. 4 Publications
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. 1 Publication
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. 4 Publications
VAR_007141
Natural varianti49 – 491H → Q in ALS1. 2 Publications
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. 2 Publications
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. 6 Publications
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. 3 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. 3 Publications
VAR_007146
Natural varianti94 – 941G → C in ALS1.
VAR_007147
Natural varianti94 – 941G → D in ALS1. 2 Publications
VAR_007148
Natural varianti94 – 941G → R in ALS1; 30% of wild-type activity. 3 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. 2 Publications
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. 5 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. 2 Publications
VAR_007158
Natural varianti140 – 1401N → K in ALS1.
VAR_007159
Natural varianti145 – 1451L → F in ALS1. 1 Publication
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. 1 Publication
VAR_007164

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
2MP3NMR-A2-126[»]
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[»]
3K91</